|
Enzyme 1
[top]
|
| Enzyme 1 ID |
6214 |
| Enzyme 1 Name |
Nitric oxide synthase, inducible |
| Enzyme 1 Synonyms |
- NOS type II
- Inducible NO synthase
- Inducible NOS
- iNOS
- Hepatocyte NOS
- HEP- NOS
|
| Enzyme 1 Gene Name |
NOS2A |
| Enzyme 1 Protein Sequence |
>Nitric oxide synthase, inducible
MACPWKFLFKTKFHQYAMNGEKDINNNVEKAPCATSSPVTQDDLQYHNLSKQQNESPQPL
VETGKKSPESLVKLDATPLSSPRHVRIKNWGSGMTFQDTLHHKAKGILTCRSKSCLGSIM
TPKSLTRGPRDKPTPPDELLPQAIEFVNQYYGSFKEAKIEEHLARVEAVTKEIETTGTYQ
LTGDELIFATKQAWRNAPRCIGRIQWSNLQVFDARSCSTAREMFEHICRHVRYSTNNGNI
RSAITVFPQRSDGKHDFRVWNAQLIRYAGYQMPDGSIRGDPANVEFTQLCIDLGWKPKYG
RFDVVPLVLQANGRDPELFEIPPDLVLEVAMEHPKYEWFRELELKWYALPAVANMLLEVG
GLEFPGCPFNGWYMGTEIGVRDFCDVQRYNILEEVGRRMGLETHKLASLWKDQAVVEINI
AVLHSFQKQNVTIMDHHSAAESFMKYMQNEYRSRGGCPADWIWLVPPMSGSITPVFHQEM
LNYVLSPFYYYQVEAWKTHVWQDEKRRPKRREIPLKVLVKAVLFACMLMRKTMASRVRVT
ILFATETGKSEALAWDLGALFSCAFNPKVVCMDKYRLSCLEEERLLLVVTSTFGNGDCPG
NGEKLKKSLFMLKELNNKFRYAVFGLGSSMYPRFCAFAHDIDQKLSHLGASQLTPMGEGD
ELSGQEDAFRSWAVQTFKAACETFDVRGKQHIQIPKLYTSNVTWDPHHYRLVQDSQPLDL
SKALSSMHAKNVFTMRLKSRQNLQSPTSSRATILVELSCEDGQGLNYLPGEHLGVCPGNQ
PALVQGILERVVDGPTPHQTVRLEALDESGSYWVSDKRLPPCSLSQALTYFLDITTPPTQ
LLLQKLAQVATEEPERQRLEALCQPSEYSKWKFTNSPTFLEVLEEFPSLRVSAGFLLSQL
PILKPRFYSISSSRDHTPTEIHLTVAVVTYHTRDGQGPLHHGVCSTWLNSLKPQDPVPCF
VRNASGFHLPEDPSHPCILIGPGTGIAPFRSFWQQRLHDSQHKGVRGGRMTLVFGCRRPD
EDHIYQEEMLEMAQKGVLHAVHTAYSRLPGKPKVYVQDILRQQLASEVLRVLHKEPGHLY
VCGDVRMARDVAHTLKQLVAAKLKLNEEQVEDYFFQLKSQKRYHEDIFGAVFPYEAKKDR
VAVQPSSLEMSAL
|
| Enzyme 1 Number of Residues |
1153 |
| Enzyme 1 Molecular Weight |
131119 |
| Enzyme 1 Theoretical pI |
8.01 |
| Enzyme 1 GO Classification |
| Function |
- FAD binding
- FMN binding
- NADP binding
- adenyl nucleotide binding
- binding
- calmodulin binding
- catalytic activity
- cation binding
- coenzyme binding
- cofactor binding
- electron transporter activity
- heme binding
- ion binding
- iron ion binding
- monooxygenase activity
- nitric-oxide synthase activity
- nucleotide binding
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD or NADH as one donor, and incorporation of one atom of oxygen
- protein binding
- purine nucleotide binding
- tetrapyrrole binding
- transition metal ion binding
- transporter activity
|
| Process |
- biosynthesis
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- nitric oxide biosynthesis
- physiological process
|
| Component |
| — |
|
| Enzyme 1 General Function |
Inorganic ion transport and metabolism |
| Enzyme 1 Specific Function |
Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In macrophages, NO mediates tumoricidal and bactericidal actions |
| Enzyme 1 Pathways |
- Arginine and Proline Metabolism (map00330
)
|
| Enzyme 1 Reactions |
- L-arginine + n NADPH + n H+ + m O2 = citrulline + nitric oxide + n NADP+
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
292242  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
P35228  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
NOS2A_HUMAN  |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>3462 bp
ATGGCCTGTCCTTGGAAATTTCTGTTCAAGACCAAATTCCACCAGTATGCAATGAATGGG
GAAAAAGACATCAACAACAATGTGGAGAAAGCCCCCTGTGCCACCTCCAGTCCAGTGACA
CAGGATGACCTTCAGTATCACAACCTCAGCAAGCAGCAGAATGAGTCCCCGCAGCCCCTC
GTGGAGACGGGAAAGAAGTCTCCAGAATCTCTGGTCAAGCTGGATGCAACCCCATTGTCC
TCCCCACGGCATGTGAGGATCAAAAACTGGGGCAGCGGGATGACTTTCCAAGACACACTT
CACCATAAGGCCAAAGGGATTTTAACTTGCAGGTCCAAATCTTGCCTGGGGTCCATTATG
ACTCCCAAAAGTTTGACCAGAGGACCCAGGGACAAGCCTACCCCTCCAGATGAGCTTCTA
CCTCAAGCTATCGAATTTGTCAACCAATATTACGGCTCCTTCAAAGAGGCAAAAATAGAG
GAACATCTGGCCAGGGTGGAAGCGGTAACAAAGGAGATAGAAACAACAGGAACCTACCAA
CTGACGGGAGATGAGCTCATCTTCGCCACCAAGCAGGCCTGGCGCAATGCCCCACGCTGC
ATTGGGAGGATCCAGTGGTCCAACCTGCAGGTCTTCGATGCCCGCAGCTGTTCCACTGCC
CGGGAAATGTTTGAACACATCTGCAGACACGTGCGTTACTCCACCAACAATGGCAACATC
AGGTCGGCCATCACCGTGTTCCCCCAGCGGAGTGATGGCAAGCACGACTTCCGGGTGTGG
AATGCTCAGCTCATCCGCTATGCTGGCTACCAGATGCCAGATGGCAGCATCAGAGGGGAC
CCTGCCAACGTGGAATTCACTCAGCTGTGCATCGACCTGGGCTGGAAGCCCAAGTACGGC
CGCTTCGATGTGGTCCCCCTGGTCCTGCAGGCCAATGGCCGTGACCCTGAGCTCTTCGAA
ATCCCACCTGACCTTGTGCTTGAGGTGGCCATGGAACATCCCAAATACGAGTGGTTTCGG
GAACTGGAGCTAAAGTGGTACGCCCTGCCTGCAGTGGCCAACATGCTGCTTGAGGTGGGC
GGCCTGGAGTTCCCAGGGTGCCCCTTCAATGGCTGGTACATGGGCACAGAGATCGGAGTC
CGGGACTTCTGTGACGTCCAGCGCTACAACATCCTGGAGGAAGTGGGCAGGAGAATGGGC
CTGGAAACGCACAAGCTGGCCTCGCTCTGGAAAGACCAGGCTGTCGTTGAGATCAACATT
GCTGTGATCCATAGTTTTCAGAAGCAGAATGTGACCATCATGGACCACCACTCGGCTGCA
GAATCCTTCATGAAGTACATGCAGAATGAATACCGGTCCCGTGGGGGCTGCCCGGCAGAC
TGGATTTGGCTGGTCCCTCCCATGTCTGGGAGCATCACCCCCGTGTTTCACCAGGAGATG
CTGAACTACGTCCTGTCCCCTTTCTACTACTATCAGGTAGAGGCCTGGAAAACCCATGTC
TGGCAGGACGAGAAGCGGAGACCCAAGAGAAGAGAGATTCCATTGAAAGTCTTGGTCAAA
GCTGTGCTCTTTGCCTGTATGCTGATGCGCAAGACAATGGCGTCCCGAGTCAGAGTCACC
ATCCTCTTTGCGACAGAGACAGGAAAATCAGAGGCGCTGGCCTGGGACCTGGGGGCCTTA
TTCAGCTGTGCCTTCAACCCCAAGGTTGTCTGCATGGATAAGTACAGGCTGAGCTGCCTG
GAGGAGGAACGGCTGCTGTTGGTGGTGACCAGTACGTTTGGCAATGGAGACTGCCCTGGC
AATGGAGAGAAACTGAAGAAATCGCTCTTCATGCTGAAAGAGCTCAACAACAAATTCAGG
TACGCTGTGTTTGGCCTCGGCTCCAGCATGTACCCTCGGTTCTGCGCCTTTGCTCATGAC
ATTGATCAGAAGCTGTCCCACCTGGGGGCCTCTCAGCTCACCCCGATGGGAGAAGGGGAT
GAGCTCAGTGGGCAGGAGGACGCCTTCCGCAGCTGGGCCGTGCAAACCTTCAAGGCAGCC
TGTGAGACGTTTGATGTCCGAGGCAAACAGCACATTCAGATCCCCAAGCTCTACACCTCC
AATGTGACCTGGGACCCGCACCACTACAGGCTCGTGCAGGACTCACAGCCTTTGGACCTC
AGCAAAGCCCTCAGCAGCATGCATGCCAAGAACGTGTTCACCATGAGGCTCAAATCTCGG
CAGAATCTACAAAGTCCGACATCCAGCCGTGCCACCATCCTGGTGGAACTCTCCTGTGAG
GATGGCCAAGGCCTGAACTACCTGCCGGGGGAGCACCTTGGGGTTTGCCCAGGCAACCAG
CCGGCCCTGGTCCAAGGCATCCTGGAGCGAGTGGTGGATGGCCCCACACCCCACCAGACA
GTGCGCCTGGAGGACCTGGATGAGAGTGGCAGCTACTGGGTCAGTGACAAGAGGCTGCCC
CCCTGCTCACTCAGCCAGGCCCTCACCTACTCCCCGGACATCACCACACCCCCAACCCAG
CTGCTGCTCCAAAAGCTGGCCCAGGTGGCCACAGAAGAGCCTGAGAGACAGAGGCTGGAG
GCCCTGTGCCAGCCCTCAGAGTACAGCAAGTGGAAGTTCACCAACAGCCCCACATTCCTG
GAGGTGCTAGAGGAGTTCCCGTCCCTGCGGGTGTCTGCTGGCTTCCTGCTTTCCCAGCTC
CCCATTCTGAAGCCCAGGTTCTACTCCATCAGCTCCTCCCGGGATCACACGCCCACGGAG
ATCCACCTGACTGTGGCCGTGGTCACCTACCACACCGGAGATGGCCAGGGTCCCCTGCAC
CACGGTGTCTGCAGCACATGGCTCAACAGCCTGAAGCCCCAAGACCCAGTGCCCTGCTTT
GTGCGGAATGCCAGCGCCTTCCACCTCCCCGAGGATCCCTCCCATCCTTGCATCCTCATC
GGGCCTGGCACAGGCATCGTGCCCTTCCGCAGTTTCTGGCAGCAACGGCTCCATGACTCC
CAGCACAAGGGAGTGCGGGGAGGCCGCATGACCTTGGTGTTTGGGTGCCGCCGCCCAGAT
GAGGACCACATCTACCAGGAGGAGATGCTGGAGATGGCCCAGAAGGGGGTGCTGCATGCG
GTGCACACAGCCTATTCCCGCCTGCCTGGCAAGCCCAAGGTCTATGTTCAGGACATCCTG
CGGCAGCAGCTGGCCAGCGAGGTGCTCCGTGTGCTCCACAAGGAGCCAGGCCACCTCTAT
GTTTGCGGGGATGTGCGCATGGCCCGGGACGTGGCCCACACCCTGAAGCAGCTGGTGGCT
GCCAAGCTGAAATTGAATGAGGAGCAGGTCGAGGACTATTTCTTTCAGCTCAAGAGCCAG
AAGCGCTATCACGAAGATATCTTCGGTGCTGTATTTCCTTACGAGGCGAAGAAGGACAGG
GTGGCGGTGCAGCCCAGCAGCCTGGAGATGTCAGCGCTCTGA
|
| Enzyme 1 GenBank Gene ID |
L09210  |
| Enzyme 1 GeneCard ID |
NOS2A  |
| Enzyme 1 GenAtlas ID |
NOS2A  |
| Enzyme 1 HGNC ID |
HGNC:7873  |
| Enzyme 1 Chromosome Location |
17 |
| Enzyme 1 Locus |
17q11.2-q12 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Geller DA, Lowenstein CJ, Shapiro RA, Nussler AK, Di Silvio M, Wang SC, Nakayama DK, Simmons RL, Snyder SH, Billiar TR: Molecular cloning and expression of inducible nitric oxide synthase from human hepatocytes. Proc Natl Acad Sci U S A. 1993 Apr 15;90(8):3491-5. [PubMed
]
- Sherman PA, Laubach VE, Reep BR, Wood ER: Purification and cDNA sequence of an inducible nitric oxide synthase from a human tumor cell line. Biochemistry. 1993 Nov 2;32(43):11600-5. [PubMed
]
- Charles IG, Palmer RM, Hickery MS, Bayliss MT, Chubb AP, Hall VS, Moss DW, Moncada S: Cloning, characterization, and expression of a cDNA encoding an inducible nitric oxide synthase from the human chondrocyte. Proc Natl Acad Sci U S A. 1993 Dec 1;90(23):11419-23. [PubMed
]
- Maier R, Bilbe G, Rediske J, Lotz M: Inducible nitric oxide synthase from human articular chondrocytes: cDNA cloning and analysis of mRNA expression. Biochim Biophys Acta. 1994 Sep 21;1208(1):145-50. [PubMed
]
- Park CS, Pardhasaradhi K, Gianotti C, Villegas E, Krishna G: Human retina expresses both constitutive and inducible isoforms of nitric oxide synthase mRNA. Biochem Biophys Res Commun. 1994 Nov 30;205(1):85-91. [PubMed
]
- Hokari A, Zeniya M, Esumi H: Cloning and functional expression of human inducible nitric oxide synthase (NOS) cDNA from a glioblastoma cell line A-172. J Biochem (Tokyo). 1994 Sep;116(3):575-81. [PubMed
]
- Guo FH, De Raeve HR, Rice TW, Stuehr DJ, Thunnissen FB, Erzurum SC: Continuous nitric oxide synthesis by inducible nitric oxide synthase in normal human airway epithelium in vivo. Proc Natl Acad Sci U S A. 1995 Aug 15;92(17):7809-13. [PubMed
]
