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Human Metabolome Database Version 2.5

 

Showing metabocard for 11b-Hydroxyandrost-4-ene-3,17-dione (HMDB06773)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2008-08-08 11:29:51
Update Date 2009-06-08 12:02:28
Accession Number HMDB06773
Secondary Accession Numbers Not Available
Common Name 11b-Hydroxyandrost-4-ene-3,17-dione
Description 11beta-Hydroxyandrost-4-ene-3,17-dione is an intermediate in adrenosterone production. 11beta-Hydroxyandrost-4-ene-3,17-dione is produced from androst-4-ene-3,17-dione, a reaction catalyzed by the enzyme cytochrome P450 B [EC:1.14.15.4]. 11beta-Hydroxyandrost-4-ene-3,17-dione is then converted into adrenosterone by the enzyme 11beta-hydroxysteroid dehydrogenase [EC:1.1.1.146].
Synonyms
  1. Androst-4-ene-3,17-dione-11beta-ol
  2. 4-Androsten-11beta-ol-3,17-dione
  3. 11beta-Hydroxyandrost-4-ene-3,17-dione
Chemical IUPAC Name Not Available
Chemical Formula C19H26O3
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Cholesterols and derivatives
Class
  • Steroids and Steroid Derivatives
Sub Class
  • Ketosteroids
Family
  • Mammalian Metabolite
Species
  • ketone
  • secondary alcohol
  • alkene
Biofunction
Application
Source
  • Endogenous
Average Molecular Weight 302.408
Monoisotopic Molecular Weight 302.188202
Isomeric SMILES C[C@]12C[C@H](O)[C@H]3[C@@H](CCC4=CC(=O)CC[C@]34C)[C@@H]1CCC2=O
Canonical SMILES CC12CC(O)C3C(CCC4=CC(=O)CCC34C)C1CCC2=O
KEGG Compound ID C05284 Link Image
BioCyc ID Not Available
BiGG ID Not Available
Wikipedia Link Not Available
NuGOwiki Link HMDB06773 Link Image
Metagene Link HMDB06773 Link Image
METLIN ID Not Available
PubChem Compound Not Available
PubChem Substance Not Available
ChEBI ID Not Available
CAS Registry Number 382-44-5
InChI Identifier InChI=1/C19H26O3/c1-18-8-7-12(20)9-11(18)3-4-13-14-5-6-16(22)19(14,2)10-15(21)17(13)18/h9,13-15,17,21H,3-8,10H2,1-2H3/t13-,14-,15?,17+,18-,19-/m0/s1
Synthesis Reference Not Available
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 0.082100004 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 2.00 [Predicted by ALOGPS] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
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 Not Available
General References Not Available
Metabolic Enzymes
  1. Cytochrome P450 11B1, mitochondrial
  2. Cytochrome P450 11B2, mitochondrial
  3. Corticosteroid 11-beta-dehydrogenase isozyme 1
  4. Hydroxysteroid (11-beta) dehydrogenase 2
  5. Mitochondrial cytochrome P450, family 11, subfamily B, polypeptide 2 (Cytochrome P450, family 11, subfamily B, polypeptide 2)
  6. cDNA, FLJ94621, Homo sapiens hydroxysteroid (11-beta) dehydrogenase 1 (HSD11B1), mRNA (Hydroxysteroid (11-beta) dehydrogenase 1, isoform CRA_a)
Enzyme 1 [top]
Enzyme 1 ID 5683
Enzyme 1 Name Cytochrome P450 11B1, mitochondrial
Enzyme 1 Synonyms
  1. CYPXIB1
  2. Cytochrome P-450c11
  3. Cytochrome P450C11
  4. Steroid 11-beta-hydroxylase
Enzyme 1 Gene Name CYP11B1
Enzyme 1 Protein Sequence >Cytochrome P450 11B1, mitochondrial
MALRAKAEVCMAVPWLSLQRAQALGTRAARVPRTVLPFEAMPRRPGNRWLRLLQIWREQG
YEDLHLEVHQTFQELGPIFRYDLGGAGMVCVMLPEDVEKLQQVDSLHPHRMSLEPWVAYR
QHRGHKCGVFLLNGPEWRFNRLRLNPEVLSPNAVQRFLPMVDAVARDFSQALKKKVLQNA
RGSLTLDVQPSIFHYTIEASNLALFGERLGLVGHSPSSASLNFLHALEVMFKSTVQLMFM
PRSLSRWTSPKVWKEHFEAWDCIFQYGDNCIQKIYQELAFSRPQQYTSIVAELLLNAELS
PDAIKANSMELTAGSVDTTVFPLLMTLFELARNPNVQQALRQESLAAAASISEHPQKATT
ELPLLRAALKETLRLYPVGLFLERVASSDLVLQNYHIPAGTLVRVFLYSLGRNPALFPRP
ERYNPQRWLDIRGSGRNFYHVPFGFGMRQCLGRRLAEAEMLLLLHHVLKHLQVETLTQED
IKMVYSFILRPSMFPLLTFRAIN
Enzyme 1 Number of Residues 503
Enzyme 1 Molecular Weight 57572.4
Enzyme 1 Theoretical pI 9.65
Enzyme 1 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • mitochondrion
  • organelle
