| Version |
2.5 |
| Creation Date |
2006-05-22 16:12:08 |
| Update Date |
2009-05-15 17:02:30 |
| Accession Number |
HMDB02757 |
| Secondary Accession Numbers |
Not Available |
| Common Name |
Cysteic acid |
| Description |
A crystalline amino acid formed in the oxidation of cysteine; it is a precursor of taurine. |
| Synonyms |
- 2-Amino-3-sulfopropionate
- 2-Amino-3-sulfopropionic acid
- 2-amino-3-sulfopropanoate
- 2-amino-3-sulfopropanoic acid
- 3-Sulfoalanine
- Cepteate
- Cepteic acid
- Cipteate
- Cipteic acid
- Cysteinate
- Cysteinesulfonate
- Cysteinesulfonic acid
- Cysteinic acid
- Cysterate
- Cysteric acid
- L-Cysteate
- L-Cysteic acid
- beta-Sulfoalanine
- cysteate
|
| Chemical IUPAC Name |
2-amino-3-sulfo-propanoic acid |
| Chemical Formula |
C3H7NO5S |
| Chemical Structure |
 |
| Chemical Taxonomy |
| Kingdom |
|
| Super Class |
- Amino acids and Amino Acid conjugates
|
| Class |
|
| Sub Class |
|
| Family |
|
| Species |
- primary amine
- primary aliphatic amine (alkylamine)
- carboxylic acid
- sulfonic acid
- alpha-aminoacid
|
| Biofunction |
- Protein synthesis, amino acid biosynthesis
|
| Application |
| — |
| Source |
|
|
| Average Molecular Weight |
169.156 |
| Monoisotopic Molecular Weight |
169.004486 |
| Isomeric SMILES |
NC(CS(O)(=O)=O)C(O)=O |
| Canonical SMILES |
NC(CS(O)(=O)=O)C(O)=O |
| KEGG Compound ID |
C00506  |
| BioCyc ID |
L-CYSTEATE  |
| BiGG ID |
35186  |
| Wikipedia Link |
Not Available |
| NuGOwiki Link |
HMDB02757  |
| Metagene Link |
HMDB02757  |
| METLIN ID |
332  |
| PubChem Compound |
25701  |
| PubChem Substance |
853853  |
| ChEBI ID |
17285  |
| CAS Registry Number |
498-40-8 |
| InChI Identifier |
InChI=1/C3H7NO5S/c4-2(3(5)6)1-10(7,8)9/h2H,1,4H2,(H,5,6)(H,7,8,9) |
| Synthesis Reference |
Zhao, Chong-tao; Wang, Qing-ping; Lin, Wan-zhen; Chen, Ping. Synthesis of L-cysteic acid by indirect electrooxidation. Jingxi Huagong (2003), 20(4), 237-238, 253. |
| Melting Point (Experimental) |
Not Available |
| Experimental Water Solubility |
Not Available
Source: PhysProp
|
| Predicted Water Solubility |
73.6 mg/mL [Predicted by ALOGPS]
Calculated using ALOGPS
|
| Physiological Charge |
-1 |
| State |
Solid |
| Experimental LogP/Hydrophobicity |
Not Available
Source: PhysProp
|
| Predicted LogP/Hydrophobicity |
-2.39 [Predicted by ALOGPS]; -4.4 [Predicted by PubChem via XLOGP]; -6.20 [MEYLAN,WM & HOWARD,PH (1995)]
Calculated using ALOGPS
|
| Material Safety Data Sheet (MSDS) |
|
| MOL File |
Show |
| SDF File |
Show |
| PDB File |
Show |
| 2D Structure |
|
| 3D Structure |
|
| Experimental PDB ID |
Not Available |
| Experimental 1H NMR Spectrum |
Not Available |
| Experimental 13C NMR Spectrum |
Not Available |
| Experimental 13C HSQC Spectrum |
Not Available |
| Predicted 1H NMR Spectrum |
Show Image Show Peaklist
|
| Predicted 13C NMR Spectrum |
Show Image Show Peaklist
|
| Mass Spectrum |
Not Available |
| Simplified TOCSY Spectrum |
Not Available |
| BMRB Spectrum |
Not Available |
| Cellular Location |
- Cytoplasm (Predicted from LogP)
- mitochondria
|
| Biofluid Location |
Not Available |
| Tissue Location |
Not Available |
| Concentrations (Normal) |
Not Available |
| Concentrations (Abnormal) |
Not Available |
| Associated Disorders |
Not Available |
| OMIM ID |
Not Available |
| Pathways |
|
| General References |