- Luss H, Li RK, Shapiro RA, Tzeng E, McGowan FX, Yoneyama T, Hatakeyama K, Geller DA, Mickle DA, Simmons RL, Billiar TR: Dedifferentiated human ventricular cardiac myocytes express inducible nitric oxide synthase mRNA but not protein in response to IL-1, TNF, IFNgamma, and LPS. J Mol Cell Cardiol. 1997 Apr;29(4):1153-65. [PubMed
]
- McLay JS, Chatterjee P, Nicolson AG, Jardine AG, McKay NG, Ralston SH, Grabowski P, Haites NE, MacLeod AM, Hawksworth GM: Nitric oxide production by human proximal tubular cells: a novel immunomodulatory mechanism? Kidney Int. 1994 Oct;46(4):1043-9. [PubMed
]
- Bloch KD, Wolfram JR, Brown DM, Roberts JD Jr, Zapol DG, Lepore JJ, Filippov G, Thomas JE, Jacob HJ, Bloch DB: Three members of the nitric oxide synthase II gene family (NOS2A, NOS2B, and NOS2C) colocalize to human chromosome 17. Genomics. 1995 Jun 10;27(3):526-30. [PubMed
]
- Taylor BS, Alarcon LH, Billiar TR: Inducible nitric oxide synthase in the liver: regulation and function. Biochemistry (Mosc). 1998 Jul;63(7):766-81. [PubMed
]
- Glynne PA, Darling KE, Picot J, Evans TJ: Epithelial inducible nitric-oxide synthase is an apical EBP50-binding protein that directs vectorial nitric oxide output. J Biol Chem. 2002 Sep 6;277(36):33132-8. Epub 2002 Jun 21. [PubMed
]
- Li H, Raman CS, Glaser CB, Blasko E, Young TA, Parkinson JF, Whitlow M, Poulos TL: Crystal structures of zinc-free and -bound heme domain of human inducible nitric-oxide synthase. Implications for dimer stability and comparison with endothelial nitric-oxide synthase. J Biol Chem. 1999 Jul 23;274(30):21276-84. [PubMed
]
- Fischmann TO, Hruza A, Niu XD, Fossetta JD, Lunn CA, Dolphin E, Prongay AJ, Reichert P, Lundell DJ, Narula SK, Weber PC: Structural characterization of nitric oxide synthase isoforms reveals striking active-site conservation. Nat Struct Biol. 1999 Mar;6(3):233-42. [PubMed
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
6216 |
| Enzyme 2 Name |
Nitric-oxide synthase, brain |
| Enzyme 2 Synonyms |
- NOS type I
- Neuronal NOS
- N-NOS
- nNOS
- Constitutive NOS
- NC-NOS
- bNOS
|
| Enzyme 2 Gene Name |
NOS1 |
| Enzyme 2 Protein Sequence |
>Nitric-oxide synthase, brain
MEDHMFGVQQIQPNVISVRLFKRKVGGLGFLVKERVSKPPVIISDLIRGGAAEQSGLIQA
GDIILAVNGRPLVDLSYDSALEVLRGIASETHVVLILRGPEGFTTHLETTFTGDGTPKTI
RVTQPLGPPTKAVDLSHQPPAGKEQPLAVDGASGPGNGPQHAYDDGQEAGSLPHANGLAP
RPPGQDPAKKATRVSLQGRGENNELLKEIEPVLSLLTSGSRGVKGGAPAKAEMKDMGIQV
DRDLDGKSHKPLPLGVENDRVFNDLWGKGNVPVVLNNPYSEKEQPPTSGKQSPTKNGSPS
KCPRFLKVKNWETEVVLTDTLHLKSTLETGCTEYICMGSIMHPSQHARRPEDVRTKGQLF
PLAKEFIDQYYSSIKRFGSKAHMERLEEVNKEIDTTSTYQLKDTELIYGAKHAWRNASRC
VGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLRSAITIFPQRTDGKHDFRVW
NSQLIRYAGYKQPDGSTLGDPANVQFTEICIQQGWKPPRGRFDVLPLLLQANGNDPELFQ
IPPELVLEVPIRHPKFEWFKDLGLKWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGV
RDYCDNSRYNILEEVAKKMNLDMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSAT
ESFIKHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEMLNYRLTPSFEYQPDPWNTHV
WKGTNGTPTKRRAIGFKKLAEAVKFSAKLMGQAMAKRVKATILYATETGKSQAYAKTLCE
IFKHAFDAKVMSMEEYDIVHLEHETLVLVVTSTFGNGDPPENGEKFGCALMEMRHPNSVQ
EERKSYKVRFNSVSSYSDSQKSSGDGPDLRDNFESAGPLANVRFSVFGLGSRAYPHFCAF
GHAVDTLLEELGGERILKMREGDELCGQEEAFRTWAKKVFKAACDVFCVGDDVNIEKANN
SLISNDRSWKRNKFRLTFVAEAPELTQGLSNVHKKRVSAARLLSRQNLQSPKSSRSTIFV
RLHTNGSQELQYQPGDHLGVFPGNHEDLVNALIERLEDAPPVNQMVKVELLEERNTALGV
ISNWTDELRLPPCTIFQAFKYYLDITTPPTPLQLQQFASLATSEKEKQRLLVLSKGLQEY
EEWKWGKNPTIVEVLEEFPSIQMPATLLLTQLSLLQPRYYSISSSPDMYPDEVHLTVAIV
SYRTRDGEGPIHHGVCSSWLNRIQADELVPCFVRGAPSFHLPRNPQVPCILVGPGTGIAP
FRSFWQQRQFDIQHKGMNPCPMVLVFGCRQSKIDHIYREETLQAKNKGVFRELYTAYSRE
PDKPKKYVQDILQEQLAESVYRALKEQGGHIYVCGDVTMAADVLKAIQRIMTQQGKLSAE
DAGVFISRMRDDNRYHEDIFGVTLRTYEVTNRLRSESIAFIEESKKDTDEVFSS
|
| Enzyme 2 Number of Residues |
1434 |
| Enzyme 2 Molecular Weight |
160972 |
| Enzyme 2 Theoretical pI |
7.44 |
| Enzyme 2 GO Classification |
| Function |
- FAD binding
- FMN binding
- NADP binding
- adenyl nucleotide binding
- binding
- calmodulin binding
- catalytic activity
- cation binding
- coenzyme binding
- cofactor binding
- electron transporter activity
- heme binding
- ion binding
- iron ion binding
- monooxygenase activity
- nitric-oxide synthase activity
- nucleotide binding
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD or NADH as one donor, and incorporation of one atom of oxygen
- protein binding
- purine nucleotide binding
- tetrapyrrole binding
- transition metal ion binding
- transporter activity
|
| Process |
- biosynthesis
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- nitric oxide biosynthesis
- physiological process
|
| Component |
| — |
|
| Enzyme 2 General Function |
Inorganic ion transport and metabolism |
| Enzyme 2 Specific Function |
Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In the brain and peripheral nervous system, NO displays many properties of a neurotransmitter |
| Enzyme 2 Pathways |
- Arginine and Proline Metabolism (map00330
)
|
| Enzyme 2 Reactions |
- L-arginine + n NADPH + n H+ + m O2 = citrulline + nitric oxide + n NADP+
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
642526  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
P29475  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
NOS1_HUMAN  |
| Enzyme 2 PDB ID |
Not Available |
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>4305 bp
ATGGAGGATCACATGTTCGGTGTTCAGCAAATCCAGCCCAATGTCATTTCTGTTCGTCTC
TTCAAGCGCAAAGTTGGGGGCCTGGGATTTCTGGTGAAGGAGCGGGTCAGTAAGCCGCCC
GTGATCATCTCTGACCTGATTCGTGGGGGCGCCGCAGAGCAGAGTGGCCTCATCCAGGCC
GGAGACATCATTCTTGCGGTCAACGGCCGGCCCTTGGTGGACCTGAGCTATGACAGCGCC
CTGGAGGTACTCAGAGGCATTGCCTCTGAGACCCACGTGGTCCTCATTCTGAGGGGCCCT
GAAGGTTTCACCACGCACCTGGAGACCACCTTTACAGGTGATGGGACCCCCAAGACCATC
CGGGTGACACAGCCCCTGGGTCCCCCCACCAAAGCCGTGGATCTGTCCCACCAGCCACCG
GCCGGCAAAGAACAGCCCCTGGCAGTGGATGGGGCCTCGGGTCCCGGGAATGGGCCTCAG
CATGCCTACGATGATGGGCAGGAGGCTGGCTCACTCCCCCATGCCAACGGCCTGGCCCCC
AGGCCCCCAGGCCAGGACCCCGCGAAGAAAGCAACCAGAGTCAGCCTCCAAGGCAGAGGG
GAGAACAATGAACTGCTCAAGGAGATAGAGCCTGTGCTGAGCCTTCTCACCAGTGGGAGC
AGAGGGGTCAAGGGAGGGGCACCTGCCAAGGCAGAGATGAAAGATATGGGAATCCAGGTG
GACAGAGATTTGGACGGCAAGTCACACAAACCTCTGCCCCTCGGCGTGGAGAACGACCGA
GTCTTCAATGACCTATGGGGGAAGGGCAATGTGCCTGTCGTCCTCAACAACCCATATTCA
GAGAAGGAGCAGCCCCCCACCTCAGGAAAACAGTCCCCCACAAAGAATGGCAGCCCCTCC
AAGTGTCCACGCTTCCTCAAGGTCAAGAACTGGGAGACTGAGGTGGTTCTCACTGACACC
CTCCACCTTAAGAGCACATTGGAAACGGGATGCACTGAGTACATCTGCATGGGCTCCATC
ATGCATCCTTCTCAGCATGCAAGGAGGCCTGAAGACGTCCGCACAAAAGGACAGCTCTTC
CCTCTCGCCAAAGAGTTTATTGATCAATACTATTCATCAATTAAAAGATTTGGCTCCAAA
GCCCACATGGAAAGGCTGGAAGAGGTGAACAAAGAGATCGACACCACTAGCACTTACCAG
CTCAAGGACACAGAGCTCATCTATGGGGCCAAGCACGCCTGGCGGAATGCCTCGCGCTGT
GTGGGCAGGATCCAGTGGTCCAAGCTGCAGGTATTCGATGCCCGTGACTGCACCACGGCC
CACGGGATGTTCAACTACATCTGTAACCATGTCAAGTATGCCACCAACAAAGGGAACCTC
AGGTCTGCCATCACCATATTCCCCCAGAGGACAGACGGCAAGCACGACTTCCGAGTCTGG
AACTCCCAGCTCATCCGCTACGCTGGCTACAAGCAGCCTGACGGCTCCACCCTGGGGGAC
CCAGCCAATGTGCAGTTCACAGAGATATGCATACAGCAGGGCTGGAAACCGCCTAGAGGC
CGCTTCGATGTCCTGCCGCTCCTGCTTCAGGCCAACGGCAATGACCCTGAGCTCTTCCAG
ATTCCTCCAGAGCTGGTGTTGGAAGTTCCCATCAGGCACCCCAAGTTTGAGTGGTTCAAG
GACCTGGGGCTGAAGTGGTACGGCCTCCCCGCCGTGTCCAACATGCTCCTAGAGATTGGC
GGCCTGGAGTTCAGCGCCTGTCCCTTCAGTGGCTGGTACATGGGCACAGAGATTGGTGTC
CGCGACTACTGTGACAACTCCCGCTACAATATCCTGGAGGAAGTGGCCAAGAAGATGAAC
TTAGACATGAGGAAGACGTCCTCCCTGTGGAAGGACCAGGCGCTGGTGGAGATCAATATC
GCGGTTCTCTATAGCTTCCAGAGTGACAAAGTGACCATTGTTGACCATCACTCCGCCACC
GAGTCCTTCATTAAGCACATGGAGAATGAGTACCGCTGCCGGGGGGGCTGCCCTGCCGAC
TGGGTGTGGATCGTGCCCCCCATGTCCGGAAGCATCACCCCTGTGTTCCACCAGGAGATG
CTCAACTACCGGCTCACCCCCTCCTTCGAATACCAGCCTGATCCCTGGAACACGCATGTC
TGGAAAGGCACCAACGGGACCCCCACAAAGCGGCGAGCCATCGGCTTCAAGAAGCTAGCA
GAAGCTGTCAAGTTCTCGGCCAAGCTGATGGGGCAGGCTATGGCCAAGAGGGTGAAAGCG
ACCATCCTCTATGCCACAGAGACAGGCAAATCGCAAGCTTATGCCAAGACCTTGTGTGAG
ATCTTCAAACACGCCTTTGATGCCAAGGTGATGTCCATGGAAGAATATGACATTGTGCAC
CTGGAACATGAAACTCTGGTCCTTGTGGTCACCAGCACCTTTGGCAATGGAGATCCCCCT
GAGAATGGGGAGAAATTCGGCTGTGCTTTGATGGAAATGAGGCACCCCAACTCTGTGCAG
GAAGAAAGGAAGAGCTACAAGGTCCGATTCAACAGCGTCTCCTCCTACTCTGACTCCCAA
AAATCATCAGGCGATGGGCCCGACCTCAGAGACAACTTTGAGAGTGCTGGACCCCTGGCC
AATGTGAGGTTCTCAGTTTTTGGCCTCGGCTCACGAGCATACCCTCACTTTTGCGCCTTC
GGACACGCTGTGGACACCCTCCTGGAAGAACTGGGAGGGGAGAGGATCCTGAAGATGAGG
GAAGGGGATGAGCTCTGTGGGCAGGAAGAGGCTTTCAGGACCTGGGCCAAGAAGGTCTTC
AAGGCAGCCTGTGATGTCTTCTGTGTGGGAGATGATGTCAACATTGAAAAGGCCAACAAT
TCCCTCATCAGCAATGATCGCAGCTGGAAGAGAAACAAGTTCCGCCTCACCTTTGTGGCC
GAAGCTCCAGAACTCACACAAGGTCTATCCAATGTCCACAAAAAGCGAGTCTCAGCTGCC
CGGCTCCTTAGCCGTCAAAACCTCCAGAGCCCTAAATCCAGTCGGTCAACTATCTTCGTG
CGTCTCCACACCAACGGGAGCCAGGAGCTGCAGTACCAGCCTGGGGACCACCTGGGTGTC
