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Human Metabolome Database Version 2.5

 

Showing metabocard for 4,4-Dimethylcholesta-8,14,24-trienol (HMDB01023)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:58:29
Accession Number HMDB01023
Secondary Accession Numbers HMDB06924
Common Name 4,4-Dimethylcholesta-8,14,24-trienol
Description 4,4-Dimethylcholesta-8,14,24-trienol is a product of the enzyme delta14-sterol reductase [EC 1.3.1.70] (KEGG). It is involved in the biosynthesis of steroids and is involved in the conversion of lanosterol to zymosterol. In particular, lanosterol 14-alpha-demethylase, catalyzes the C-14 demethylation of lanosterol to form 4,4-Dimethylcholesta-8,14,24-trienol in the ergosterol biosynthesis pathway. It is thought to be a meiosis activating sterol.
Synonyms
  1. (3beta,5alpha)-4,4-Dimethylcholesta-8,14,24-trien-3-ol
  2. (3beta,5alpha)-4,4-dimethyl-Cholesta-8,14,24-trien-3-ol
  3. 4,4-Dimechol-8,14,24-trienol
  4. 4,4-Dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol
  5. 4,4-Dimethylcholesta-8,14,24-trienol
  6. 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol
  7. 4,4-dimethyl-5-alpha-cholesta-8,14,24-trien-3-beta-ol
  8. 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3-ol
  9. FF-MAS
  10. follicular fluid meiosis activating sterol
  11. 4,4-dimethyl-cholesta-8,14,24-trienol
Chemical IUPAC Name (3R,5S,10S,13S,17S)-4,4,10,13-tetramethyl-17-[(2R)-6-methylhept-5-en-2-yl]-1,2,3,5,6,7,11,12,16,17-decahydrocyclopenta[a]phenanthren-3-ol
Chemical Formula C29H46O
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Cholesterols and derivatives
Class
  • Steroids and Steroid Derivatives
Sub Class
  • Miscellaneous steroids
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
  • alkene
Biofunction
  • Hormones, Membrane component
Application
—
Source
  • Endogenous
Average Molecular Weight 410.675
Monoisotopic Molecular Weight 410.354858
Isomeric SMILES C[C@H](CCC=C(C)C)[C@H]1CC=C2C3=C(CC[C@]12C)[C@@]1(C)CC[C@H](O)C(C)(C)[C@@H]1CC3
Canonical SMILES CC(CCC=C(C)C)C1CC=C2C3=C(CCC12C)C1(C)CCC(O)C(C)(C)C1CC3
KEGG Compound ID C11455 Link Image
BioCyc ID 44-DIMETHYL-CHOLESTA-812-24-TRIENOL Link Image
BiGG ID 1454719 Link Image
Wikipedia Link Not Available
NuGOwiki Link HMDB01023 Link Image
Metagene Link HMDB01023 Link Image
METLIN ID 5952 Link Image
PubChem Compound 443212 Link Image
PubChem Substance 13626 Link Image
ChEBI ID 17813 Link Image
CAS Registry Number 64284-64-6
InChI Identifier InChI=1/C29H46O/c1-19(2)9-8-10-20(3)22-12-13-23-21-11-14-25-27(4,5)26(30)16-18-29(25,7)24(21)15-17-28(22,23)6/h9,13,20,22,25-26,30H,8,10-12,14-18H2,1-7H3/t20-,22-,25+,26+,28-,29-/m1/s1
Synthesis Reference Ruan B; Wilson W K; Schroepfer G J Jr An alternative synthesis of 4,4-dimethyl-5 alpha-cholesta-8,14,24-trien-3 beta-ol, an intermediate in sterol biosynthesis and a reported activator of meiosis and of nuclear orphan receptor LXR alpha. Bioorganic & medicinal chemistry letters (1998), 8(3), 233-6.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 1.01e-03 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 7.40 [Predicted by ALOGPS]; 6.9 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