- Sarwar G, Botting HG, Peace RW: Complete amino acid analysis in hydrolysates of foods and feces by liquid chromatography of precolumn phenylisothiocyanate derivatives. J Assoc Off Anal Chem. 1988 Nov-Dec;71(6):1172-5. [PubMed
]
- Paroni R, De Vecchi E, Fermo I, Arcelloni C, Diomede L, Magni F, Bonini PA: Total urinary hydroxyproline determined with rapid and simple high-performance liquid chromatography. Clin Chem. 1992 Mar;38(3):407-11. [PubMed
]
- Jasin HE: Oxidative modification of inflammatory synovial fluid immunoglobulin G. Inflammation. 1993 Apr;17(2):167-81. [PubMed
]
|
| Metabolic Enzymes |
- Aspartate aminotransferase, cytoplasmic
- Aspartate aminotransferase, mitochondrial precursor
- Glutamate decarboxylase 2
- Cysteine sulfinic acid decarboxylase
- Hypothetical protein GAD1
- cDNA, FLJ93078, Homo sapiens glutamic-oxaloacetic transaminase 1, soluble(aspartate aminotransferase 1) (GOT1), mRNA (Glutamic-oxaloacetic transaminase 1, soluble (Aspartate aminotransferase 1), isoform CRA_b)
|
|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5515 |
| Enzyme 1 Name |
Aspartate aminotransferase, cytoplasmic |
| Enzyme 1 Synonyms |
- Transaminase A
- Glutamate oxaloacetate transaminase 1
|
| Enzyme 1 Gene Name |
GOT1 |
| Enzyme 1 Protein Sequence |
>Aspartate aminotransferase, cytoplasmic
MAPPSVFAEVPQAQPVLVFKLTADFREDPDPRKVNLGVGAYRTDDCHPWVLPVVKKVEQK
IANDNSLNHEYLPILGLAEFRSCASRLALGDDSPALKEKRVGGVQSLGGTGALRIGADFL
ARWYNGTNNKNTPVYVSSPTWENHNAVFSAAGFKDIRSYRYWDAEKRGLDLQGFLNDLEN
APEFSIVVLHACAHNPTGIDPTPEQWKQIASVMKHRFLFPFFDSAYQGFASGNLERDAWA
IRYFVSEGFEFFCAQSFSKNFGLYNERVGNLTVVGKEPESILQVLSQMEKIVRITWSNPP
AQGARIVASTLSNPELFEEWTGNVKTMADRILTMRSELRARLEALKTPGTWNHITDQIGM
FSFTGLNPKQVEYLVNEKHIYLLPSGRINVSGLTTKNLDYVATSIHEAVTKIQ
|
| Enzyme 1 Number of Residues |
413 |
| Enzyme 1 Molecular Weight |
46248 |
| Enzyme 1 Theoretical pI |
7.01 |
| Enzyme 1 GO Classification |
| Function |
- catalytic activity
- transaminase activity
- transferase activity
- transferase activity, transferring nitrogenous groups
|
| Process |
- amino acid and derivative metabolism
- amino acid metabolism
- biosynthesis
- cellular metabolism
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 1 General Function |
Amino acid transport and metabolism |
| Enzyme 1 Specific Function |
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate |
| Enzyme 1 Pathways |
|
| Enzyme 1 Reactions |
- L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
179067  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
P17174  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
AATC_HUMAN  |
| Enzyme 1 PDB ID |
1AJS  |
| Enzyme 1 PDB File |
Show |
| Enzyme 1 3D Structure |
|
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>1242 bp
ATGGCACCTCCGTCAGTCTTTGCCGAGGTTCCGCAGGCCCAGCCTGTCCTGGTCTTCAAG
CTCACTGCCGACTTCAGGGAGGATCCGGACCCCCGCAAGGTCAACCTGGGAGTGGGAGCA
TATCGCACGGATGACTGCCATCCCTGGGTTTTGCCAGTAGTGAAGAAAGTGGAGCAGAAG
ATTGCTAATGACAATAGCCTAAATCACGAGTATCTGCCAATCCTGGGCCTGGCTGAGTTC
CGGAGCTGTGCTTCTCGTCTTGCCCTTGGGGATGACAGCCCAGCACTCAAGGAGAAGCGG
GTAGGAGGTGTGCAATCTTTGGGGGGAACAGGTGCACTTCGAATTGGAGCTGATTTCTTA
GCGCGTTGGTACAATGGAACAAACAACAAGAACACACCTGTCTATGTGTCCTCACCAACC
TGGGAGAATCACAATGCTGTGTTTTCCGCTGCTGGTTTTAAAGACATTCGGTCCTATCGC
TACTGGGATGCAGAGAAGAGAGGATTGGACCTCCAGGGCTTCCTGAATGATCTGGAGAAT
GCTCCTGAGTTCTCCATTGTTGTCCTCCACGCCTGTGCACACAACCCAACTGGGATTGAC