TTCCCTGGCAACCACGAGGACCTCGTGAATGCCCTGATCGAGCGGCTGGAGGACGCGCCG
CCTGTCAACCAGATGGTGAAAGTGGAACTGCTGGAGGAGCGGAACACGGCTTTAGGTGTC
ATCAGTAACTGGACAGACGAGCTCCGCCTCCCGCCCTGCACCATCTTCCAGGCCTTCAAG
TACTACCTGGACATCACCACGCCACCAACGCCTCTGCAGCTGCAGCAGTTTGCCTCCCTA
GCTACCAGCGAGAAGGAGAAGCAGCGTCTGCTGGTCCTCAGCAAGGGTTTGCAGGAGTAC
GAGGAATGGAAATGGGGCAAGAACCCCACCATCGTGGAGGTGCTGGAGGAGTTCCCATCT
ATCCAGATGCCGGCCACCCTGCTCCTGACCCAGCTGTCCCTGCTGCAGCCCCGCTACTAT
TCCATCAGCTCCTCCCCAGACATGTACCCTGATGAAGTGCACCTCACTGTGGCCATCGTT
TCCTACCGCACTCGAGATGGAGAAGGACCAATTCACCACGGCGTATGCTCCTCCTGGCTC
AACCGGATACAGGCTGACGAACTGGTCCCCTGTTTCGTGAGAGGAGCACCCAGCTTCCAC
CTGCCCCGGAACCCCCAAGTCCCCTGCATCCTCGTTGGACCAGGCACCGGCATTGCCCCT
TTCCGAAGCTTCTGGCAACAGCGGCAATTTGATATCCAACACAAAGGAATGAACCCCTGC
CCCATGGTCCTGGTCTTCGGGTGCCGGCAATCCAAGATAGATCATATCTACAGGGAAGAG
ACCCTGCAGGCCAAGAACAAGGGGGTCTTCAGAGAGCTGTACACGGCTTACTCCCGGGAG
CCAGACAAACCAAAGAAGTACGTGCAGGACATCCTGCAGGAGCAGCTGGCGGAGTCTGTG
TACCGAGCCCTGAAGGAGCAAGGGGGCCACATATACGTCTGTGGGGACGTCACCATGGCT
GCTGATGTCCTCAAAGCCATCCAGCGCATCATGACCCAGCAGGGGAAGCTCTCGGCAGAG
GACGCCGGCGTATTCATCAGCCGGATGAGGGATGACAACCGATACCATGAGGATATTTTT
GGAGTCACCCTGCGAACGTACGAAGTGACCAACCGCCTTAGATCTGAGTCCATTGCCTTC
ATTGAAGAGAGCAAAAAAGACACCGATGAGGTTTTCAGCTCCTAA
|
| Enzyme 2 GenBank Gene ID |
U17327  |
| Enzyme 2 GeneCard ID |
NOS1  |
| Enzyme 2 GenAtlas ID |
NOS1  |
| Enzyme 2 HGNC ID |
HGNC:7872  |
| Enzyme 2 Chromosome Location |
12 |
| Enzyme 2 Locus |
12q24.2-q24.31 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Hall AV, Antoniou H, Wang Y, Cheung AH, Arbus AM, Olson SL, Lu WC, Kau CL, Marsden PA: Structural organization of the human neuronal nitric oxide synthase gene (NOS1). J Biol Chem. 1994 Dec 30;269(52):33082-90. [PubMed
]
- Fujisawa H, Ogura T, Kurashima Y, Yokoyama T, Yamashita J, Esumi H: Expression of two types of nitric oxide synthase mRNA in human neuroblastoma cell lines. J Neurochem. 1994 Jul;63(1):140-5. [PubMed
]
- Nakane M, Schmidt HH, Pollock JS, Forstermann U, Murad F: Cloned human brain nitric oxide synthase is highly expressed in skeletal muscle. FEBS Lett. 1993 Jan 25;316(2):175-80. [PubMed
]
- Park CS, Gianotti C, Park R, Krishna G: Neuronal isoform of nitric oxide synthase is expressed at low levels in human retina. Cell Mol Neurobiol. 1996 Aug;16(4):499-515. [PubMed
]
- Wang Y, Goligorsky MS, Lin M, Wilcox JN, Marsden PA: A novel, testis-specific mRNA transcript encoding an NH2-terminal truncated nitric-oxide synthase. J Biol Chem. 1997 Apr 25;272(17):11392-401. [PubMed
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
6217 |
| Enzyme 3 Name |
Nitric-oxide synthase, endothelial |
| Enzyme 3 Synonyms |
- EC-NOS
- NOS type III
- NOSIII
- Endothelial NOS
- eNOS
- Constitutive NOS
- cNOS
|
| Enzyme 3 Gene Name |
NOS3 |
| Enzyme 3 Protein Sequence |
>Nitric-oxide synthase, endothelial
MGNLKSVAQEPGPPCGLGLGLGLGLCGKQGPATPAPEPSRAPASLLPPAPEHSPPSSPLT
QPPEGPKFPRVKNWEVGSITYDTLSAQAQQDGPCTPRRCLGSLVFPRKLQGRPSPGPPAP
EQLLSQARDFINQYYSSIKRSGSQAHEQRLQEVEAEVAATGTYQLRESELVFGAKQAWRN
APRCVGRIQWGKLQVFDARDCRSAQEMFTYICNHIKYATNRGNLRSAITVFPQRCPGRGD
FRIWNSQLVRYAGYRQQDGSVRGDPANVEITELCIQHGWTPGNGRFDVLPLLLQAPDEPP
ELFLLPPELVLEVPLEHPTLEWFAALGLRWYALPAVSNMLLEIGGLEFPAAPFSGWYMST
EIGTRNLCDPHRYNILEDVAVCMDLDTRTTSSLWKDKAAVEINVAVLHSYQLAKVTIVDH
HAATASFMKHLENEQKARGGCPADWAWIVPPISGSLTPVFHQEMVNYFLSPAFRYQPDPW
KGSAAKGTGITRKKTFKEVANAVKISASLMGTVMAKRVKATILYGSETGRAQSYAQQLGR
LFRKAFDPRVLCMDEYDVVSLEHETLVLVVTSTFGNGDPPENGESFAAALMEMSGPYNSS
PRPEQHKSYKIRFNSISCSDPLVSSWRRKRKESSNTDSAGALGTLRFCVFGLGSRAYPHF
CAFARAVDTRLEELGGERLLQLGQGDELCGQEEAFRGWAQAAFQAACETFCVGEDAKAAA
RDIFSPKRSWKRQRYRLSAQAEGLQLLPGLIHVHRRKMFQATIRSVENLQSSKSTRATIL
VRLDTGGQEGLQYQPGDHIGVCPPNRPGLVEALLSRVEDPPAPTEPVAVEQLEKGSPGGP
PPGWVRDPRLPPCTLRQALTFFLDITSPPSPQLLRLLSTLAEEPREQQELEALSQDPRRY
EEWKWFRCPTLLEVLEQFPSVALPAPLLLTQLPLLQPRYYSVSSAPSTHPGEIHLTVAVL
AYRTQDGLGPLHYGVCSTWLSQLKPGDPVPCFIRGAPSFRLPPDPSLPCILVGPGTGIAP
FRGFWQERLHDIESKGLQPTPMTLVFGCRCSQLDHLYRDEVQNAQQRGVFGRVLTAFSRE
PDNPKTYVQDILRTELAAEVHRVLCLERGHMFVCGDVTMATNVLQTVQRILATEGDMELD
EAGDVIGVLRDQQRYHEDIFGLTLRTQEVTSRIRTQSFSLQERQLRGAVPWAFDPPGSDT
NSP
|
| Enzyme 3 Number of Residues |
1203 |
| Enzyme 3 Molecular Weight |
133290 |
| Enzyme 3 Theoretical pI |
7.27 |
| Enzyme 3 GO Classification |
| Function |
- FMN binding
- binding
- catalytic activity
- monooxygenase activity
- nitric-oxide synthase activity
- nucleotide binding
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD or NADH as one donor, and incorporation of one atom of oxygen
|
| Process |
- biosynthesis
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- nitric oxide biosynthesis
- physiological process
|
| Component |
| — |
|
| Enzyme 3 General Function |
Inorganic ion transport and metabolism |
| Enzyme 3 Specific Function |
Produces nitric oxide (NO) which is implicated in vascular smooth muscle relaxation through a cGMP-mediated signal transduction pathway. No mediates vascular endothelial growth factor (VEGF)-induced angiogenesis in coronary vessels and promotes blood clotting through the activation of platelets |
| Enzyme 3 Pathways |
- Arginine and Proline Metabolism (map00330
)
|
| Enzyme 3 Reactions |
- L-arginine + n NADPH + n H+ + m O2 = citrulline + nitric oxide + n NADP+
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
189212  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
P29474  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
NOS3_HUMAN  |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>3612 bp
ATGGGCAACTTGAAGAGCGTGGCCCAGGAGCCTGGGCCACCCTGCGGCCTGGGGCTGGGG
CTGGGCCTTGGGCTGTGCGGCAAGCAGGGCCCAGCCACCCCGGCCCCTGAGCCCAGCCGG
GCCCCAGCATCCCTACTCCCACCAGCGCCAGAACACAGCCCCCCGAGCTCCCCGCTAACC
CAGCCCCCAGAGGGGCCCAAGTTCCCTCGTGTGAAGAACTGGGAGGTGGGGAGCATCACC
TATGACACCCTCAGCGCCCAGGCGCAGCAGGATGGGCCCTGCACCCCAAGACGCTGCCTG
GGCTCCCTGGTATTTCCACGGAAACTACAGGGCCGGCCCTCCCCCGGCCCCCCGGCCCCT
GAGCAGCTGCTGAGTCAGGCCCGGGACTTCATCAACCAGTACTACAGCTCCATTAAGAGG
AGCGGCTCCCAGGCCCACGAACAGCGGCTTCAAGAGGTGGAAGCCGAGGTGGCAGCCACA
GGCACCTACCAGCTTAGGGAGAGCGAGCTGGTGTTCGGGGCTAAGCAGGCCTGGCGCAAC
GCTCCCCGCTGCGTGGGCCGGATCCAGTGGGGGAAGCTGCAGGTGTTCGATGCCCGGGAC
TGCAGGTCTGCACAGGAAATGTTCACCTACATCTGCAACCACATCAAGTATGCCACCAAC
CGGGGCAACCTTCGCTCGGCCATCACAGTGTTCCCGCAGCGCTGCCCTGGCCGAGGAGAC
TTCCGAATCTGGAACAGCCAGCTGGTGCGCTACGCGGGCTACCGGCAGCAGGACGGCTCT
GTGCGGGGGGACCCAGCCAACGTGGAGATCACCGAGCTCTGCATTCAGCACGGCTGGACC
CCAGGAAACGGTCGCTTCGACGTGCTGCCCCTGCTGCTGCAGGCCCCAGATGAGCCCCCA
GAACTCTTCCTTCTGCCCCCCGAGCTGGTCCTTGAGGTGCCCCTGGAGCACCCCACGCTG
GAGTGGTTTGCAGCCCTGGGCCTGCGCTGGTACGCCCTCCCGGCAGTGTCCAACATGCTG
CTGGAAATTGGGGGCCTGGAGTTCCCCGCAGCCCCCTTCAGTGGCTGGTACATGAGCACT
GAGATCGGCACGAGGAACCTGTGTGACCCTCACCGCTACAACATCCTGGAGGATGTGGCT
GTCTGCATGGACCTGGATACCCGGACCACCTCGTCCCTGTGGAAAGACAAGGCAGCAGTG
GAAATCAACGTGGCCGTGCTGCACAGTTACCAGCTAGCCAAAGTCACCATCGTGGACCAC
CACGCCGCCACGGCCTCTTTCATGAAGCACCTGGAGAATGAGCAGAAGGCCAGGGGGGGC
TGCCCTGCAGACTGGGCCTGGATCGTGCCCCCCATCTCGGGCAGCCTCACTCCTGTTTTC
CATCAGGAGATGGTCAACTATTTCCTGTCCCCGGCCTTCCGCTACCAGCCAGACCCCTGG
AAGGGGAGTGCCGCCAAGGGCACCGGCATCACCAGGAAGAAGACCTTTAAAGAAGTGGCC
AACGCCGTGAAGATCTCCGCCTCGCTCATGGGCACGGTGATGGCGAAGCGAGTGAAGGCG
ACAATCCTGTATGGCTCCGAGACCGGCCGGGCCCAGAGCTACGCACAGCAGCTGGGGAGA
CTCTTCCGGAAGGCTTTTGATCCCCGGGTCCTGTGTATGGATGAGTATGACGTGGTGTCC
CTCGAACACGAGACGCTGGTGCTGGTGGTAACCAGCACATTTGGGAATGGGGATCCCCCG
GAGAATGGAGAGAGCTTTGCAGCTGCCCTGATGGAGATGTCCGGCCCCTACAACAGCTCC
CCTCGGCCGGAACAGCACAAGAGTTATAAGATCCGCTTCAACAGCATCTCCTGCTCAGAC
CCACTGGTGTCCTCTTGGCGGCGGAAGAGGAAGGAGTCCAGTAACACAGACAGTGCAGGG
GCCCTGGGCACCCTCAGGTTCTGTGTGTTCGGGCTCGGCTCCCGGGCATACCCCCACTTC
TGCGCCTTTGCTCGTGCCGTGGACACACGGCTGGAGGAACTGGGCGGGGAGCGGCTGCTG
CAGCTGGGCCAGGGCGACGAGCTGTGCGGCCAGGAGGAGGCCTTCCGAGGCTGGGCCCAG
GCTGCCTTCCAGGCCGCCTGTGAGACCTTCTGTGTGGGAGAGGATGCCAAGGCCGCCGCC
CGAGACATCTTCAGCCCCAAACGGAGCTGGAAGCGCCAGAGGTACCGGCTGAGCGCCCAG
GCCGAGGGCCTGCAGTTGCTGCCAGGTCTGATCCACGTGCACAGGCGGAAGATGTTCCAG
GCTACAATCCGCTCAGTGGAAAACCTGCAAAGCAGCAAGTCCACGAGGGCCACCATCCTG
GTGCGCCTGGACACCGGAGGCCAGGAGGGGCTGCAGTACCAGCCGGGGGACCACATAGGT
GTCTGCCCGCCCAACCGGCCCGGCCTTGTGGAGGCGCTGCTGAGCCGCGTGGAGGACCCG
CCGGCGCCCACTGAGCCCGTGGCAGTAGAGCAGCTGGAGAAGGGCAGCCCTGGTGGCCCT
CCCCCCGGCTGGGTGCGGGACCCCCGGCTGCCCCCGTGCACGCTGCGCCAGGCTCTCACC
TTCTTCCTGGACATCACCTCCCCACCCAGCCCTCAGCTCTTGCGGCTGCTCAGCACCTTG
GCAGAAGAGCCCAGGGAACAGCAGGAGCTGGAGGCCCTCAGCCAGGATCCCCGACGCTAC
GAGGAGTGGAAGTGGTTCCGCTGCCCCACGCTGCTGGAGGTGCTGGAGCAGTTCCCGTCG
GTGGCGCTGCCTGCCCCACTGCTCCTCACCCAGCTGCCTCTGCTCCAGCCCCGGTACTAC
TCAGTCAGCTCGGCACCCAGCACCCACCCAGGAGAGATCCACCTCACTGTAGCTGTGCTG
GCATACAGGACTCAGGATGGGCTGGGCCCCCTGCACTATGGAGTCTGCTCCACGTGGCTA
AGCCAGCTCAAGCCCGGAGACCCTGTGCCCTGCTTCATCCGGGGGGCTCCCTCCTTCCGG
CTGCCACCCGATCCCAGCTTGCCCTGCATCCTGGTGGGTCCAGGCACTGGCATTGCCCCC