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
  • Membrane (Predicted from LogP)
  • Cytoplasm
  • endoplasmic reticulum
Biofluid Location Not Available
Tissue Location
Tissue References
Testes —
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Steroid Biosynthesis SMP00023 Link Image map00100 Link Image
General References
  1. Ruan B, Watanabe S, Eppig JJ, Kwoh C, Dzidic N, Pang J, Wilson WK, Schroepfer GJ Jr: Sterols affecting meiosis: novel chemical syntheses and the biological activity and spectral properties of the synthetic sterols. J Lipid Res. 1998 Oct;39(10):2005-20. [PubMed Link Image]
Metabolic Enzymes
  1. Delta(14)-sterol reductase
  2. Cytochrome P450 51A1
  3. Cytochrome P450, family 51, subfamily A, polypeptide 1 (Cytochrome P450, family 51, subfamily A, polypeptide 1, isoform CRA_a)
Enzyme 1 [top]
Enzyme 1 ID 5494
Enzyme 1 Name Delta(14)-sterol reductase
Enzyme 1 Synonyms
  1. C-14 sterol reductase
  2. Sterol C14-reductase
  3. Delta-14-SR
  4. Transmembrane 7 superfamily member 2
  5. Another new gene 1 protein
  6. Putative sterol reductase SR- 1
Enzyme 1 Gene Name TM7SF2
Enzyme 1 Protein Sequence >Delta(14)-sterol reductase 
MAPTQGPRAPLEFGGPLGAAALLLLLPATMFHLLLAARSGPARLLGPPASLPGLEVLWSP
RALLLWLAWLGLQAALYLLPARKVAEGQELKDKSRLRYPINGFQALVLTALLVGLGMSAG
LPLGALPEMLLPLAFVATLTAFIFSLFLYMKAQVAPVSALAPGGNSGNPIYDFFLGRELN
PRICFFDFKYFCELRPGLIGWVLINLALLMKEAELRGSPSLAMWLVNGFQLLYVGDALWH
EEAVLTTMDITHDGFGFMLAFGDMAWVPFTYSLQAQFLLHHPQPLGLPMASVICLINATG
YYIFRGANSQKNTFRKNPSDPRVAGLETISTATGRKLLVSGWWGMVRHPNYLGDLIMALA
WSLPCGVSHLLPYFYLLYFTALLVHREARDERQCLQKYGLAWQEYCRRVPYRIMPYIY
Enzyme 1 Number of Residues 418
Enzyme 1 Molecular Weight 46407
Enzyme 1 Theoretical pI 9.04
Enzyme 1 GO Classification
Function
—
Process
—
Component
  • cell
  • membrane
Enzyme 1 General Function Not Available
Enzyme 1 Specific Function Involved in the conversion of lanosterol to cholesterol
Enzyme 1 Pathways Not Available
Enzyme 1 Reactions
  • 4,4-dimethyl-5alpha-cholesta-8,24-dien-3beta-ol + NADP+ = 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + NADPH + H+
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • 1-36
Enzyme 1 Transmembrane Regions Not Available
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 3211744 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID O76062 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name ERG24_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1770 bp 
ATGGAAGGCTTTGGGGGTGTCGGAGGCAGAGGGACCCGGGGGTTTGCAGCGAAGGGTGTC
TGGAGAGGGAGAGCTGAGGAGGGGCCGGTTCTGGGGGCTGCAGAACGGGGATTTATGGTG
TCGACTGGGAGCAGGAGGAGGGTCTTCGAGGGGCCTGGGGGCGGGGGACTAAGATGGACG
CCTGGGAAGGGAACTGGGAGGCAGCGGGGTGCCTGGGGGCCGAGGGCTGAGGACGGGGTG
CGGAGGCGCACTCTGGGAATGCCGAGAGGGTCCCGCAGAGACGTCAGGGCGCCGTGCGGG
CCGGCGGGGAGCTGGGGGGCTAGGGGCGGACGCCGACGTGATGGCCCTTCCCGCAGGCGC
CGCGGCTCTGCTACTGCTGCTGCCCGCCACCATGTTCCACCTGCTCCTGGCGGCCCGTTC