CCAACTCCGGAGCAGTGGAAGCAGATTGCTTCTGTCATGAAGCACCGGTTTCTGTTCCCC
TTCTTTGACTCAGCCTATCAGGGCTTCGCATCTGGAAACCTGGAGAGAGATGCCTGGGCC
ATTCGCTATTTTGTGTCTGAAGGCTTCGAGTTCTTCTGTGCCCAGTCCTTCTCCAAGAAC
TTCGGGCTCTACAATGAGAGAGTCGGGAATCTGACTGTGGTTGGAAAAGAACCTGAGAGC
ATCCTGCAAGTCCTTTCCCAGATGGAGAAGATCGTGCGGATTACTTGGTCCAATCCCCCC
GCCCAGGGAGCACGAATTGTGGCCAGCACCCTCTCTAACCCTGAGCTCTTTGAGGAATGG
ACAGGTAATGTGAAGACAATGGCTGACCGGATTCTGACCATGAGATCTGAACTCAGGGCA
CGACTAGAAGCCCTCAAAACCCCTGGGACCTGGAACCACATCACTGATCAAATTGGCATG
TTCAGCTTCACTGGGTTGAACCCCAAGCAGGTTGAGTATCTGGTCAATGAAAAGCACATC
TACCTGCTGCCAAGTGGTCGAATCAACGTGAGTGGCTTAACCACCAAAAATCTAGATTAC
GTGGCCACCTCCATCCATGAAGCAGTCACCAAAATCCAGTGA
|
| Enzyme 1 GenBank Gene ID |
M37400  |
| Enzyme 1 GeneCard ID |
GOT1  |
| Enzyme 1 GenAtlas ID |
GOT1  |
| Enzyme 1 HGNC ID |
HGNC:4432  |
| Enzyme 1 Chromosome Location |
10 |
| Enzyme 1 Locus |
10q24.1-q25.1 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Bousquet-Lemercier B, Pol S, Pave-Preux M, Hanoune J, Barouki R: Properties of human liver cytosolic aspartate aminotransferase mRNAs generated by alternative polyadenylation site selection. Biochemistry. 1990 Jun 5;29(22):5293-9. [PubMed
]
- Doyle JM, Schinina ME, Bossa F, Doonan S: The amino acid sequence of cytosolic aspartate aminotransferase from human liver. Biochem J. 1990 Sep 15;270(3):651-7. [PubMed
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5516 |
| Enzyme 2 Name |
Aspartate aminotransferase, mitochondrial precursor |
| Enzyme 2 Synonyms |
- Transaminase A
- Glutamate oxaloacetate transaminase 2
|
| Enzyme 2 Gene Name |
GOT2 |
| Enzyme 2 Protein Sequence |
>Aspartate aminotransferase, mitochondrial precursor
MALLHSGRVLPGIAAAFHPGLAAAASARASSWWTHVEMGPPDPILGVTEAFKRDTNSKKM
NLGVGAYRDDNGKPYVLPSVRKAEAQIAAKNLDKEYLPIGGLAEFCKASAELALGENSEV
LKSGRFVTVQTISGTGALRIGASFLQRFFKFSRDVFLPKPTWGNHTPIFRDAGMQLQGYR
YYDPKTCGFDFTGAVEDISKIPEQSVLLLHACAHNPTGVDPRPEQWKEIATVVKKRNLFA
FFDMAYQGFASGDGDKDAWAVRHFIEQGINVCLCQSYAKNMGLYGERVGAFTMVCKDADE
AKRVESQLKILIRPMYSNPPLNGARIAAAILNTPDLRKQWLQEVKGMADRIIGMRTQLVS
NLKKEGSTHNWQHITDQIGMFCFTGLKPEQVERLIKEFSIYMTKDGRISVAGVTSSNVGY
LAHAIHQVTK
|
| Enzyme 2 Number of Residues |
430 |
| Enzyme 2 Molecular Weight |
47476 |
| Enzyme 2 Theoretical pI |
9.38 |
| Enzyme 2 GO Classification |
| Function |
- catalytic activity
- transaminase activity
- transferase activity
- transferase activity, transferring nitrogenous groups
|
| Process |
- amino acid and derivative metabolism
- amino acid metabolism
- biosynthesis
- cellular metabolism
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 2 General Function |
Amino acid transport and metabolism |
| Enzyme 2 Specific Function |
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate |
| Enzyme 2 Pathways |
|
| Enzyme 2 Reactions |
- L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
Not Available |
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
179104  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
P00505  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
AATM_HUMAN  |
| Enzyme 2 PDB ID |
Not Available |
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>1293 bp
ATGGCCCTGCTGCACTCCGGCCGCGTCCTCCCCGGGATCGCCGCCGCCTTCCACCCGGGC
CTCGCCGCCGCGGCCTCTGCCAGAGCCAGCTCCTGGTGGACCCATGTGGAAATGGGACCT
CCAGATCCCATTCTGGGAGTCACTGAAGCCTTTAAGAGGGACACCAATAGCAAAAAGATG
AATCTGGGAGTTGGTGCCTACCGGGATGATAATGGAAAGCCTTACGTTCTGCCTAGCGTC