TTCCGGGGATTCTGGCAGGAGCGGCTGCATGACATTGAGAGCAAAGGGCTGCAGCCCACT
CCCATGACTTTGGTGTTCGGCTGCCGATGCTCCCAACTTGACCATCTCTACCGCGACGAG
GTGCAGAACGCCCAGCAGCGCGGGGTGTTTGGCCGAGTCCTCACCGCCTTCTCCCGGGAA
CCTGACAACCCCAAGACCTACGTGCAGGACATCCTGAGGACGGAGCTGGCTGCGGAGGTG
CACCGCGTGCTGTGCCTCGAGCGGGGCCACATGTTTGTCTGCGGCGATGTTACCATGGCA
ACCAACGTCCTGCAGACCGTGCAGCGCATCCTGGCGACGGAGGGCGACATGGAGCTGGAC
GAGGCCGGCGACGTCATCGGCGTGCTGCGGGATCAGCAACGCTACCACGAAGACATTTTC
GGGCTCACGCTGCGCACCCAGGAGGTGACAAGCCGCATACGCACCCAGAGCTTTTCCTTG
CAGGAGCGTCAGTTGCGGGGCGCAGTGCCCTGGGCGTTCGACCCTCCCGGCTCAGACACC
AACAGCCCCTGA
|
| Enzyme 3 GenBank Gene ID |
M93718  |
| Enzyme 3 GeneCard ID |
NOS3  |
| Enzyme 3 GenAtlas ID |
NOS3  |
| Enzyme 3 HGNC ID |
HGNC:7876  |
| Enzyme 3 Chromosome Location |
7 |
| Enzyme 3 Locus |
7q36 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- Janssens SP, Shimouchi A, Quertermous T, Bloch DB, Bloch KD: Cloning and expression of a cDNA encoding human endothelium-derived relaxing factor/nitric oxide synthase. J Biol Chem. 1992 Jul 25;267(21):14519-22. [PubMed
]
- Marsden PA, Schappert KT, Chen HS, Flowers M, Sundell CL, Wilcox JN, Lamas S, Michel T: Molecular cloning and characterization of human endothelial nitric oxide synthase. FEBS Lett. 1992 Aug 3;307(3):287-93. [PubMed
]
- Marsden PA, Heng HH, Scherer SW, Stewart RJ, Hall AV, Shi XM, Tsui LC, Schappert KT: Structure and chromosomal localization of the human constitutive endothelial nitric oxide synthase gene. J Biol Chem. 1993 Aug 15;268(23):17478-88. [PubMed
]
- Nadaud S, Bonnardeaux A, Lathrop M, Soubrier F: Gene structure, polymorphism and mapping of the human endothelial nitric oxide synthase gene. Biochem Biophys Res Commun. 1994 Feb 15;198(3):1027-33. [PubMed
]
- Miyahara K, Kawamoto T, Sase K, Yui Y, Toda K, Yang LX, Hattori R, Aoyama T, Yamamoto Y, Doi Y, et al.: Cloning and structural characterization of the human endothelial nitric-oxide-synthase gene. Eur J Biochem. 1994 Aug 1;223(3):719-26. [PubMed
]
- Robinson LJ, Weremowicz S, Morton CC, Michel T: Isolation and chromosomal localization of the human endothelial nitric oxide synthase (NOS3) gene. Genomics. 1994 Jan 15;19(2):350-7. [PubMed
]
- Sase K, Michel T: Expression of constitutive endothelial nitric oxide synthase in human blood platelets. Life Sci. 1995;57(22):2049-55. [PubMed
]
- Fischmann TO, Hruza A, Niu XD, Fossetta JD, Lunn CA, Dolphin E, Prongay AJ, Reichert P, Lundell DJ, Narula SK, Weber PC: Structural characterization of nitric oxide synthase isoforms reveals striking active-site conservation. Nat Struct Biol. 1999 Mar;6(3):233-42. [PubMed
]
- Rosenfeld RJ, Garcin ED, Panda K, Andersson G, Aberg A, Wallace AV, Morris GM, Olson AJ, Stuehr DJ, Tainer JA, Getzoff ED: Conformational changes in nitric oxide synthases induced by chlorzoxazone and nitroindazoles: crystallographic and computational analyses of inhibitor potency. Biochemistry. 2002 Nov 26;41(47):13915-25. [PubMed
]
- Yoshimura M, Yasue H, Nakayama M, Shimasaki Y, Sumida H, Sugiyama S, Kugiyama K, Ogawa H, Ogawa Y, Saito Y, Miyamoto Y, Nakao K: A missense Glu298Asp variant in the endothelial nitric oxide synthase gene is associated with coronary spasm in the Japanese. Hum Genet. 1998 Jul;103(1):65-9. [PubMed
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
6948 |
| Enzyme 4 Name |
Hemoglobin subunit beta |
| Enzyme 4 Synonyms |
- Hemoglobin beta chain
- Beta-globin
|
| Enzyme 4 Gene Name |
HBB |
| Enzyme 4 Protein Sequence |
>Hemoglobin subunit beta
MVHLTPEEKSAVTALWGKVNVDEVGGEALGRLLVVYPWTQRFFESFGDLSTPDAVMGNPK
VKAHGKKVLGAFSDGLAHLDNLKGTFATLSELHCDKLHVDPENFRLLGNVLVCVLAHHFG
KEFTPPVQAAYQKVVAGVANALAHKYH
|
| Enzyme 4 Number of Residues |
147 |
| Enzyme 4 Molecular Weight |
15999 |
| Enzyme 4 Theoretical pI |
7.32 |
| Enzyme 4 GO Classification |
| Function |
- binding
- heme binding
- oxygen binding
- tetrapyrrole binding
|
| Process |
- cellular physiological process
- gas transport
- oxygen transport
- physiological process
- transport
|
| Component |
- hemoglobin complex
- protein complex
|
|
| Enzyme 4 General Function |
Not Available |
| Enzyme 4 Specific Function |
Involved in oxygen transport from the lung to the various peripheral tissues |
| Enzyme 4 Pathways |
Not Available |
| Enzyme 4 Reactions |
Not Available |
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
455993  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
P68871  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
HBB_HUMAN  |
| Enzyme 4 PDB ID |
1DXT  |
| Enzyme 4 PDB File |
Show |
| Enzyme 4 3D Structure |
|
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>444 bp
ATGGTGCACCTGACTCCTGAGGAGAAGTCTGCCGTTACTGCCCTGTGGGGCAAGGTGAAC
GTGGATGAAGTTGGTGGTGAGGCCCTGGGCAGGCTGCTGGTGGTCTACCCTTGGACCCAG
AGGTTCTTTGAGTCCTTTGGGGATCTGTCCACTCCTGATGCTGTTATGGGCAACCCTAAG
GTGAAGGCTCATGGCAAGAAAGTGCTCGGTGCCTTTAGTGATGGCCTGGCTCACCTGGAC
AACCTCAAGGGCACCTTTGCCACACTGAGTGAGCTGCACTGTGACAAGCTGCACGTGGAT
CCTGAGAACTTCAGGCTCCTGGGCAACGTGCTGGTCTGTGTGCTGGCCCATCACTTTGGC
AAAGAATTCACCCCACCAGTGCAGGCTGCCTATCAGAAAGTGGTGGCTGGTGTGGCTAAT
GCCCTGGCCCACAAGTATCACTAA
|
| Enzyme 4 GenBank Gene ID |
U01317  |
| Enzyme 4 GeneCard ID |
HBB  |
| Enzyme 4 GenAtlas ID |
HBB  |
| Enzyme 4 HGNC ID |
HGNC:4827  |
| Enzyme 4 Chromosome Location |
11 |
| Enzyme 4 Locus |
11p15.5 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
- Lawn RM, Efstratiadis A, O'Connell C, Maniatis T: The nucleotide sequence of the human beta-globin gene. Cell. 1980 Oct;21(3):647-51. [PubMed
]
- Marotta CA, Forget BG, Cohen-Solal M, Weissman SM: Nucleotide sequence analysis of coding and noncoding regions of human beta-globin mRNA. Prog Nucleic Acid Res Mol Biol. 1976;19:165-75. [PubMed
]
- Lang KM, Spritz RA: Cloning specific complete polyadenylylated 3'-terminal cDNA segments. Gene. 1985;33(2):191-6. [PubMed
]
- Yoshioka N, Atassi MZ: Haemoglobin binding with haptoglobin. Localization of the haptoglobin-binding sites on the beta-chain of human haemoglobin by synthetic overlapping peptides encompassing the entire chain. Biochem J. 1986 Mar 1;234(2):453-6. [PubMed
]
- Bunn HF, Gabbay KH, Gallop PM: The glycosylation of hemoglobin: relevance to diabetes mellitus. Science. 1978 Apr 7;200(4337):21-7. [PubMed
]
- Durner J, Gow AJ, Stamler JS, Glazebrook J: Ancient origins of nitric oxide signaling in biological systems. Proc Natl Acad Sci U S A. 1999 Dec 7;96(25):14206-7. [PubMed
]
- Chan NL, Rogers PH, Arnone A: Crystal structure of the S-nitroso form of liganded human hemoglobin. Biochemistry. 1998 Nov 24;37(47):16459-64. [PubMed
]
- Fermi G: Three-dimensional fourier synthesis of human deoxyhaemoglobin at 2-5 A resolution: refinement of the atomic model. J Mol Biol. 1975 Sep 15;97(2):237-56. [PubMed
]
- Kavanaugh JS, Rogers PH, Case DA, Arnone A: High-resolution X-ray study of deoxyhemoglobin Rothschild 37 beta Trp----Arg: a mutation that creates an intersubunit chloride-binding site. Biochemistry. 1992 Apr 28;31(16):4111-21. [PubMed
]
- Brimhall B, Jones RT, Schneider RG, Hosty TS, Tomlin G, Atkins R: Two new hemoglobins. Hemoglobin Alabama (beta39(C5)Gln leads to Lys) and hemoglobin Montgomery (alpha 48(CD 6) Leu leads to Arg). Biochim Biophys Acta. 1975 Jan 30;379(1):28-32. [PubMed
]
- Molchanova TP, Postnikov YuV, Pobedimskaya DD, Smetanina NS, Moschan AA, Kazanetz EG, Tokarev YuN, Huisman TH: Hb Alesha or alpha 2 beta (2)67(E11)Val-->Met: a new unstable hemoglobin variant identified through sequencing of amplified DNA. Hemoglobin. 1993 Jun;17(3):217-25. [PubMed
]
- Adams JG 3rd, Przywara KP, Heller P, Shamsuddin M: Hemoglobin J Altgeld Gardens. A hemoglobin variant with a substitution of the proximal histidine of the beta-chain. Hemoglobin. 1978;2(5):403-15. [PubMed
]
- Arcasoy A, Casey R, Lehmann H, Cavdar AO, Berki A: A new haemoglobin J from Turkey--Hb Ankara (beta10 (A7) Ala-Asp). FEBS Lett. 1974 Jun 1;42(2):121-3. [PubMed
]
- Huisman TH, Wilson JB, Kutlar A, Yang KG, Chen SS, Webber BB, Altay C, Martinez AV: Hb J-Antakya or alpha 2 beta (2)65(E9)Lys----Met in a Turkish family and Hb complutense or alpha 2 beta (2)127(H5)Gln----Glu in a Spanish family; correction of a previously published identification. Biochim Biophys Acta. 1986 Jun 5;871(2):229-31. [PubMed
]
- Williamson D, Wells RM, Anderson R, Matthews J: A new unstable and low oxygen affinity hemoglobin variant: Hb J-Auckland [beta 25(B7)Gly----Asp]. Hemoglobin. 1987;11(3):221-30. [PubMed
]