GGGCCCCGCGCGCCTGCTGGGTCCACCCGCGTCCCTGCCCGGGCTGGAGGTGCTGTGGAG
CCCACGGGCGCTGCTGCTGTGGCTCGCCTGGCTCGGCCTGCAGGCGGCGCTCTACCTACT
GCCGGCGCGCAAGGTGCGGGCCCCGCTCGCGGACGCTCGGGGGAGGGAAGCGAATGGGCT
CGGCGAGGGAAAGGACGCCCCGGGCCTTATCAGAGCCCCCTTGGACCCGCAGTGGCCGAG
GGGCAGGAATTGAAGGACAAGAGTCGCCTGCGCTATCCTATTAACGGCTTCCAGGCCCTG
GTGCTGACAGCCCTGTTGGTGGGGCTGGGGATGTCAGCGGGGCTGCCTCTGGGGGCGCTC
CCGGAAATGCTCCTGCCCTTGGCGTTTGTCGCCACCCTCACCGCTTTCATCTTCAGCCTC
TTTCTCTACATGAAGGCGCAGGTAGCCCCAGTTTCGGCCCTGGCACCTGGGGGGAACTCA
GGCAATCCGATTTACGACTTTTTTCTGGGACGAGAGCTCAACCCTCGTATCTGTTTCTTC
GACTTCAAATATTTCTGTGAACTGCGACCCGGCCTCATCGGCTGGGTCCTCATCAACCTG
GCCCTGTTGATGAAGGAGGCAGAGCTTCGAGGCAGTCCCTCACTGGCCATGTGGCTGGTC
AATGGCTTCCAGTTGCTCTACGTGGGTGATGCCCTCTGGCACGAGGAGGCCGTCCTCACC
ACCATGGATATCACACATGACGGGTTTGGCTTCATGCTGGCGTTTGGGGACATGGCCTGG
GTGCCCTTCACCTACAGCCTGCAGGCCCAGTTCCTGCTGCACCACCCGCAGCCCCTGGGG
TTGCCCATGGCCTCTGTCATCTGCCTCATCAATGCTACTGGTTACTACATCTTCCGTGGG
GCGAATTCCCAGAAAAACACTTTCCGAAAGAATCCTTCTGACCCCAGAGTGGCTGGGCTT
GAGACCATCTCTACAGCCACAGGGCGGAAACTGCTGGTGTCTGGGTGGTGGGGTATGGTC
CGCCATCCCAACTATCTTGGAGACCTCATCATGGCTCTGGCTTGGTCCTTGCCCTGCGGG
GTGTCACACCTGCTGCCCTACTTCTACCTCCTCTACTTCACCGCGCTGCTGGTGCACCGT
GAGGCCCGGGATGAGCGGAGTGCCTGCAGAAGTACGGCCTGGCCTGGCAGGAGTACTGCC
GGCGTGTGCCTTACCGCATCATGCCCTACATCTACTGAAGCGGCTCCACCACCCCAGGTG
GGGCATGTGCCCACTCATCCACCAGCACACCCAGGACCAGGAGCCTCGACACACTTGGGA
CTCAAGGGCTTGCACCCCACCCAGCCCTGA
Enzyme 1 GenBank Gene ID AF048704 Link Image
Enzyme 1 GeneCard ID TM7SF2 Link Image
Enzyme 1 GenAtlas ID TM7SF2 Link Image
Enzyme 1 HGNC ID HGNC:11863 Link Image
Enzyme 1 Chromosome Location Not Available
Enzyme 1 Locus Not Available
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Lemmens IH, Kas K, Merregaert J, Van de Ven WJ: Identification and molecular characterization of TM7SF2 in the FAUNA gene cluster on human chromosome 11q13. Genomics. 1998 May 1;49(3):437-42. [PubMed Link Image]
  2. Holmer L, Pezhman A, Worman HJ: The human lamin B receptor/sterol reductase multigene family. Genomics. 1998 Dec 15;54(3):469-76. [PubMed Link Image]
  3. Roberti R, Bennati AM, Galli G, Caruso D, Maras B, Aisa C, Beccari T, Della Fazia MA, Servillo G: Cloning and expression of sterol Delta 14-reductase from bovine liver. Eur J Biochem. 2002 Jan;269(1):283-90. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5497
Enzyme 2 Name Cytochrome P450 51A1
Enzyme 2 Synonyms
  1. CYPLI
  2. P450LI
  3. Sterol 14-alpha demethylase
  4. Lanosterol 14-alpha demethylase
  5. LDM
  6. P450-14DM
  7. P45014DM
Enzyme 2 Gene Name CYP51A1
Enzyme 2 Protein Sequence >Cytochrome P450 51A1 
MLLLGLLQAGGSVLGQAMEKVTGGNLLSMLLIACAFTLSLVYLIRLAAGHLVQLPAGVKS
PPYIFSPIPFLGHAIAFGKSPIEFLENAYEKYGPVFSFTMVGKTFTYLLGSDAAALLFNS
KNEDLNAEDVYSRLTTPVFGKGVAYDVPNPVFLEQKKMLKSGLNIAHFKQHVSIIEKETK
EYFESWGESGEKNVFEALSELIILTASHCLHGKEIRSQLNEKVAQLYADLDGGFSHAAWL
LPGWLPLPSFRRRDRAHREIKDIFYKAIQKRRQSQEKIDDILQTLLDATYKDGRPLTDDE
VAGMLIGLLLAGQHTSSTTSAWMGFFLARDKTLQKKCYLEQKTVCGENLPPLTYDQLKDL
NLLDRCIKETLRLRPPIMIMMRMARTPQTVAGYTIPPGHQVCVSPTVNQRLKDSWVERLD
FNPDRYLQDNPASGEKFAYVPFGAGRHRCIGENFAYVQIKTIWSTMLRLYEFDLIDGYFP