CGCAAGGCAGAGGCCCAGATTGCCGCAAAAAATTTGGACAAGGAATACCTGCCCATTGGG
GGACTGGCTGAATTTTGCAAGGCATCTGCAGAACTAGCCCTGGGTGAGAACAGCGAAGTC
TTGAAGAGTGGCCGGTTTGTCACTGTGCAGACCATTTCTGGAACTGGAGCCTTAAGGATC
GGAGCCAGTTTTCTGCAAAGATTTTTTAAGTTCAGCCGAGATGTCTTTCTGCCCAAACCA
ACCTGGGGAAACCACACACCCATCTTCAGGGATGCTGGCATGCAGCTACAAGGTTATCGG
TATTATGACCCCAAGACTTGCGGTTTTGACTTCACAGGCGCTGTGGAGGATATTTCAAAA
ATACCAGAGCAGAGTGTTCTTCTTCTGCATGCCTGCGCCCACAATCCCACGGGAGTGGAC
CCGCGTCCGGAACAGTGGAAGGAAATAGCAACAGTGGTGAAGAAAAGGAATCTCTTTGCG
TTCTTTGACATGGCCTACCAAGGCTTTGCCAGTGGTGATGGTGATAAGGATGCCTGGGCT
GTGCGCCACTTCATCGAACAGGGCATTAATGTTTGCCTCTGCCAATCATATGCCAAGAAC
ATGGGCTTATATGGTGAGCGTGTAGGAGCCTTCACTATGGTCTGCAAAGATGCGGATGAA
GCCAAAAGGGTAGAGTCACAGTTGAAGATCTTGATCCGTCCCATGTATTCCAACCCTCCC
CTCAATGGGGCCCGGATTGCTGCTGCCATTCTGAACACCCCAGATTTGCGAAAACAATGG
CTGCAAGAAGTGAAAGGCATGGCTGACCGCATCATTGGCATGCGGACTCAACTGGTCTCC
AACCTCAAGAAGGAGGGTTCCACCCACAATTGGCAACACATCACCGACCAAATTGGCATG
TTCTGTTTCACAGGGCTAAAGCCTGAACAGGTGGAGCGGCTGATCAAGGAGTTCTCCATC
TACATGACAAAAGATGGCCGCATCTCTGTGGCAGGGGTCACCTCCAGCAACGTGGGCTAC
CTTGCCCATGCCATTCACCAGGTCACCAAGTAA
|
| Enzyme 2 GenBank Gene ID |
M22632  |
| Enzyme 2 GeneCard ID |
GOT2  |
| Enzyme 2 GenAtlas ID |
GOT2  |
| Enzyme 2 HGNC ID |
HGNC:4433  |
| Enzyme 2 Chromosome Location |
16 |
| Enzyme 2 Locus |
16q21 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Pol S, Bousquet-Lemercier B, Pave-Preux M, Pawlak A, Nalpas B, Berthelot P, Hanoune J, Barouki R: Nucleotide sequence and tissue distribution of the human mitochondrial aspartate aminotransferase mRNA. Biochem Biophys Res Commun. 1988 Dec 30;157(3):1309-15. [PubMed
]
- Martini F, Angelaccio S, Barra D, Pascarella S, Maras B, Doonan S, Bossa F: The primary structure of mitochondrial aspartate aminotransferase from human heart. Biochim Biophys Acta. 1985 Nov 8;832(1):46-51. [PubMed
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
5975 |
| Enzyme 3 Name |
Glutamate decarboxylase 2 |
| Enzyme 3 Synonyms |
- Glutamate decarboxylase 65 kDa isoform
- GAD-65
- 65 kDa glutamic acid decarboxylase
|
| Enzyme 3 Gene Name |
GAD2 |
| Enzyme 3 Protein Sequence |
>Glutamate decarboxylase 2
MASPGSGFWSFGSEDGSGDSENPGTARAWCQVAQKFTGGIGNKLCALLYGDAEKPAESGG
SQPPRAAARKAACACDQKPCSCSKVDVNYAFLHATDLLPACDGERPTLAFLQDVMNILLQ
YVVKSFDRSTKVIDFHYPNELLQEYNWELADQPQNLEEILMHCQTTLKYAIKTGHPRYFN
QLSTGLDMVGLAADWLTSTANTNMFTYEIAPVFVLLEYVTLKKMREIIGWPGGSGDGIFS
PGGAISNMYAMMIARFKMFPEVKEKGMAALPRLIAFTSEHSHFSLKKGAAALGIGTDSVI
LIKCDERGKMIPSDLERRILEAKQKGFVPFLVSATAGTTVYGAFDPLLAVADICKKYKIW
MHVDAAWGGGLLMSRKHKWKLSGVERANSVTWNPHKMMGVPLQCSALLVREEGLMQNCNQ
MHASYLFQQDKHYDLSYDTGDKALQCGRHVDVFKLWLMWRAKGTTGFEAHVDKCLELAEY
LYNIIKNREGYEMVFDGKPQHTNVCFWYIPPSLRTLEDNEERMSRLSKVAPVIKARMMEY
GTTMVSYQPLGDKVNFFRMVISNPAATHQDIDFLIEEIERLGQDL
|
| Enzyme 3 Number of Residues |
585 |
| Enzyme 3 Molecular Weight |
65412 |
| Enzyme 3 Theoretical pI |
6.89 |
| Enzyme 3 GO Classification |
| Function |
- carbon-carbon lyase activity
- carboxy-lyase activity
- catalytic activity
- lyase activity
|
| Process |
- amino acid and derivative metabolism
- amino acid metabolism
- cellular metabolism
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 3 General Function |
Amino acid transport and metabolism |
| Enzyme 3 Specific Function |
Catalyzes the production of GABA |
| Enzyme 3 Pathways |
|
| Enzyme 3 Reactions |
- L-glutamate = 4-aminobutanoate + CO2