- Lafferty J, Ali M, Matthew K, Eng B, Patterson M, Waye JS: Identification of a new high oxygen affinity hemoglobin variant: Hb Aurora [beta 139(H17) Asn-->Tyr] Hemoglobin. 1995;19(6):335-41. [PubMed
]
- Baudin-Chich V, Wajcman H, Gombaud-Saintonge G, Arous N, Riou J, Briere J, Galacteros F: Hemoglobin Brest [beta 127 (H5)Gln----Lys] a new unstable human hemoglobin variant located at the alpha 1 beta 1 interface with specific electrophoretic behavior. Hemoglobin. 1988;12(2):179-88. [PubMed
]
- Brennan SO, Wells RM, Smith H, Carrell RW: Hemoglobin Brisbane: beta68 Leu replaced by His. A new high oxygen affinity variant. Hemoglobin. 1981;5(4):325-35. [PubMed
]
- Como PF, Kennett D, Wilkinson T, Kronenberg H: A new hemoglobin with high oxygen affinity--hemoglobin bunbury: alpha 2 beta 2 [94 (FG1) Asp replaced by Asn] Hemoglobin. 1983;7(5):413-21. [PubMed
]
- Garel MC, Hassan W, Coquelet MT, Goossens M, Rosa J, Arous N: Hemoglobin J Cairo: beta 65 (E9) Lys leads to Gln, A new hemoglobin variant discovered in an Egyptian family. Biochim Biophys Acta. 1976 Jan 20;420(1):97-104. [PubMed
]
- Wilkinson T, Chua CG, Carrell RW, Robin H, Exner T, Lee KM, Kronenberg H: Haemoglobin Camperdown beta104(G6) arginine leads to serine. Biochim Biophys Acta. 1975 May 30;393(1):195-200. [PubMed
]
- Ahern E, Ahern V, Hilton T, Serjeant GR, Serjeant BE, Seakins M, Lang A, Middleton A, Lehmann H: Haemoglobin caribbean beta91 (F7) Leu replaced by Arg: a mildly haemoglobin with a low oxygen affinity. FEBS Lett. 1976 Oct 15;69(1):99-102. [PubMed
]
- Rahbar S, Asmerom Y, Blume KG: A silent hemoglobin variant detected by HPLC: hemoglobin City of Hope beta 69 (E13) Gly----Ser. Hemoglobin. 1984;8(4):333-42. [PubMed
]
- Tamagnini GP, Ribeiro ML, Valente V, Ramachandran M, Wilson JB, Baysal E, Gu LH, Huisman TH: Hb Coimbra or alpha 2 beta (2)99(G1)Asp----Glu, a newly discovered highoxygen affinity variant. Hemoglobin. 1991;15(6):487-96. [PubMed
]
- Rodriguez Romero WE, Castillo M, Chaves MA, Saenz GF, Gu LH, Wilson JB, Baysal E, Smetanina NS, Leonova JY, Huisman TH: Hb Costa Rica or alpha 2 beta 2 77(EF1)His --> Arg: the first example of a somatic cell mutation in a globin gene. Hum Genet. 1996 Jun;97(6):829-33. [PubMed
]
- Lacan P, Kister J, Francina A, Souillet G, Galacteros F, Delaunay J, Wajcman H: Hemoglobin Debrousse (beta 96[FG3]Leu-->Pro): a new unstable hemoglobin with twofold increased oxygen affinity. Am J Hematol. 1996 Apr;51(4):276-81. [PubMed
]
- Bardakdjian-Michau J, Fucharoen S, Delanoe-Garin J, Kister J, Lacombe C, Winichagoon P, Blouquit Y, Riou J, Wasi P, Galacteros F: Hemoglobin Dhonburi alpha 2 beta 2 126 (H4) Val----Gly: a new unstable beta variant producing a beta-thalassemia intermedia phenotype in association with beta zero-thalassemia. Am J Hematol. 1990 Oct;35(2):96-9. [PubMed
]
- Wajcman H, Blouquit Y, Vasseur C, Le Querrec A, Laniece M, Melevendi C, Rasore A, Galacteros F: Two new human hemoglobin variants caused by unusual mutational events: Hb Zaire contains a five residue repetition within the alpha-chain and Hb Duino has two residues substituted in the beta-chain. Hum Genet. 1992 Aug;89(6):676-80. [PubMed
]
- Murru S, Poddie D, Sciarratta GV, Agosti S, Baffico M, Melevendi C, Pirastu M, Cao A: A novel beta-globin structural mutant, Hb Brescia (beta 114 Leu-Pro), causing a severe beta-thalassemia intermedia phenotype. Hum Mutat. 1992;1(2):124-8. [PubMed
]
- de Castro CM, Devlin B, Fleenor DE, Lee ME, Kaufman RE: A novel beta-globin mutation, beta Durham-NC [beta 114 Leu-->Pro], produces a dominant thalassemia-like phenotype. Blood. 1994 Feb 15;83(4):1109-16. [PubMed
]
- Kiger L, Kister J, Groff P, Kalmes G, Prome D, Galacteros F, Wajcman H: Hb J-Europa [beta 62(E6)Ala-->Asp]: normal oxygen binding properties in a new variant involving a residue located distal to the heme. Hemoglobin. 1996 May;20(2):135-40. [PubMed
]
- Como PF, Hocking DR, Swinton GW, Trent RJ, Holland RA, Tibben EA, Wilkinson T, Kronenberg H: Hb Geelong [beta 139(H17)Asn----Asp] Hemoglobin. 1991;15(1-2):85-95. [PubMed
]
- Baklouti F, Giraud Y, Francina A, Richard G, Perier C, Geyssant A, Jaubert J, Brizard C, Delaunay J: Hemoglobin Grange-Blanche [beta 27(B9) Ala----Val], a new variant with normal expression and increased affinity for oxygen. FEBS Lett. 1987 Oct 19;223(1):59-62. [PubMed
]
- Liu JS, Molchanova TP, Gu LH, Wilson JB, Hopmeier P, Schnedl W, Balaun E, Krejs GJ, Huisman TH: Hb Graz or alpha 2 beta 2(2)(NA2)His-->Leu; a new beta chain variant observed in four families from southern Austria. Hemoglobin. 1992;16(6):493-501. [PubMed
]
- Ikkala E, Koskela J, Pikkarainen P, Rahiala EL, El-Hazmi MA, Nagai K, Lang A, Lehmann H: Hb Helsinki: a variant with a high oxygen affinity and a substitution at a 2,3-DPG binding site (beta82[EF6] Lys replaced by Met). Acta Haematol. 1976;56(5):257-75. [PubMed
]
- Ohba Y, Miyaji T, Murakami M, Kadowaki S, Fujita T, Oimomi M, Hatanaka H, Ishikawa K, Baba S, Hitaka K, et al.: Hb Himeji or beta 140 (H18) Ala----Asp. A slightly unstable hemoglobin with increased beta N-terminal glycation. Hemoglobin. 1986;10(2):109-25. [PubMed
]
- Moo-Penn WF, Johnson MH, Jue DL, Lonser R: Hb Hinsdale [beta 139 (H17)Asn----Lys]: a variant in the central cavity showing reduced affinity for oxygen and 2,3-diphosphoglycerate. Hemoglobin. 1989;13(5):455-64. [PubMed
]
- Frischknecht H, Ventruto M, Hess D, Hunziker P, Rosatelli MC, Cao A, Breitenstein U, Fehr J, Tuchschmid P: HB Hinwil or beta 38(C4)Thr-->Asn: a new beta chain variant detected in a Swiss family. Hemoglobin. 1996 Feb;20(1):31-40. [PubMed
]
- Owen MC, Ockelford PA, Wells RM: Hb Howick [beta 37(C3)Trp-->Gly]: a new high oxygen affinity variant of the alpha 1 beta 2 contact. Hemoglobin. 1993 Dec;17(6):513-21. [PubMed
]
- Adams JG, Steinberg MH, Boxer LA, Baehner RL, Forget BG, Tsistrakis GA: The structure of hemoglobin Indianapolis [beta112(G14) arginine]. An unstable variant detectable only by isotopic labeling. J Biol Chem. 1979 May 10;254(9):3479-82. [PubMed
]
- Harano T, Harano K, Kushida Y, Ueda S, Yoshii A, Nishinarita M: Hb Isehara (or Hb Redondo) [beta 92 (F8) His----Asn]: an unstable variant with a proximal histidine substitution at the heme contact. Hemoglobin. 1991;15(4):279-90. [PubMed
]
- Aksoy M, Erdem S, Efremov GD, Wilson JB, Huisman TH, Schroeder WA, Shelton JR, Shelton JB, Ulitin ON, Muftuoglu A: Hemoglobin Istanbul: substitution of glutamine for histidine in a proximal histidine (F8(92) ). J Clin Invest. 1972 Sep;51(9):2380-7. [PubMed
]
- Gaudry CL Jr, Pitel PA, Jue DL, Hine TK, Johnson MH, Moo-Penn WF: Hb Jacksonville [alpha 2 beta 2(54)(D5)Val----Asp]: a new unstable variant found in a patient with hemolytic anemia. Hemoglobin. 1990;14(6):653-9. [PubMed
]
- Lu YQ, Fan JL, Liu JF, Hu HL, Peng XH, Huang CH, Huang PY, Chen SS, Jai PC, Yang KG, et al.: Hemoglobin Jianghua [beta 120(GH3) LYS leads to ILE]: a new fast-moving variant found in China. Hemoglobin. 1983;7(4):321-6. [PubMed
]
- Landin B: Hb Karlskoga or alpha 2 beta (2)21(B3) Asp-->His: a new slow-moving variant found in Sweden. Hemoglobin. 1993 Jun;17(3):201-8. [PubMed
]
- Arous N, Galacteros F, Fessas P, Loukopoulos D, Blouquit Y, Komis G, Sellaye M, Boussiou M, Rosa J: Structural study of hemoglobin Knossos, beta 27 (B9) Ala leads to Ser. A new abnormal hemoglobin present as a silent beta-thalassemia. FEBS Lett. 1982 Oct 18;147(2):247-50. [PubMed
]
- Harano T, Harano K, Kushida Y, Imai K, Nishinakamura R, Matsunaga T: Hb Kodaira [beta 146(HC3)His----Gln]: a new beta chain variant with an amino acid substitution at the C-terminus. Hemoglobin. 1992;16(1-2):85-91. [PubMed
]
- Harano T, Harano K, Ueda S, Imai N, Kitazumi T: A new electrophoretically-silent hemoglobin variant: hemoglobin Kofu or alpha 2 beta 2 84 (EF8) Thr----Ile. Hemoglobin. 1986;10(4):417-20. [PubMed
]
- Divoky V, Svobodova M, Indrak K, Chrobak L, Molchanova TP, Huisman TH: Hb Hradec Kralove (Hb HK) or alpha 2 beta 2 115(G17)Ala-->Asp, a severely unstable hemoglobin variant resulting in a dominant beta-thalassemia trait in a Czech family. Hemoglobin. 1993 Aug;17(4):319-28. [PubMed
]
- Merault G, Keclard L, Garin J, Poyart C, Blouquit Y, Arous N, Galacteros F, Feingold J, Rosa J: Hemoglobin La Desirade alpha A2 beta 2 129 (H7) Ala----Val: a new unstable hemoglobin. Hemoglobin. 1986;10(6):593-605. [PubMed
]
- Wajcman H, Kister J, Vasseur C, Blouquit Y, Trastour JC, Cottenceau D, Galacteros F: Structure of the EF corner favors deamidation of asparaginyl residues in hemoglobin: the example of Hb La Roche-sur-Yon [beta 81 (EF5) Leu----His] Biochim Biophys Acta. 1992 Feb 14;1138(2):127-32. [PubMed
