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Human Metabolome Database Version 2.5

 

Showing metabocard for 4a-Methylzymosterol (HMDB01217)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:58:36
Accession Number HMDB01217
Secondary Accession Numbers HMDB06926
Common Name 4a-Methylzymosterol
Description 4a-Methylzymosterol is an intermediate in the biosynthesis of steroids (KEGG ID C05103). It is the 7th to last step in the synthesis of vitamin D2 and is converted from 3-keto-4-methtylzymosterol via the enzyme 3-keto steroid reductase [EC:1.1.1.270]. It is then converted to zymosterol. (KEGG)
Synonyms
  1. 4alpha-methyl-5alpha-cholesta-8,24-dien-3beta-ol
  2. 4a-methyl-5a-cholesta-8,24-dien-3b-ol
  3. (3b,4a,5a)-4-methylcholesta-8,24-dien-3-ol
  4. (3beta,4alpha,5alpha)-4-methylcholesta-8,24-dien-3-ol
  5. 4alpha-Methylzymosterol
  6. 4a-Methylzymosterol
  7. (4S,5S)-4,10,13-trimethyl-17-(6-methylhept-5-en-2-yl)-2,3,4,5,6,7,11,12,14, 15,16,17-dodecahydro-1H-cyclopenta[a]phenanthren-3-ol
Chemical IUPAC Name (4S,5S)-4,10,13-trimethyl-17-(6-methylhept-5-en-2-yl)-2,3,4,5,6,7,11,12,14, 15,16,17-dodecahydro-1H-cyclopenta[a]phenanthren-3-ol
Chemical Formula C28H46O
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 398.664
Monoisotopic Molecular Weight 398.354858
Isomeric SMILES C[C@H](CCC=C(/C)C)[C@H]1CC[C@H]2C3=C(CC[C@]12C)[C@@]1(C)CC[C@H](O)[C@@H](C)[C@@H]1CC3
Canonical SMILES CC(CCC=C(C)C)C1CCC2C3=C(CCC12C)C1(C)CCC(O)C(C)C1CC3
KEGG Compound ID C05103 Link Image
BioCyc ID 4-METHYL-824-CHOLESTADIENOL Link Image
BiGG ID Not Available
Wikipedia Link Not Available
NuGOwiki Link HMDB01217 Link Image
Metagene Link HMDB01217 Link Image
METLIN ID 6087 Link Image
PubChem Compound 22212495 Link Image
PubChem Substance 7531 Link Image
ChEBI ID 1949 Link Image
CAS Registry Number 7448-03-5
InChI Identifier InChI=1/C28H46O/c1-18(2)8-7-9-19(3)22-12-13-24-21-10-11-23-20(4)26(29)15-17-28(23,6)25(21)14-16-27(22,24)5/h8,19-20,22-24,26,29H,7,9-17H2,1-6H3/t19-,20+,22-,23+,24+,26+,27-,28+/m1/s1
Synthesis Reference Not Available
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 7.04e-04 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 6.52 [Predicted by ALOGPS]; 7.1 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
MOL File Show Link Image
SDF File Show Link Image
PDB File Show Link Image
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 Not Available
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
Name SMPDB Link KEGG Link
Steroid Biosynthesis SMP00023 Link Image map00100 Link Image
General References Not Available
Metabolic Enzymes
  1. 3-keto-steroid reductase
Enzyme 1 [top]
Enzyme 1 ID 6129
Enzyme 1 Name 3-keto-steroid reductase
Enzyme 1 Synonyms
  1. 17-beta-hydroxysteroid dehydrogenase 7
  2. 17-beta-HSD 7
  3. Estradiol 17-beta-dehydrogenase 7
Enzyme 1 Gene Name HSD17B7
Enzyme 1 Protein Sequence >3-keto-steroid reductase
MRKVVLITGASSGIGLALCKRLLAEDDELHLCLACRNMSKAEAVCAALLASHPTAEVTIV
QVDVSNLQSVFRASKELKQRFQRLDCIYLNAGIMPNPQLNIKALFFGLFSRKVIHMFSTA
EGLLTQGDKITADGLQEVFETNVFGHFILIRELEPLLCHSDNPSQLIWTSSRSARKSNFS
LEDFQHSKGKEPYSSSKYATDLLSVALNRNFNQQGLYSNVACPGTALTNLTYGILPPFIW
TLLMPAILLLRFFANAFTLTPYNGTEALVWLFHQKPESLNPLIKYLSATTGFGRNYIMTQ