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
182934  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
Q05329  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
DCE2_HUMAN  |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>1758 bp
ATGGCATCTCCGGGCTCTGGCTTTTGGTCTTTCGGGTCGGAAGATGGCTCTGGGGATTCC
GAGAATCCCGGCACAGCGCGAGCCTGGTGCCAAGTGGCTCAGAAGTTCACGGGCGGCATC
GGAAACAAACTGTGCGCCCTGCTCTACGGAGACGCCGAGAAGCCGGCGGAGAGCGGCGGG
AGCCAACCCCCGCGGGCCGCCGCCCGGAAGGCCGCCTGCGCCTGCGACCAGAAGCCCTGC
AGCTGCTCCAAAGTGGATGTCAACTACGCGTTTCTCCATGCAACAGACCTGCTGCCGGCG
TGTGATGGAGAAAGGCCCACTTTGGCGTTTCTGCAAGATGTTATGAACATTTTACTTCAG
TATGTGGTGAAAAGTTTCGATAGATCAACCAAAGTGATTGATTTCCATTATCCTAATGAG
CTTCTCCAAGAATATAATTGGGAATTGGCAGACCAACCACAAAATTTGGAGGAAATTTTG
ATGCATTGCCAAACAACTCTAAAATATGCAATTAAAACAGGGCATCCTAGATACTTCAAT
CAACTTTCTACTGGTTTGGATATGGTTGGATTAGCAGCAGACTGGCTGACATCAACAGCA
AATACTAACATGTTCACCTATGAAATTGCTCCAGTATTTGTGCTTTTGGAATATGTCACA
CTAAAGAAAATGAGAGAAATCATTGGCTGGCCAGGGGGCTCTGGCGATGGGATATTTTCT
CCCGGTGGCGCCATATCTAACATGTATGCCATGATGATCGCACGCTTTAAGATGTTCCCA
GAAGTCAAGGAGAAAGGAATGGCTGCTCTTCCCAGGCTCATTGCCTTCACGTCTGAACAT
AGTCATTTTTCTCTCAAGAAGGGAGCTGCAGCCTTAGGGATTGGAACAGACAGCGTGATT
CTGATTAAATGTGATGAGAGAGGGAAAATGATTCCATCTGATCTTGAAAGAAGGATTCTT
GAAGCCAAACAGAAAGGGTTTGTTCCTTTCCTCGTGAGTGCCACAGCTGGAACCACCGTG
TACGGAGCATTTGACCCCCTCTTAGCTGTCGCTGACATTTGCAAAAAGTATAAGATCTGG
ATGCATGTGGATGCAGCTTGGGGTGGGGGATTACTGATGTCCCGAAAACACAAGTGGAAA
CTGAGTGGCGTGGAGAGGGCCAACTCTGTGACGTGGAATCCACACAAGATGATGGGAGTC
CCTTTGCAGTGCTCTGCTCTCCTGGTTAGAGAAGAGGGATTGATGCAGAATTGCAACCAA
ATGCATGCCTCCTACCTCTTTCAGCAAGATAAACATTATGACCTGTCCTATGACACTGGA
GACAAGGCCTTACAGTGCGGACGCCACGTTGATGTTTTTAAACTATGGCTGATGTGGAGG
GCAAAGGGGACTACCGGGTTTGAAGCGCATGTTGATAAATGTTTGGAGTTGGCAGAGTAT
TTATACAACATCATAAAAAACCGAGAAGGATATGAGATGGTGTTTGATGGGAAGCCTCAG
CACACAAATGTCTGCTTCTGGTACATTCCTCCAAGCTTGCGTACTCTGGAAGACAATGAA
GAGAGAATGAGTCGCCTCTCGAAGGTGGCTCCAGTGATTAAAGCCAGAATGATGGAGTAT
GGAACCACAATGGTCAGCTACCAACCCTTGGGAGACAAGGTCAATTTCTTCCGCATGGTC
ATCTCAAACCCAGCGGCAACTCACCAAGACATTGACTTCCTGATTGAAGAAATAGAACGC
CTTGGACAAGATTTATAA
|
| Enzyme 3 GenBank Gene ID |
M81882  |
| Enzyme 3 GeneCard ID |
GAD2  |
| Enzyme 3 GenAtlas ID |
GAD2  |
| Enzyme 3 HGNC ID |
HGNC:4093  |
| Enzyme 3 Chromosome Location |
10 |
| Enzyme 3 Locus |
10p11.23 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- Karlsen AE, Hagopian WA, Grubin CE, Dube S, Disteche CM, Adler DA, Barmeier H, Mathewes S, Grant FJ, Foster D, et al.: Cloning and primary structure of a human islet isoform of glutamic acid decarboxylase from chromosome 10. Proc Natl Acad Sci U S A. 1991 Oct 1;88(19):8337-41. [PubMed
]
- Bu DF, Erlander MG, Hitz BC, Tillakaratne NJ, Kaufman DL, Wagner-McPherson CB, Evans GA, Tobin AJ: Two human glutamate decarboxylases, 65-kDa GAD and 67-kDa GAD, are each encoded by a single gene. Proc Natl Acad Sci U S A. 1992 Mar 15;89(6):2115-9. [PubMed
]
- Bu DF, Tobin AJ: The exon-intron organization of the genes (GAD1 and GAD2) encoding two human glutamate decarboxylases (GAD67 and GAD65) suggests that they derive from a common ancestral GAD. Genomics. 1994 May 1;21(1):222-8. [PubMed
]
- Mauch L, Abney CC, Berg H, Scherbaum WA, Liedvogel B, Northemann W: Characterization of a linear epitope within the human pancreatic 64-kDa glutamic acid decarboxylase and its autoimmune recognition by sera from insulin-dependent diabetes mellitus patients. Eur J Biochem. 1993 Mar 1;212(2):597-603. [PubMed