TVNYTTMIHTPENPVIRYKRRSK
Enzyme 2 Number of Residues 503
Enzyme 2 Molecular Weight 56807
Enzyme 2 Theoretical pI 8.72
Enzyme 2 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • heme binding
  • ion binding
  • iron ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • tetrapyrrole binding
  • transition metal ion binding
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
—
Enzyme 2 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 2 Specific Function Catalyzes C14-demethylation of lanosterol; it transforms lanosterol into 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol
Enzyme 2 Pathways Not Available
Enzyme 2 Reactions
  • obtusifoliol + 3 O2 + 3 NADPH + 3 H+ = 4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + 3 NADP+ + 3 H2O
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • 24-44
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 1698396 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q16850 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name CP51A_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1530 bp 
ATGGCGGCGGCGGCTGGGATGCTGCTGCTGGGCTTGCTGCAGGCGGGTGGGTCGGTGCTG
GGCCAGGCGATGGAGAAGGTGACAGGCGGCAACCTCTTGTCCATGCTGCTGATCGCCTGC
GCCTTCACCCTCAGCCTGGTCTACCTGATCCGTCTGGCCGCCGGCCACCTGGTCCAGCTG
CCCGCAGGGGTGAAAAGTCCTCCATACATTTTCTCCCCAATTCCATTCCTTGGGCATGCC
ATAGCATTTGGGAAAAGTCCAATTGAATTTCTAGAAAATGCATATGAGAAGTATGGACCT
GTATTTAGTTTTACCATGGTAGGCAAGACATTTACTTACCTTCTGGGGAGTGATGCTGCT
GCACTGCTTTTTAATAGTAAAAATGAAGACCTGAATGCAGAAGATGTCTACAGTCGCCTG
ACAACACCTGTGTTTGGGAAGGGAGTTGCATACGATGTGCCTAATCCAGTTTTCTTGGAG
CAGAAGAAAATGTTAAAAAGTGGCCTTAACATAGCCCACTTTAAACAGCATGTTTCTATA
ATTGAAAAAGAAACAAAGGAATACTTTGAGAGTTGGGGAGAAAGTGGAGAAAAAAATGTG
TTTGAAGCTCTTTCTGAGCTCATAATTTTAACAGCTAGCCATTGTTTGCATGGAAAGGAA
ATCAGAAGTCAACTCAATGAAAAGGTAGCACAGCTGTATGCAGATTTGGATGGAGGTTTC
AGCCATGCAGCCTGGCTCTTACCAGGTTGGCTGCCTTTGCCTAGTTTCAGACGCAGGGAC
AGAGCTCATCGGGAAATCAAGGATATTTTCTATAAGGCAATCCAGAAACGCAGACAGTCT
CAAGAAAAAATTGATGACATTCTCCAAACTTTACTAGATGCTACATACAAGGATGGGCGT
CCTTTGACTGATGATGAAGTAGCAGGGATGCTTATTGGATTACTCTTGGCAGGGCAGCAT
ACATCCTCAACTACTAGTGCTTGGATGGGCTTCTTTTTGGCCAGAGACAAAACACTTCAA
AAAAAATGTTATTTAGAACAGAAAACAGTCTGTGGAGAGAATCTGCCTCCTTTAACTTAT
GACCAGCTCAAGGATCTAAATTTACTTGATCGCTGTATAAAAGAAACATTAAGACTTAGA
CCTCCTATAATGATCATGATGAGAATGGCCAGAACTCCTCAGACTGTGGCAGGGTATACC
ATTCCTCCAGGACATCAGGTGTGTGTTTCTCCCACTGTCAATCAAAGACTTAAAGACTCA
TGGGTAGAACGCCTGGACTTTAATCCTGATCGCTACTTACAGGATAACCCAGCATCAGGG
GAAAAGTTTGCCTATGTGCCATTTGGAGCTGGGCGTCATCGTTGTATTGGGGAAAATTTT
GCCTATGTTCAAATTAAGACAATTTGGTCCACTATGCTTCGTTTATATGAATTTGATCTC
ATTGATGGATACTTTCCCACTGTGAATTATACAACTATGATTCACACCCCTGAGAACCCA
GTTATCCGTTACAAACGAAGATCAAAATGA
Enzyme 2 GenBank Gene ID U23942 Link Image
Enzyme 2 GeneCard ID CYP51A1 Link Image
Enzyme 2 GenAtlas ID CYP51A1 Link Image
Enzyme 2 HGNC ID HGNC:2649 Link Image
Enzyme 2 Chromosome Location Not Available
Enzyme 2 Locus Not Available
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Stromstedt M, Rozman D, Waterman MR: The ubiquitously expressed human CYP51 encodes lanosterol 14 alpha-demethylase, a cytochrome P450 whose expression is regulated by oxysterols. Arch Biochem Biophys. 1996 May 1;329(1):73-81. [PubMed Link Image]