KMDLDEDTAEKFYQKLLELEKHIRVTIQKTDNQARLSGSCL
Enzyme 1 Number of Residues 341
Enzyme 1 Molecular Weight 38205.8
Enzyme 1 Theoretical pI 8.21
Enzyme 1 GO Classification
Function
  • binding
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 1 General Function Involved in oxidoreductase activity
Enzyme 1 Specific Function Responsible for the reduction of the keto group on the C-3 of sterols
Enzyme 1 Pathways
  • Androgen and Estrogen Metabolism (map00150 Link Image)
Enzyme 1 Reactions
  • 4alpha-methyl-5alpha-cholest-7-en-3beta-ol + NADP+ = 4alpha-methyl-5alpha-cholest-7-en-3-one + NADPH + H+ [RN:R05691]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • 230-250
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 6721095 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P56937 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name DHB7_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1026 bp
ATGCGAAAGGTGGTTTTGATCACCGGGGCTAGCAGTGGCATTGGCCTGGCCCTCTGCAAG
CGGCTGCTGGCGGAAGATGATGAGCTTCATCTGTGTTTGGCGTGCAGGAACATGAGCAAG
GCAGAAGCTGTCTGTGCTGCTCTGCTGGCCTCTCACCCCACTGCTGAGGTCACCATTGTC
CAGGTGGATGTCAGCAACCTGCAGTCGGTCTTCCGGGCCTCCAAGGAACTTAAGCAAAGG
TTTCAGAGATTAGACTGTATATATCTAAATGCTGGGATCATGCCTAATCCACAACTAAAT
ATCAAAGCACTTTTCTTTGGCCTCTTTTCAAGAAAAGTGATTCATATGTTCTCCACAGCT
GAAGGCCTGCTGACCCAGGGTGATAAGATCACTGCTGATGGACTTCAGGAGGTGTTTGAG
ACCAATGTCTTTGGCCATTTTATCCTGATTCGGGAACTGGAGCCTCTCCTCTGTCACAGT
GACAATCCATCTCAGCTCATCTGGACATCATCTCGCAGTGCAAGGAAATCTAATTTCAGC
CTCGAGGACTTCCAGCACAGCAAAGGCAAGGAACCCTACAGCTCTTCCAAATATGCCACT
GACCTTTTGAGTGTGGCTTTGAACAGGAACTTCAACCAGCAGGGTCTCTATTCCAATGTG
GCCTGTCCAGGTACAGCATTGACCAATTTGACATATGGAATTCTGCCTCCGTTTATATGG
ACGCTGTTGATGCCGGCAATATTGCTACTTCGCTTTTTTGCAAATGCATTCACTTTGACA
CCATATAATGGAACAGAAGCTCTGGTATGGCTTTTCCACCAAAAGCCTGAATCTCTCAAT
CCTCTGATCAAATATCTGAGTGCCACCACTGGCTTTGGAAGAAATTATATTATGACCCAG
AAGATGGACCTAGATGAAGACACTGCTGAAAAATTTTATCAAAAGTTACTGGAACTGGAA
AAGCACATTAGGGTCACTATTCAAAAAACAGATAATCAGGCCAGGCTCAGTGGCTCATGC
CTATAA
Enzyme 1 GenBank Gene ID AF098786 Link Image
Enzyme 1 GeneCard ID HSD17B7 Link Image
Enzyme 1 GenAtlas ID HSD17B7 Link Image
Enzyme 1 HGNC ID HGNC:5215 Link Image
Enzyme 1 Chromosome Location 1
Enzyme 1 Locus 1q23
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Krazeisen A, Breitling R, Imai K, Fritz S, Moller G, Adamski J: Determination of cDNA, gene structure and chromosomal localization of the novel human 17beta-hydroxysteroid dehydrogenase type 7(1). FEBS Lett. 1999 Oct 29;460(2):373-9. [PubMed Link Image]
  2. Torn S, Nokelainen P, Kurkela R, Pulkka A, Menjivar M, Ghosh S, Coca-Prados M, Peltoketo H, Isomaa V, Vihko P: Production, purification, and functional analysis of recombinant human and mouse 17beta-hydroxysteroid dehydrogenase type 7. Biochem Biophys Res Commun. 2003 May 23;305(1):37-45. [PubMed Link Image]
  3. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Marijanovic Z, Laubner D, Moller G, Gege C, Husen B, Adamski J, Breitling R: Closing the gap: identification of human 3-ketosteroid reductase, the last unknown enzyme of mammalian cholesterol biosynthesis. Mol Endocrinol. 2003 Sep;17(9):1715-25. Epub 2003 Jun 26. [PubMed Link Image]
  8. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available