]
- Kim J, Richter W, Aanstoot HJ, Shi Y, Fu Q, Rajotte R, Warnock G, Baekkeskov S: Differential expression of GAD65 and GAD67 in human, rat, and mouse pancreatic islets. Diabetes. 1993 Dec;42(12):1799-808. [PubMed
]
- Namchuk M, Lindsay L, Turck CW, Kanaani J, Baekkeskov S: Phosphorylation of serine residues 3, 6, 10, and 13 distinguishes membrane anchored from soluble glutamic acid decarboxylase 65 and is restricted to glutamic acid decarboxylase 65alpha. J Biol Chem. 1997 Jan 17;272(3):1548-57. [PubMed
]
- Kanaani J, el-Husseini Ael-D, Aguilera-Moreno A, Diacovo JM, Bredt DS, Baekkeskov S: A combination of three distinct trafficking signals mediates axonal targeting and presynaptic clustering of GAD65. J Cell Biol. 2002 Sep 30;158(7):1229-38. [PubMed
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
6224 |
| Enzyme 4 Name |
Cysteine sulfinic acid decarboxylase |
| Enzyme 4 Synonyms |
- Sulfinoalanine decarboxylase
- Cysteine-sulfinate decarboxylase
|
| Enzyme 4 Gene Name |
CSAD |
| Enzyme 4 Protein Sequence |
>Cysteine sulfinic acid decarboxylase
MADSEALPSLAGDPVAVEALLRAVFGVVVDEAIQKGTSVSQKVCEWKEPEELKQLLDLEL
RSQGESQKQILERCRAVIRYSVKTGHPRFFNQLFSGLDPHALAGRIITESLNTSQYTYEI
APVFVLMEEEVLRKLRALVGWSSGDGIFCPGGSISNMYAVNLARYQRYPDCKQRGLRTLP
PLALFTSKECHYSIQKGAAFLGLGTDSVRVVKADERGKMVPEDLERQIGMAEAEGAVPFL
VSATSGTTVLGAFDPLEAIADVCQRHGLWLHVDAAWGGSVLLSQTHRHLLDGIQRADSVA
WNPHKLLAAGLQCSALLLQDTSNLLKRCHGSQASYLFQQDKFYDVALDTGDKVVQCGRRV
DCLKLWLMWKAQGDQGLERRIDQAFVLARYLVEEMKKREGFELVMEPEFVNVCFWFVPPS
LRGKQESPDYHERLSKVAPVLKERMVKEGSMMIGYQPHGTRGNFFRVVVANSALTCADMD
FLLNELERLGQDL
|
| Enzyme 4 Number of Residues |
493 |
| Enzyme 4 Molecular Weight |
55024 |
| Enzyme 4 Theoretical pI |
6.44 |
| Enzyme 4 GO Classification |
| Function |
- carbon-carbon lyase activity
- carboxy-lyase activity
- catalytic activity
- lyase activity
|
| Process |
- amino acid and derivative metabolism
- amino acid metabolism
- cellular metabolism
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 4 General Function |
Amino acid transport and metabolism |
| Enzyme 4 Specific Function |
3-sulfino-L-alanine = hypotaurine + CO(2) |
| Enzyme 4 Pathways |
- Taurine and Hypotaurine Metabolism (map00430
)
|
| Enzyme 4 Reactions |
- 3-sulfino-L-alanine = hypotaurine + CO2
|
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
4894558  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
Q9Y600  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
CSAD_HUMAN  |
| Enzyme 4 PDB ID |
Not Available |
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>1041 bp
ATGGCTGACTCAGAAGCACTCCCCTCCCTTGCTGGGGACCCAGTGGCTGTGGAAGCCTTG
CTCCGGGCCGTGTTTGGGGTTGTTGTGGATGAGGCCATTCAGAAAGGAACCAGTGTCTCC
CAGAAGTGTCACTACTCCATCCAGAAGGGAGCTGCGTTTCTGGGACTTGGCACCGACAGT
GTCCGAGTGGTCAAGGCTGATGAGAGAGGGAAAATGGTCCCCGAGGATCTGGAGAGGCAG
ATTGGTATGGCCGAGGCTGAGGGTGCTGTGCCGTTCCTGGTCAGTGCCACCTCTGGCACC
ACTGTGCTAGGGGCCTTTGACCCCCTGGAGGCAATTGCTGATGTGTGCCAGCGTCATGGG
CTATGGCTGCATGTGGATGCTGCCTGGGGTGGGAGCGTCCTGCTGTCACAGACACACAGG
CATCTCCTGGATGGGATCCAGAGGGCTGACTCTGTGGCCTGGAATCCCCACAAGCTCCTC
GCAGCAGGCCTGCAATGCTCTGCACTTCTTCTCCAGGATACCTCGAACCTGCTCAAGCGC
TGCCATGGGTCCCAGGCCAGCTACCTTTTCCAGCAGGACAAGTTCTACGATGTGGCTCTG
GACACGGGAGACAAGGTGGTGCAGTGTGGCCGCCGTGTGGACTGTCTGAAGCTGTGGCTC