  2. Rozman D, Stromstedt M, Waterman MR: The three human cytochrome P450 lanosterol 14 alpha-demethylase (CYP51) genes reside on chromosomes 3, 7, and 13: structure of the two retrotransposed pseudogenes, association with a line-1 element, and evolution of the human CYP51 family. Arch Biochem Biophys. 1996 Sep 15;333(2):466-74. [PubMed Link Image]
  3. Rozman D, Stromstedt M, Tsui LC, Scherer SW, Waterman MR: Structure and mapping of the human lanosterol 14alpha-demethylase gene (CYP51) encoding the cytochrome P450 involved in cholesterol biosynthesis; comparison of exon/intron organization with other mammalian and fungal CYP genes. Genomics. 1996 Dec 15;38(3):371-81. [PubMed Link Image]
  4. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 15218
Enzyme 3 Name Cytochrome P450, family 51, subfamily A, polypeptide 1 (Cytochrome P450, family 51, subfamily A, polypeptide 1, isoform CRA_a)
Enzyme 3 Synonyms Not Available
Enzyme 3 Gene Name CYP51A1
Enzyme 3 Protein Sequence >Cytochrome P450, family 51, subfamily A, polypeptide 1 (Cytochrome P450, family 51, subfamily A, polypeptide 1, isoform CRA_a) 
MAAAAGMLLLGLLQAGGSVLGQAMEKVTGGNLLSMLLIACAFTLSLVYLIRLAAGHLVQL
PAGVKSPPYIFSPIPFLGHAIAFGKSPIEFLENAYEKYGPVFSFTMVGKTFTYLLGSDAA
ALLFNSKNEDLNAEDVYSRLTTPVFGKGVAYDVPNPVFLEQKKMLKSGLNIAHFKQHVSI
IEKETKEYFESWGESGEKNVFEALSELIILTASHCLHGKEIRSQLNEKVAQLYADLDGGF
SHAAWLLPGWLPLPSFRRRDRAHREIKDIFYKAIQKRRQSQEKIDDILQTLLDATYKDGR
PLTDDEVAGMLIGLLLAGQHTSSTTSAWMGFFLARDKTLQKKCYLEQKTVCGENLPPLTY
DQLKDLNLLDRCIKETLRLRPPIMIMMRMARTPQTVAGYTIPPGHQVCVSPTVNQRLKDS
WVERLDFNPDRYLQDNPASGEKFAYVPFGAGRHRCIGENFAYVQIKTIWSTMLRLYEFDL
IDGYFPTVNYTTMIHTPENPVIRYKRRSK
Enzyme 3 Number of Residues 509
Enzyme 3 Molecular Weight 57279
Enzyme 3 Theoretical pI 8.72
Enzyme 3 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • endopeptidase activity
  • heme binding
  • hydrolase activity
  • ion binding
  • iron ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • peptidase activity
  • serine-type endopeptidase activity
  • tetrapyrrole binding
  • transition metal ion binding
Process
  • cellular metabolism
  • cellular protein metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein metabolism
  • proteolysis
Component
—
Enzyme 3 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 3 Specific Function Not Available
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions Not Available
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein Not Available
Enzyme 3 UniProtKB/Swiss-Prot ID A4D1F8 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name A4D1F8_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence Not Available
Enzyme 3 GenBank Gene ID CH236949 Link Image
Enzyme 3 GeneCard ID A4D1F8 Link Image
Enzyme 3 GenAtlas ID Not Available
Enzyme 3 HGNC ID Not Available
Enzyme 3 Chromosome Location Not Available
Enzyme 3 Locus Not Available
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available