]
- Malcorra-Azpiazu JJ, Balda-Aguirre MI, Diaz-Chico JC, Hu H, Wilson JB, Webber BB, Kutlar F, Kutlar A, Huisman TH: Hb Las Palmas or alpha 2 beta 2(49)(CD8)Ser----Phe, a mildly unstable hemoglobin variant. Hemoglobin. 1988;12(2):163-70. [PubMed
]
- Berlin G, Wranne B, Jeppsson JO: Hb Linkoping (beta 36 Pro----Thr): a new high oxygen affinity hemoglobin variant found in two families of Finnish origin. Eur J Haematol. 1987 Nov;39(5):452-6. [PubMed
]
- Marinucci M, Boissel JP, Massa A, Wajcman H, Tentori L, Labie D: Hemoglobin Maputo: a new beta-chain variant (alpha 2 beta 2 47 (CD6) Asp replaced by Tyr) in combination with hemoglobin S, identified by high performance liquid chromatography (HPLC). Hemoglobin. 1983;7(5):423-33. [PubMed
]
- Sciarratta GV, Ivaldi G: Hb Matera [beta 55(D6)Met----Lys]: a new unstable hemoglobin variant in an Italian family. Hemoglobin. 1990;14(1):79-85. [PubMed
]
- Nakatsuji T, Miwa S, Ohba Y, Hattori Y, Miyaji T, Miyata H, Shinohara T, Hori T, Takayama J: Hemoglobin Miyashiro (beta 23[B5] val substituting for gly) an electrophoretically silent variant discovered by the isopropanol test. Hemoglobin. 1981;5(7-8):653-66. [PubMed
]
- Ohba Y, Miyaji T, Matsuoka M, Sugiyama K, Suzuki T, Sugiura T: Hemoglobin Mizuho or beta 68 (E 12) leucine leads to proline, a new unstable variant associated with severe hemolytic anemia. Hemoglobin. 1977;1(5):467-77. [PubMed
]
- Ramachandran M, Gu LH, Wilson JB, Kitundu MN, Adekile AD, Liu JC, McKie KM, Huisman TH: A new variant, HB Muscat [alpha 2 beta (2)32(B14)Leu----Val] observed in association with HB S in an Arabian family. Hemoglobin. 1992;16(4):259-66. [PubMed
]
- Lena-Russo D, Orsini A, Vovan L, Bardakdjian-Michau J, Lacombe C, Blouquit Y, Craescu CT, Galacteros F: Hb N-Timone [alpha 2 beta 2(8)(A5)Lys----Glu]: a new fast-moving variant with normal stability and oxygen affinity. Hemoglobin. 1989;13(7-8):743-7. [PubMed
]
- Ohba Y, Imanaka M, Matsuoka M, Hattori Y, Miyaji T, Funaki C, Shibata K, Shimokata H, Kuzuya F, Miwa S: A new unstable, high oxygen affinity hemoglobin: Hb Nagoya or beta 97 (FG4) His----Pro. Hemoglobin. 1985;9(1):11-24. [PubMed
]
- Welch SG, Bateman C: Hb D-Neath or beta 121 (GH4) Glu-->Ala: a new member of the Hb D family. Hemoglobin. 1993 Jun;17(3):255-9. [PubMed
]
- Rahbar S, Louis J, Lee T, Asmerom Y: Hemoglobin North Chicago (beta 36 [C2] proline----serine): a new high affinity hemoglobin. Hemoglobin. 1985;9(6):559-76. [PubMed
]
- Arends T, Lehmann H, Plowman D, Stathopoulou R: Haemoglobin North Shore-Caracas beta 134 (H12) valine replaced by glutamic acid. FEBS Lett. 1977 Aug 15;80(2):261-5. [PubMed
]
- Indrak K, Wiedermann BF, Batek F, Wilson JB, Webber BB, Kutlar A, Huisman TH: Hb Olomouc or alpha 2 beta 2(86)(F2)Ala----Asp, a new high oxygen affinity variant. Hemoglobin. 1987;11(2):151-5. [PubMed
]
- Brennan SO, Williamson D, Whisson ME, Carrell RW: Hemoglobin Palmerston North beta 23 (B5) Val replaced by Phe. A new variant identified in a patient with polycythemia. Hemoglobin. 1982;6(6):569-75. [PubMed
]
- Baklouti F, Giraud Y, Francina A, Richard G, Favre-Gilly J, Delaunay J: Hemoglobin Pierre-Benite [beta 90(F6)Glu----Asp], a new high affinity variant found in a French family. Hemoglobin. 1988;12(2):171-7. [PubMed
]
- Moo-Penn WF, Wolff JA, Simon G, Vacek M, Jue DL, Johnson MH: Hemoglobin Presbyterian: beta108 (G10) asparagine leads to lysine, A hemoglobin variant with low oxygen affinity. FEBS Lett. 1978 Aug 1;92(1):53-6. [PubMed
]
- Wajcman H, Girodon E, Prome D, North ML, Plassa F, Duwig I, Kister J, Bergerat JP, Oberling F, Lampert E, et al.: Germline mosaicism for an alanine to valine substitution at residue beta 140 in hemoglobin Puttelange, a new variant with high oxygen affinity. Hum Genet. 1995 Dec;96(6):711-6. [PubMed
]
- Jen PC, Chen LC, Chen PF, Wong Y, Chen LF, Guo YY, Chang FQ, Chow YC, Chiu Y: Hemoglobin Quin-Hai, beta 78 (EF2) Leu replaced by Arg, a new abnormal hemoglobin found in Guangdong, China. Hemoglobin. 1983;7(5):407-12. [PubMed
]
- Bisse E, Zorn N, Eigel A, Lizama M, Huaman-Guillen P, Marz W, Van Dorsselaer A, Wieland H: Hemoglobin Rambam (beta69[E13]Gly-->Asp), a pitfall in the assessment of diabetic control: characterization by electrospray mass spectrometry and HPLC. Clin Chem. 1998 Oct;44(10):2172-7. [PubMed
]
- Gilbert AT, Fleming PJ, Sumner DR, Hughes WG, Ip F, Kwan YL, Holland RA: Hemoglobin Randwick or beta 15 (A12)Trp----Gly: a new unstable beta-chain hemoglobin variant. Hemoglobin. 1988;12(2):149-61. [PubMed
]
- Moo-Penn WF, Johnson MH, McGuffey JE, Jue DL, Therrell BL Jr: Hemoglobin Rio Grande [beta 8 (A5) Lys leads to Thr] a new variant found in a Mexican-American family. Hemoglobin. 1983;7(1):91-5. [PubMed
]
- Adams JG 3rd, Winter WP, Tausk K, Heller P: Hemoglobin Rush (beta 101 (g3) glutamine): a new unstable hemoglobin causing mild hemolytic anemia. Blood. 1974 Feb;43(2):261-9. [PubMed
]
- Ohba Y, Hasegawa Y, Amino H, Miwa S, Nakatsuji T, Hattori Y, Miyaji T: Hemoglobin saitama or beta 117 (G19) His leads to Pro, a new variant causing hemolytic disease. Hemoglobin. 1983;7(1):47-56. [PubMed
]
- Moo-Penn WF, Johnson MH, McGuffey JE, Jue DL: Hemoglobin Shelby [beta 131(H9) Gln----Lys] a correction to the structure of hemoglobin Deaconess and hemoglobin Leslie. Hemoglobin. 1984;8(6):583-93. [PubMed
]
- Ricco G, Pich PG, Mazza U, Rossi G, Ajmar F, Arese P, Gallo E: Hb J Sicilia: beta 65 (E9) Lys-Asn, a beta homologue of Hb Zambia. FEBS Lett. 1974 Feb 15;39(2):200-4. [PubMed
]
- Como PF, Wylie BR, Trent RJ, Bruce D, Volpato F, Wilkinson T, Kronenberg H, Holland RA, Tibben EA: A new unstable and low oxygen affinity hemoglobin variant: Hb Stanmore [beta 111(G13)Val----Ala] Hemoglobin. 1991;15(1-2):53-65. [PubMed
]
- Arous N, Braconnier F, Thillet J, Blouquit Y, Galacteros F, Chevrier M, Bordahandy C, Rosa J: Hemoglobin Saint Mande beta 102 (G4) asn replaced by tyr: a new low oxygen affinity variant. FEBS Lett. 1981 Apr 6;126(1):114-6. [PubMed
]
- Gilbert AT, Fleming PJ, Sumner DR, Hughes WG, Holland RA, Tibben EA: Hemoglobin Windsor or beta 11 (A8)Val----Asp: a new unstable beta-chain hemoglobin variant producing a hemolytic anemia. Hemoglobin. 1989;13(5):437-53. [PubMed
]
- Harano T, Harano K, Kushida Y, Ueda S: A new abnormal variant, Hb Yahata or beta 112(G14)Cys----Tyr, found in a Japanese: structural confirmation by DNA sequencing of the beta-globin gene. Hemoglobin. 1991;15(1-2):109-13. [PubMed
]
- Nakatsuji T, Miwa S, Ohba Y, Hattori Y, Miyaji T, Hino S, Matsumoto N: A new unstable hemoglobin, Hb Yokohama beta 31 (B13)Leu substituting for Pro, causing hemolytic anemia. Hemoglobin. 1981;5(7-8):667-78. [PubMed
]
- Plaseska D, Wilson JB, Gu LH, Kutlar F, Huisman TH, Zeng YT, Shen M: Hb Zengcheng or alpha 2 beta(2)114(G16)Leu----Met. Hemoglobin. 1990;14(5):555-7. [PubMed
]
|
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
7570 |
| Enzyme 5 Name |
Endothelin-1 precursor |
| Enzyme 5 Synonyms |
- Preproendothelin-1
- PPET1[Contains: Endothelin-1
- ET-1
- Big endothelin-1]
|
| Enzyme 5 Gene Name |
EDN1 |
| Enzyme 5 Protein Sequence |
>Endothelin-1 precursor
MDYLLMIFSLLFVACQGAPETAVLGAELSAVGENGGEKPTPSPPWRLRRSKRCSCSSLMD
KECVYFCHLDIIWVNTPEHVVPYGLGSPRSKRALENLLPTKATDRENRCQCASQKDKKCW
NFCQAGKELRAEDIMEKDWNNHKKGKDCSKLGKKCIYQQLVRGRKIRRSSEEHLRQTRSE
TMRNSVKSSFHDPKLKGKPSRERYVTHNRAHW
|
| Enzyme 5 Number of Residues |
212 |
| Enzyme 5 Molecular Weight |
24425 |
| Enzyme 5 Theoretical pI |
9.92 |
| Enzyme 5 GO Classification |
| Function |
| — |
| Process |
- interaction between organisms
- interspecies interaction between organisms
- pathogenesis
- regulation of biological process
- regulation of organismal physiological process
- regulation of physiological process
- regulation of vasoconstriction
- symbiosis, encompassing mutualism through parasitism
|
| Component |
|
|
| Enzyme 5 General Function |
Not Available |
| Enzyme 5 Specific Function |
Endothelins are endothelium-derived vasoconstrictor peptides |
| Enzyme 5 Pathways |
Not Available |
| Enzyme 5 Reactions |
Not Available |
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
Not Available |
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
31255  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
P05305  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
EDN1_HUMAN  |
| Enzyme 5 PDB ID |
Not Available |