ATGTGGAAGGCACAGGGCGATCAAGGGCTGGAGCGGCGCATCGACCAGGCCTTTGTCCTT
GCCCGGTACCTGGTGGAGGAAATGAAGAAGCGGGAAGGGTTTGAGCTAGTCATGGAGCCT
GAGTTTGTCAATGTGTGTTTCTGGTTCGTACCCCCCAGCCTGCGAGGGAAGCAGGAGAGT
CCAGATTACCACGAAGGGCTGTCAAAGGTGGCCCCCGTGCTCAAGGAGCGCATGGTGAAG
GAGGGCTCCATGATGATTGGCTACCAGCCCCACGGGACCCGGGGCAACTTCTTCCGTGTG
GTTGTGGCCAACTCTGCACTGACCTGTGCTGATATGGACTTCCTCCTCAACGAGCTGGAG
CGGCTAGGCCAGGACCTGTGA
|
| Enzyme 4 GenBank Gene ID |
AF116546  |
| Enzyme 4 GeneCard ID |
CSAD  |
| Enzyme 4 GenAtlas ID |
CSAD  |
| Enzyme 4 HGNC ID |
HGNC:18966  |
| Enzyme 4 Chromosome Location |
12 |
| Enzyme 4 Locus |
12q13.11-q14.3 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
Not Available |
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
7966 |
| Enzyme 5 Name |
Hypothetical protein GAD1 |
| Enzyme 5 Synonyms |
Not Available |
| Enzyme 5 Gene Name |
GAD1 |
| Enzyme 5 Protein Sequence |
>Hypothetical protein GAD1
MASSTPSSSATSSNAGADPNTTNLRPTTYDTWCGVAHGCTRKLGLKICGFLQRTNSLEEK
SRLVSAFKERQSSKNLLSCENSDRDARFRRTETDFSNLFARDLLPAKNGEEQTVQFLLEV
VDILLNYVRKTFDRSTKVLDFHHPHQLLEGMEGFNLELSDHPESLEQILVDCRDTLKYGV
RTGHPRFFNQLSTGLDIIGLAGEWLTSTANTNMFTYEIAPVFVLMEQITLKKMREIVGWS
SKDGDGIFSPGGAISNMYSIMAARYKYFPEVKTKGMAAVPKLVLFTSEQSHYSIKKAGAA
LGFGTDNVILIKCNERGKIIPADFEAKILEAKQKGYVPFYVNATAGTTVYGAFDPIQEIA
DICEKYNLWLHVDAAWGGGLLMSRKHRHKLNGIERANSVTWNPHKMMGVLLQCSAILVKE
KGILQGCNQMCAGYLFQPDKQYDVSYDTGDKAIQCGRHVDIFKFWLMWKAKGTVGFENQI
NKCLELAEYLYAKIKNREEFEMVFNGEPEHTNVCFWYIPQSLRGVPDSPQRREKLHKVAP
KIKALMMESGTTMVGYQPQGDKANFFRMVISNPAATQSDIDFLIEEIERLGQDL
|
| Enzyme 5 Number of Residues |
594 |
| Enzyme 5 Molecular Weight |
66897 |
| Enzyme 5 Theoretical pI |
7.67 |
| Enzyme 5 GO Classification |
| Function |
- carbon-carbon lyase activity
- carboxy-lyase activity
- catalytic activity
- lyase activity
|
| Process |
- amino acid and derivative metabolism
- amino acid metabolism
- cellular metabolism
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 5 General Function |
Amino acid transport and metabolism |
| Enzyme 5 Specific Function |
Not Available |
| Enzyme 5 Pathways |
Not Available |
| Enzyme 5 Reactions |
Not Available |
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
62988850  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
Q53TQ7  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
Q53TQ7_HUMAN  |
| Enzyme 5 PDB ID |
Not Available |
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>1785 bp
ATGGCGTCTTCGACCCCATCTTCGTCCGCAACCTCCTCGAACGCGGGAGCGGACCCCAAT
ACCACTAACCTGCGCCCCACAACGTACGATACCTGGTGCGGCGTGGCCCATGGATGCACC
AGAAAACTGGGGCTCAAGATCTGCGGCTTCTTGCAAAGGACCAACAGCCTGGAAGAGAAG
AGTCGCCTTGTGAGTGCCTTCAAGGAGAGGCAATCCTCCAAGAACCTGCTTTCCTGTGAA
AACAGCGACCGGGATGCCCGCTTCCGGCGCACAGAGACTGACTTCTCTAATCTGTTTGCT
AGAGATCTGCTTCCGGCTAAGAACGGTGAGGAGCAAACCGTGCAATTCCTCCTGGAAGTG
GTGGACATACTCCTCAACTATGTCCGCAAGACATTTGATCGCTCCACCAAGGTGCTGGAC
TTTCATCACCCACACCAGTTGCTGGAAGGCATGGAGGGCTTCAACTTGGAGCTCTCTGAC
CACCCCGAGTCCCTGGAGCAGATCCTGGTTGACTGCAGAGACACCTTGAAGTATGGGGTT
CGCACAGGTCATCCTCGATTTTTCAACCAGCTCTCCACTGGATTGGATATTATTGGCCTA
GCTGGAGAATGGCTGACATCAACGGCCAATACCAACATGTTTACATATGAAATTGCACCA
GTGTTTGTCCTCATGGAACAAATAACACTTAAGAAGATGAGAGAGATAGTTGGATGGTCA
AGTAAAGATGGTGATGGGATATTTTCTCCTGGGGGCGCCATATCCAACATGTACAGCATC
ATGGCTGCTCGCTACAAGTACTTCCCGGAAGTTAAGACAAAGGGCATGGCGGCTGTGCCT
AAACTGGTCCTCTTCACCTCAGAACAGAGTCACTATTCCATAAAGAAAGCTGGGGCTGCA
CTTGGCTTTGGAACTGACAATGTGATTTTGATAAAGTGCAATGAAAGGGGGAAAATAATT
CCAGCTGATTTTGAGGCAAAAATTCTTGAAGCCAAACAGAAGGGATATGTTCCCTTTTAT
GTCAATGCAACTGCTGGCACGACTGTTTATGGAGCTTTTGATCCGATACAAGAGATTGCA
GATATATGTGAGAAATATAACCTTTGGTTGCATGTCGATGCTGCCTGGGGAGGTGGGCTG
CTCATGTCCAGGAAGCACCGCCATAAACTCAACGGCATAGAAAGGGCCAACTCAGTCACC
TGGAACCCTCACAAGATGATGGGCGTGCTGTTGCAGTGCTCTGCCATTCTCGTCAAGGAA
AAGGGTATACTCCAAGGATGCAACCAGATGTGTGCAGGATACCTCTTCCAGCCAGACAAG
CAGTATGATGTCTCCTACGACACCGGGGACAAGGCAATTCAGTGTGGCCGCCACGTGGAT
ATCTTCAAGTTCTGGCTGATGTGGAAAGCAAAGGGCACAGTGGGATTTGAAAACCAGATC
AACAAATGCCTGGAACTGGCTGAATACCTCTATGCCAAGATTAAAAACAGAGAAGAATTT
GAGATGGTTTTCAATGGCGAGCCTGAGCACACAAACGTCTGTTTTTGGTATATTCCACAA
AGCCTCAGGGGTGTGCCAGACAGCCCTCAACGACGGGAAAAGCTACACAAGGTGGCTCCA
AAAATCAAAGCCCTGATGATGGAGTCAGGTACGACCATGGTTGGCTACCAGCCCCAAGGG
GACAAGGCCAACTTCTTCCGGATGGTCATCTCCAACCCAGCCGCTACCCAGTCTGACATT
GACTTCCTCATTGAGGAGATAGAAAGACTGGGCCAGGATCTGTAA
|
| Enzyme 5 GenBank Gene ID |
AC007405  |
| Enzyme 5 GeneCard ID |
GAD1  |
| Enzyme 5 GenAtlas ID |
GAD1  |
| Enzyme 5 HGNC ID |
HGNC:4092  |
| Enzyme 5 Chromosome Location |
2 |
| Enzyme 5 Locus |
2q31 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
Not Available |
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
16502 |
| Enzyme 6 Name |
cDNA, FLJ93078, Homo sapiens glutamic-oxaloacetic transaminase 1, soluble(aspartate aminotransferase 1) (GOT1), mRNA (Glutamic-oxaloacetic transaminase 1, soluble (Aspartate aminotransferase 1), isoform CRA_b) |
| Enzyme 6 Synonyms |
Not Available |
| Enzyme 6 Gene Name |
GOT1 |
| Enzyme 6 Protein Sequence |
>cDNA, FLJ93078, Homo sapiens glutamic-oxaloacetic transaminase 1, soluble(aspartate aminotransferase 1) (GOT1), mRNA (Glutamic-oxaloacetic transaminase 1, soluble (Aspartate aminotransferase 1), isoform CRA_b)
MAPPSVFAEVPQAQPVLVFKLTADFREDPDPRKVNLGVGAYRTDDCHPWVLPVVKKVEQK
IANDNSLNHEYLPILGLAEFRSCASRLALGDDSPALKEKRVGGVQSLGGTGALRIGADFL
ARWYNGTNNKNTPVYVSSPTWENHNAVFSAAGFKDIRSYRYWDAEKRGLDLQGFLNDLEN
APEFSIVVLHACAHNPTGIDPTPEQWKQIASVMKHRFLFPFFDSAYQGFASGNLERDAWA
IRYFVSEGFEFFCAQSFSKNFGLYNERVGNLTVVGKEPESILQVLSQMEKIVRITWSNPP
AQGARIVASTLSNPELFEEWTGNVKTMADRILTMRSELRARLEALKTPGTWNHITDQIGM
FSFTGLNPKQVEYLVNEKHIYLLPSGRINVSGLTTKNLDYVATSIHEAVTKIQ
|
| Enzyme 6 Number of Residues |
413 |
| Enzyme 6 Molecular Weight |
46248 |
| Enzyme 6 Theoretical pI |
7.01 |
| Enzyme 6 GO Classification |
| Function |
- catalytic activity
- transaminase activity
- transferase activity
- transferase activity, transferring nitrogenous groups
|
| Process |
- amino acid and derivative metabolism
- amino acid metabolism
- biosynthesis
- cellular metabolism
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 6 General Function |
Amino acid 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 |
Not Available |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
B2R6R7  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
B2R6R7_HUMAN  |
| Enzyme 6 PDB ID |
1AJS  |
| Enzyme 6 PDB File |
Show |
| Enzyme 6 3D Structure |
|
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
Not Available |
| Enzyme 6 GenBank Gene ID |
AK312684  |
| Enzyme 6 GeneCard ID |
B2R6R7  |
| Enzyme 6 GenAtlas ID |
Not Available |
| Enzyme 6 HGNC ID |
Not Available |
| Enzyme 6 Chromosome Location |
10 |
| Enzyme 6 Locus |
10q24.1-q25.1 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
Not Available |
| Enzyme 6 Metabolite References |
Not Available |