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>639 bp
ATGGATTATTTGCTCATGATTTTCTCTCTGCTGTTTGTGGCTTGCCAAGGAGCTCCAGAA
ACAGCAGTCTTAGGCGCTGAGCTCAGCGCGGTGGGTGAGAACGGCGGGGAGAAACCCACT
CCCAGTCCACCCTGGCGGCTCCGCCGGTCCAAGCGCTGCTCCTGCTCGTCCCTGATGGAT
AAAGAGTGTGTCTACTTCTGCCACCTGGACATCATTTGGGTCAACACTCCCGAGCACGTT
GTTCCGTATGGACTTGGAAGCCCTAGGTCCAAGAGAGCCTTGGAGAATTTACTTCCCACA
AAGGCAACAGACCGTGAGAATAGATGCCAATGTGCTAGCCAAAAAGACAAGAAGTGCTGG
AATTTTTGCCAAGCAGGAAAAGAACTCAGGGCTGAAGACATTATGGAGAAAGACTGGAAT
AATCATAAGAAAGGAAAAGACTGTTCCAAGCTTGGGAAAAAGTGTATTTATCAGCAGTTA
GTGAGAGGAAGAAAAATCAGAAGAAGTTCAGAGGAACACCTAAGACAAACCAGGTCGGAG
ACCATGAGAAACAGCGTCAAATCATCTTTTCATGATCCCAAGCTGAAAGGCAAGCCCTCC
AGAGAGCGTTATGTGACCCACAACCGAGCACATTGGTGA
|
| Enzyme 5 GenBank Gene ID |
Y00749  |
| Enzyme 5 GeneCard ID |
EDN1  |
| Enzyme 5 GenAtlas ID |
EDN1  |
| Enzyme 5 HGNC ID |
HGNC:3176  |
| Enzyme 5 Chromosome Location |
6 |
| Enzyme 5 Locus |
6p24.1 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- Itoh Y, Yanagisawa M, Ohkubo S, Kimura C, Kosaka T, Inoue A, Ishida N, Mitsui Y, Onda H, Fujino M, et al.: Cloning and sequence analysis of cDNA encoding the precursor of a human endothelium-derived vasoconstrictor peptide, endothelin: identity of human and porcine endothelin. FEBS Lett. 1988 Apr 25;231(2):440-4. [PubMed
]
- Inoue A, Yanagisawa M, Takuwa Y, Mitsui Y, Kobayashi M, Masaki T: The human preproendothelin-1 gene. Complete nucleotide sequence and regulation of expression. J Biol Chem. 1989 Sep 5;264(25):14954-9. [PubMed
]
- Bloch KD, Friedrich SP, Lee ME, Eddy RL, Shows TB, Quertermous T: Structural organization and chromosomal assignment of the gene encoding endothelin. J Biol Chem. 1989 Jun 25;264(18):10851-7. [PubMed
]
- Benatti L, Bonecchi L, Cozzi L, Sarmientos P: Two preproendothelin 1 mRNAs transcribed by alternative promoters. J Clin Invest. 1993 Mar;91(3):1149-56. [PubMed
]
- Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed
]
- Inoue A, Yanagisawa M, Kimura S, Kasuya Y, Miyauchi T, Goto K, Masaki T: The human endothelin family: three structurally and pharmacologically distinct isopeptides predicted by three separate genes. Proc Natl Acad Sci U S A. 1989 Apr;86(8):2863-7. [PubMed
]
- Fabbrini MS, Valsasina B, Nitti G, Benatti L, Vitale A: The signal peptide of human preproendothelin-1. FEBS Lett. 1991 Jul 29;286(1-2):91-4. [PubMed
]
- Bourgeois C, Robert B, Rebourcet R, Mondon F, Mignot TM, Duc-Goiran P, Ferre F: Endothelin-1 and ETA receptor expression in vascular smooth muscle cells from human placenta: a new ETA receptor messenger ribonucleic acid is generated by alternative splicing of exon 3. J Clin Endocrinol Metab. 1997 Sep;82(9):3116-23. [PubMed
]
- Wolff M, Day J, Greenwood A, Larson S, McPherson A: Crystallization and preliminary X-ray analysis of human endothelin. Acta Crystallogr B. 1992 Apr 1;48 ( Pt 2):239-40. [PubMed
]
- Janes RW, Peapus DH, Wallace BA: The crystal structure of human endothelin. Nat Struct Biol. 1994 May;1(5):311-9. [PubMed
]
- Reily MD, Dunbar JB Jr: The conformation of endothelin-1 in aqueous solution: NMR-derived constraints combined with distance geometry and molecular dynamics calculations. Biochem Biophys Res Commun. 1991 Jul 31;178(2):570-7. [PubMed
]
- Andersen NH, Chen CP, Marschner TM, Krystek SR Jr, Bassolino DA: Conformational isomerism of endothelin in acidic aqueous media: a quantitative NOESY analysis. Biochemistry. 1992 Feb 11;31(5):1280-95. [PubMed
]
- Donlan ML, Brown FK, Jeffs PW: Solution conformation of human big endothelin-1. J Biomol NMR. 1992 Sep;2(5):407-20. [PubMed
]
- Wallace BA, Janes RW, Bassolino DA, Krystek SR Jr: A comparison of X-ray and NMR structures for human endothelin-1. Protein Sci. 1995 Jan;4(1):75-83. [PubMed
]
- Hewage CM, Jiang L, Parkinson JA, Ramage R, Sadler IH: Solution structure of a novel ETB receptor selective agonist ET1-21 [Cys(Acm)1,15, Aib3,11, Leu7] by nuclear magnetic resonance spectroscopy and molecular modelling. J Pept Res. 1999 Mar;53(3):223-33. [PubMed
]
- Tiret L, Poirier O, Hallet V, McDonagh TA, Morrison C, McMurray JJ, Dargie HJ, Arveiler D, Ruidavets JB, Luc G, Evans A, Cambien F: The Lys198Asn polymorphism in the endothelin-1 gene is associated with blood pressure in overweight people. Hypertension. 1999 May;33(5):1169-74. [PubMed
]
- Halushka MK, Fan JB, Bentley K, Hsie L, Shen N, Weder A, Cooper R, Lipshutz R, Chakravarti A: Patterns of single-nucleotide polymorphisms in candidate genes for blood-pressure homeostasis. Nat Genet. 1999 Jul;22(3):239-47. [PubMed
]
|
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
15242 |
| Enzyme 6 Name |
Nitric oxide synthase 2A (Inducible, hepatocytes) |
| Enzyme 6 Synonyms |
Not Available |
| Enzyme 6 Gene Name |
NOS2A |
| Enzyme 6 Protein Sequence |
>Nitric oxide synthase 2A (Inducible, hepatocytes)
MACPWKFLFKTKFHQYAMNGEKDINNNVEKAPCATSSPVTQDDLQYHNLSKQQNESPQPL
VETGKKSPESLVKLDATPLSSPRHVRIKNWGSGMTFQDTLHHKAKGILTCRSKSCLGSIM
TPKSLTRGPRDKPTPPDELLPQAIEFVNQYYGSFKEAKIEEHLARVEAVTKEIETTGTYQ
LTGDELIFATKQAWRNAPRCIGRIQWSNLQVFDARSCSTAREMFEHICRHVRYSTNNGNI
RSAITVFPQRSDGKHDFRVWNAQLIRYAGYQMPDGSIRGDPANVEFTQLCIDLGWKPKYG
RFDVVPLVLQANGRDPELFEIPPDLVLEVAMEHPKYEWFRELELKWYALPAVANMLLEVG
GLEFPGCPFNGWYMGTEIGVRDFCDVQRYNILEEVGRRMGLETHKLASLWKDQAVVEINI
AVLHSFQKQNVTIMDHHSAAESFMKYMQNEYRSRGGCPADWIWLVPPMSGSITPVFHQEM
LNYVLSPFYYYQVEAWKTHVWQDEKRRPKRREIPLKVLVKAVLFACMLMRKTMASRVRVT
ILFATETGKSEALAWDLGALFSCAFNPKVVCMDKYRLSCLEEERLLLVVTSTFGNGDCPG
NGEKLKKSLFMLKELNNKFRYAVFGLGSSMYPRFCAFAHDIDQKLSHLGASQLTPMGEGD
ELSGQEDAFRSWAVQTFKAACETFDVRGKQHIQIPKLYTSNVTWDPHHYRLVQDSQPLDL
SKALSSMHAKNVFTMRLKSRQNLQSPTSSRATILVELSCEDGQGLNYLPGEHLGVCPGNQ
PALVQGILERVVDGPTPHQTVRLEALDESGSYWVSDKRLPPCSLSQALTYFLDITTPPTQ
LLLQKLAQVATEEPERQRLEALCQPSEYSKWKFTNSPTFLEVLEEFPSLRVSAGFLLSQL
PILKPRFYSISSSRDHTPTEIHLTVAVVTYHTRDGQGPLHHGVCSTWLNSLKPQDPVPCF
VRNASGFHLPEDPSHPCILIGPGTGIAPFRSFWQQRLHDSQHKGVRGGRMTLVFGCRRPD
EDHIYQEEMLEMAQKGVLHAVHTAYSRLPGKPKVYVQDILRQQLASEVLRVLHKEPGHLY
VCGDVRMARDVAHTLKQLVAAKLKLNEEQVEDYFFQLKSQKRYHEDIFGAVFPYEAKKDR
VAVQPSSLEMSAL
|
| Enzyme 6 Number of Residues |
1153 |
| Enzyme 6 Molecular Weight |
131119 |
| Enzyme 6 Theoretical pI |
8.01 |
| Enzyme 6 GO Classification |
| Function |
- FAD binding
- FMN binding
- NADP binding
- adenyl nucleotide binding
- binding
- calmodulin binding
- catalytic activity
- cation binding
- coenzyme binding
- cofactor binding
- electron transporter activity
- heme binding
- ion binding
- iron ion binding
- monooxygenase activity
- nitric-oxide synthase activity
- nucleotide binding
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD or NADH as one donor, and incorporation of one atom of oxygen
- protein binding
- purine nucleotide binding
- tetrapyrrole binding
- transition metal ion binding
- transporter activity
|
| Process |
- biosynthesis
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- nitric oxide biosynthesis
- physiological process
|
| Component |
| — |
|
| Enzyme 6 General Function |
Inorganic ion transport and metabolism |
| Enzyme 6 Specific Function |
Not Available |
| Enzyme 6 Pathways |
Not Available |
| Enzyme 6 Reactions |
Not Available |
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
120660146  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
A1L3U5  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
A1L3U5_HUMAN  |
| Enzyme 6 PDB ID |
2NSI  |
| Enzyme 6 PDB File |
Show |
| Enzyme 6 3D Structure |
|
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
>3462 bp
ATGGCCTGTCCTTGGAAATTTCTGTTCAAGACCAAATTCCACCAGTATGCAATGAATGGG
GAAAAAGACATCAACAACAATGTGGAGAAAGCCCCCTGTGCCACCTCCAGTCCAGTGACA
CAGGATGACCTTCAGTATCACAACCTCAGCAAGCAGCAGAATGAGTCCCCGCAGCCCCTC
GTGGAGACGGGAAAGAAGTCTCCAGAATCTCTGGTCAAGCTGGATGCAACCCCATTGTCC
TCCCCACGGCATGTGAGGATCAAAAACTGGGGCAGCGGGATGACTTTCCAAGACACACTT
CACCATAAGGCCAAAGGGATTTTAACTTGCAGGTCCAAATCTTGCCTGGGGTCCATTATG
ACTCCCAAAAGTTTGACCAGAGGACCCAGGGACAAGCCTACCCCTCCAGATGAGCTTCTA
CCTCAAGCTATCGAATTTGTCAACCAATATTACGGCTCCTTCAAAGAGGCAAAAATAGAG
GAACATCTGGCCAGGGTGGAAGCGGTAACAAAGGAGATAGAAACAACAGGAACCTACCAA
CTGACGGGAGATGAGCTCATCTTCGCCACCAAGCAGGCCTGGCGCAATGCCCCACGCTGC
ATTGGGAGGATCCAGTGGTCCAACCTGCAGGTCTTCGATGCCCGCAGCTGTTCCACTGCC
CGGGAAATGTTTGAACACATCTGCAGACACGTGCGTTACTCCACCAACAATGGCAACATC
AGGTCGGCCATCACCGTGTTCCCCCAGCGGAGTGATGGCAAGCACGACTTCCGGGTGTGG
AATGCTCAGCTCATCCGCTATGCTGGCTACCAGATGCCAGATGGCAGCATCAGAGGGGAC
CCTGCCAACGTGGAATTCACTCAGCTGTGCATCGACCTGGGCTGGAAGCCCAAGTACGGC
CGCTTCGATGTGGTCCCCCTGGTCCTGCAGGCCAATGGCCGTGACCCTGAGCTCTTCGAA
ATCCCACCTGACCTTGTGCTTGAGGTGGCCATGGAACATCCCAAATACGAGTGGTTTCGG
GAACTGGAGCTAAAGTGGTACGCCCTGCCTGCAGTGGCCAACATGCTGCTTGAGGTGGGC
GGCCTGGAGTTCCCAGGGTGCCCCTTCAATGGCTGGTACATGGGCACAGAGATCGGAGTC
CGGGACTTCTGTGACGTCCAGCGCTACAACATCCTGGAGGAAGTGGGCAGGAGAATGGGC
CTGGAAACGCACAAGCTGGCCTCGCTCTGGAAAGACCAGGCTGTCGTTGAGATCAACATT
GCTGTGCTCCATAGTTTCCAGAAGCAGAATGTGACCATCATGGACCACCACTCGGCTGCA
GAATCCTTCATGAAGTACATGCAGAATGAATACCGGTCCCGTGGGGGCTGCCCGGCAGAC
TGGATTTGGCTGGTCCCTCCCATGTCTGGGAGCATCACCCCCGTGTTTCACCAGGAGATG
CTGAACTACGTCCTGTCCCCTTTCTACTACTATCAGGTAGAGGCCTGGAAAACCCATGTC
TGGCAGGACGAGAAGCGGAGACCCAAGAGAAGAGAGATTCCATTGAAAGTCTTGGTCAAA
GCTGTGCTCTTTGCCTGTATGCTGATGCGCAAGACAATGGCGTCCCGAGTCAGAGTCACC
ATCCTCTTTGCGACAGAGACAGGAAAATCAGAGGCGCTGGCCTGGGACCTGGGGGCCTTA
TTCAGCTGTGCCTTCAACCCCAAGGTTGTCTGCATGGATAAGTACAGGCTGAGCTGCCTG
GAGGAGGAACGGCTGCTGTTGGTGGTGACCAGTACGTTTGGCAATGGAGACTGCCCTGGC
AATGGAGAGAAACTGAAGAAATCGCTCTTCATGCTGAAAGAGCTCAACAACAAATTCAGG
TACGCTGTGTTTGGCCTCGGCTCCAGCATGTACCCTCGGTTCTGCGCCTTTGCTCATGAC
ATTGATCAGAAGCTGTCCCACCTGGGGGCCTCTCAGCTCACCCCGATGGGAGAAGGGGAT
GAGCTCAGTGGGCAGGAGGACGCCTTCCGCAGCTGGGCCGTGCAAACCTTCAAGGCAGCC
TGTGAGACGTTTGATGTCCGAGGCAAACAGCACATTCAGATCCCCAAGCTCTACACCTCC
AATGTGACCTGGGACCCGCACCACTACAGGCTCGTGCAGGACTCACAGCCTTTGGACCTC
AGCAAAGCCCTCAGCAGCATGCATGCCAAGAACGTGTTCACCATGAGGCTCAAATCTCGG
CAGAATCTACAAAGTCCGACATCCAGCCGTGCCACCATCCTGGTGGAACTCTCCTGTGAG
GATGGCCAAGGCCTGAACTACCTGCCGGGGGAGCACCTTGGGGTTTGCCCAGGCAACCAG
CCGGCCCTGGTCCAAGGCATCCTGGAGCGAGTGGTGGATGGCCCCACACCCCACCAGACA
GTGCGCCTGGAGGCCCTGGATGAGAGTGGCAGCTACTGGGTCAGTGACAAGAGGCTGCCC
CCCTGCTCACTCAGCCAGGCCCTCACCTACTTCCTGGACATCACCACACCCCCAACCCAG
CTGCTGCTCCAAAAGCTGGCCCAGGTGGCCACAGAAGAGCCTGAGAGACAGAGGCTGGAG
GCCCTGTGCCAGCCCTCAGAGTACAGCAAGTGGAAGTTCACCAACAGCCCCACATTCCTG
GAGGTGCTAGAGGAGTTCCCGTCCCTGCGGGTGTCTGCTGGCTTCCTGCTTTCCCAGCTC
CCCATTCTGAAGCCCAGGTTCTACTCCATCAGCTCCTCCCGGGATCACACGCCCACGGAG
ATCCACCTGACTGTGGCCGTGGTCACCTACCACACCCGAGATGGCCAGGGTCCCCTGCAC
CACGGCGTCTGCAGCACATGGCTCAACAGCCTGAAGCCCCAAGACCCAGTGCCCTGCTTT
GTGCGGAATGCCAGCGGCTTCCACCTCCCCGAGGATCCCTCCCATCCTTGCATCCTCATC
GGGCCTGGCACAGGCATCGCGCCCTTCCGCAGTTTCTGGCAGCAACGGCTCCATGACTCC
CAGCACAAGGGAGTGCGGGGAGGCCGCATGACCTTGGTGTTTGGGTGCCGCCGCCCAGAT
GAGGACCACATCTACCAGGAGGAGATGCTGGAGATGGCCCAGAAGGGGGTGCTGCATGCG
GTGCACACAGCCTATTCCCGCCTGCCTGGCAAGCCCAAGGTCTATGTTCAGGACATCCTG
CGGCAGCAGCTGGCCAGCGAGGTGCTCCGTGTGCTCCACAAGGAGCCAGGCCACCTCTAT
GTTTGCGGGGATGTGCGCATGGCCCGGGACGTGGCCCACACCCTGAAGCAGCTGGTGGCT
GCCAAGCTGAAATTGAATGAGGAGCAGGTCGAGGACTATTTCTTTCAGCTCAAGAGCCAG
AAGCGCTATCACGAAGATATCTTTGGTGCTGTATTTCCTTACGAGGCGAAGAAGGACAGG
GTGGCGGTGCAGCCCAGCAGCCTGGAGATGTCAGCGCTCTGA
|
| Enzyme 6 GenBank Gene ID |
BC130283  |
| Enzyme 6 GeneCard ID |
A1L3U5  |
| Enzyme 6 GenAtlas ID |
Not Available |
| Enzyme 6 HGNC ID |
Not Available |
| Enzyme 6 Chromosome Location |
17 |
| Enzyme 6 Locus |
17q11.2-q12 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed
]
|
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
16523 |
| Enzyme 7 Name |
NOS1 mutant (Nitric oxide synthase 1 (Neuronal), isoform CRA_c) |
| Enzyme 7 Synonyms |
Not Available |
| Enzyme 7 Gene Name |
NOS1 |
| Enzyme 7 Protein Sequence |
>NOS1 mutant (Nitric oxide synthase 1 (Neuronal), isoform CRA_c)
MEDHMFGVQQIQPNVISVRLFKRKVGGLGFLVKERVSKPPVIISDLIRGGAAEQSGLIQA
GDIILAVNGRPLVDLSYDSALEVLRGIASETHVVLILRGPEGFTTHLETTFTGDGTPKTI
RVTQPLGPPTKAVDLSHQPPAGKEQPLAVDGASGPGNGPQHAYDDGQEAGSLPHANGLAP
RPPGQDPAKKATRVSLQGRGENNELLKEIEPVLSLLTSGSRGVKGGAPAKAEMKDMGIQV
DRDLDGKSHKPLPLGVENDRVFNDLWGKGNVPVVLNNPYSEKEQPPTSGKQSPTKNGSPS
KCPRFLKVKNWETEVVLTDTLHLKSTLETGCTEYICMGSIMHPSQHARRPEDVRTKGQLF
PLAKEFIDQYYSSIKRFGSKAHMERLEEVNKEIDTTSTYQLKDTELIYGAKHAWRNASRC
VGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLRSAITIFPQRTDGKHDFRVW
NSQLIRYAGYKQPDGSTLGDPANVQFTEICIQQGWKPPRGRFDVLPLLLQANGNDPELFQ
IPPELVLEVPIRHPKFEWFKDLGLKWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGV
RDYCDNSRYNILEEVAKKMNLDMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSAT
ESFIKHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEMLNYRLTPSFEYQPDPWNTHV
WKGTNGTPTKRRAIGFKKLAEAVKFSAKLMGQAMAKRVKATILYATETGKSQAYAKTLCE
IFKHAFDAKVMSMEEYDIVHLEHETLVLVVTSTFGNGDPPENGEKFGCALMEMRHPNSVQ
EERKSYKVRFNSVSSYSDSQKSSGDGPDLRDNFESAGPLANVRFSVFGLGSRAYPHFCAF
GHAVDTLLEELGGERILKMREGDELCGQEEAFRTWAKKVFKAACDVFCVGDDVNIEKANN
SLISNDRSWKRNKFRLTFVAEAPELTQGLSNVHKKRVSAARLLSRQNLQSPKSSRSTIFV
RLHTNGSQELQYQPGDHLGVFPGNHEDLVNALIERLEDAPPVNQMVKVELLEERNTALGV
ISNWTDELRLPPCTIFQAFKYYLDITTPPTPLQLQQFASLATSEKEKQRLLVLSKGLQEY
EEWKWGKNPTIVEVLEEFPSIQMPATLLLTQLSLLQPRYYSISSSPDMYPDEVHLTVAIV
SYRTRDGEGPIHHGVCSSWLNRIQADELVPCFVRGAPSFHLPRNPQVPCILVGPGTGIAP
FRSFWQQRQFDIQHKGMNPCPMVLVFGCRQSKIDHIYREETLQAKNKGVFRELYTAYSRE
PDKPKKYVQDILQEQLAESVYRALKEQGGHIYVCGDVTMAADVLKAIQRIMTQQGKLSAE
DAGVFISRMRDDNRYHEDIFGVTLRTYEVTNRLRSESIAFIEESKKDTDEVFSS
|
| Enzyme 7 Number of Residues |
1434 |
| Enzyme 7 Molecular Weight |
160972 |
| Enzyme 7 Theoretical pI |
7.44 |
| Enzyme 7 GO Classification |
| Function |
- FAD binding
- FMN binding
- NADP binding
- adenyl nucleotide binding
- binding
- calmodulin binding
- catalytic activity
- cation binding
- coenzyme binding
- cofactor binding
- electron transporter activity
- heme binding
- ion binding
- iron ion binding
- monooxygenase activity
- nitric-oxide synthase activity
- nucleotide binding
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD or NADH as one donor, and incorporation of one atom of oxygen
- protein binding
- purine nucleotide binding
- tetrapyrrole binding
- transition metal ion binding
- transporter activity
|
| Process |
- biosynthesis
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- nitric oxide biosynthesis
- physiological process
|
| Component |
| — |
|
| Enzyme 7 General Function |
Inorganic ion transport and metabolism |
| Enzyme 7 Specific Function |
Not Available |
| Enzyme 7 Pathways |
Not Available |
| Enzyme 7 Reactions |
Not Available |
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
Not Available |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
B3VK56  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
B3VK56_HUMAN  |
| Enzyme 7 PDB ID |
1TLL  |
| Enzyme 7 PDB File |
Show |
| Enzyme 7 3D Structure |
|
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
Not Available |
| Enzyme 7 GenBank Gene ID |
EU753241  |
| Enzyme 7 GeneCard ID |
B3VK56  |
| Enzyme 7 GenAtlas ID |
Not Available |
| Enzyme 7 HGNC ID |
Not Available |
| Enzyme 7 Chromosome Location |
12 |
| Enzyme 7 Locus |
12q24.2-q24.31 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 General References |
Not Available |
| Enzyme 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
16944 |
| Enzyme 8 Name |
Dynein light chain 1, cytoplasmic |
| Enzyme 8 Synonyms |
- Dynein light chain LC8-type 1
- 8 kDa dynein light chain
- DLC8
- Protein inhibitor of neuronal nitric oxide synthase
- PIN
|
| Enzyme 8 Gene Name |
DYNLL1 |
| Enzyme 8 Protein Sequence |
>Dynein light chain 1, cytoplasmic
MCDRKAVIKNADMSEEMQQDSVECATQALEKYNIEKDIAAHIKKEFDKKYNPTWHCIVGR
NFGSYVTHETKHFIYFYLGQVAILLFKSG
|
| Enzyme 8 Number of Residues |
89 |
| Enzyme 8 Molecular Weight |
10366 |
| Enzyme 8 Theoretical pI |
7.50 |
| Enzyme 8 GO Classification |
| Function |
- microtubule motor activity
- motor activity
|
| Process |
- cell organization and biogenesis
- cellular physiological process
- cytoskeleton organization and biogenesis
- microtubule-based process
- organelle organization and biogenesis
- physiological process
|
| Component |
- microtubule associated complex
- protein complex
|
|
| Enzyme 8 General Function |
Not Available |
| Enzyme 8 Specific Function |
Binds and inhibits the catalytic activity of neuronal nitric oxide synthase |
| Enzyme 8 Pathways |
Not Available |
| Enzyme 8 Reactions |
Not Available |
| Enzyme 8 Pfam Domain Function |
|
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
Not Available |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
P63167  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
DYL1_HUMAN  |
| Enzyme 8 PDB ID |
1F96  |
| Enzyme 8 PDB File |
Show |
| Enzyme 8 3D Structure |
|
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 Gene Sequence |
Not Available |
| Enzyme 8 GenBank Gene ID |
U32944  |
| Enzyme 8 GeneCard ID |
P63167  |
| Enzyme 8 GenAtlas ID |
DYNLL1  |
| Enzyme 8 HGNC ID |
HGNC:15476  |
| Enzyme 8 Chromosome Location |
12 |
| Enzyme 8 Locus |
12q24.23 |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 General References |
- Dick T, Ray K, Salz HK, Chia W: Cytoplasmic dynein (ddlc1) mutations cause morphogenetic defects and apoptotic cell death in Drosophila melanogaster. Mol Cell Biol. 1996 May;16(5):1966-77. [PubMed
]
|
| Enzyme 8 Metabolite References |
Not Available |