Enzyme 1 General Function Involved in monooxygenase activity
Enzyme 1 Specific Function Has steroid 11-beta-hydroxylase activity. In addition to this activity, the 18 or 19-hydroxylation of steroids and the aromatization of androstendione to estrone have also been ascribed to cytochrome P450 XIB
Enzyme 1 Pathways
Enzyme 1 Reactions
  • a steroid + reduced adrenal ferredoxin + O2 = an 11beta-hydroxysteroid + oxidized adrenal ferredoxin + H2O [RN:R02726]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 30184 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P15538 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name C11B1_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1512 bp
ATGGCACTCAGGGCAAAGGCAGAGGTGTGCATGGCAGTGCCCTGGCTGTCCCTGCAAAGG
GCACAGGCACTGGGCACGAGAGCCGCCCGGGTCCCCAGGACAGTGCTGCCCTTTGAAGCC
ATGCCCCAGCGTCCAGGCAACAGGTGGCTGAGGCTGCTGCAGATCTGGAGGGAGCAGGGT
TATGAGGACCTGCACCTGGAAGTACACCAGACCTTCCAGGAACTGGGGCCCATTTTCAGG
TACGACTTGGGAGGAGCAGGCATGGTGTGTGTGATGCTGCCGGAGGACGTGGAGAAGCTG
CAACAGGTGGACAGCCTGCATCCCCACAGGATGAGCCTGGAGCCCTGGGTGGCCTACAGA
CAACATCGTGGGCACAAATGTGGCGTGTTCTTGCTGAATGGGCCTGAATGGCGCTTCAAC
CGATTGCGGCTGAATCCAGAAGTGCTGTCGCCCAACGCTGTGCAGAGGTTCCTCCCGATG
GTGGATGCAGTGGCCAGGGACTTCTCCCAGGCCCTGAAGAAGAAGGTGCTGCAGAACGCC
CGGGGGAGCCTGACCCTGGACGTCCAGCCCAGCATCTTCCACTACACCATAGAAGCCAGC
AACTTGGCTCTTTTTGGAGAGCGGCTGGGCCTGGTTGGCCACAGCCCCAGTTCTGCCAGC
CTGAACTTCCTCCATGCCCTGGAGGTCATGTTCAAATCCACCGTCCAGCTCATGTTCATG
CCCAGGAGCCTGTCTCGCTGGACCAGCCCCAAGGTGTGGAAGGAGCACTTTGAGGCCTGG
GACTGCATCTTCCAGTACGGCGACAACTGTATCCAGAAAATCTATCAGGAACTGGCCTTC
AGCCGCCCTCAACAGTACACCAGCATCGTGGCGGAGCTCCTGTTGAATGCGGAACTGTCG
CCAGATGCCATCAAGGCCAACTCTATGGAACTCACTGCAGGGAGCGTGGACACGACGGTG
TTTCCCTTGCTGATGACGCTCTTTGAGCTGGCTCGGAACCCCAACGTGCAGCAGGCCCTG
CGCCAGGAGAGCCTGGCCGCCGCAGCCAGCATCAGTGAACATCCCCAGAAGGCAACCACC
GAGCTCCCCTTGCTGCGTGCGGCCCTCAAGGAGACCTTGCGGCTCTACCCTGTGGGTCTG
TTTCTGGAGCGAGTGGTGAGCTCAGACTTGGTGCTTCAGAACTACCACATCCCAGCTGGG
ACATTGGTGCGCGTGTTCCTCTACTCTCTGGGTCGCAACCCCGCCTTGTTCCCGAGGCCT
GAGCGCTATAACCCCCAGCGCTGGCTAGACATCAGGGGCTCCGGCAGGAACTTCTACCAC
GTGCCCTTTGGCTTTGGCATGCGCCAGTGCCTTGGGCGGCGCCTGGCAGAGGCAGAGATG
CTGCTGCTGCTGCACCATGTGCTGAAACACCTCCAGGTGGAGACACTAACCCAAGAGGAC
ATAAAGATGGTCTACAGCTTCATATTGAGGCCCAGCATGTTCCCCCTCCTCACCTTCAGA
GCCATCAACTAA
Enzyme 1 GenBank Gene ID X55764 Link Image
Enzyme 1 GeneCard ID CYP11B1 Link Image
Enzyme 1 GenAtlas ID CYP11B1 Link Image
Enzyme 1 HGNC ID HGNC:2591 Link Image
Enzyme 1 Chromosome Location 8
Enzyme 1 Locus 8q21
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Mornet E, Dupont J, Vitek A, White PC: Characterization of two genes encoding human steroid 11 beta-hydroxylase (P-450(11) beta). J Biol Chem. 1989 Dec 15;264(35):20961-7. [PubMed Link Image]
  2. Kawamoto T, Mitsuuchi Y, Toda K, Miyahara K, Yokoyama Y, Nakao K, Hosoda K, Yamamoto Y, Imura H, Shizuta Y: Cloning of cDNA and genomic DNA for human cytochrome P-45011 beta. FEBS Lett. 1990 Sep 3;269(2):345-9. [PubMed Link Image]
  3. Nusbaum C, Mikkelsen TS, Zody MC, Asakawa S, Taudien S, Garber M, Kodira CD, Schueler MG, Shimizu A, Whittaker CA, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Yang X, Allen NR, Anderson S, Asakawa T, Blechschmidt K, Bloom T, Borowsky ML, Butler J, Cook A, Corum B, DeArellano K, DeCaprio D, Dooley KT, Dorris L 3rd, Engels R, Glockner G, Hafez N, Hagopian DS, Hall JL, Ishikawa SK, Jaffe DB, Kamat A, Kudoh J, Lehmann R, Lokitsang T, Macdonald P, Major JE, Matthews CD, Mauceli E, Menzel U, Mihalev AH, Minoshima S, Murayama Y, Naylor JW, Nicol R, Nguyen C, O'Leary SB, O'Neill K, Parker SC, Polley A, Raymond CK, Reichwald K, Rodriguez J, Sasaki T, Schilhabel M, Siddiqui R, Smith CL, Sneddon TP, Talamas JA, Tenzin P, Topham K, Venkataraman V, Wen G, Yamazaki S, Young SK, Zeng Q, Zimmer AR, Rosenthal A, Birren BW, Platzer M, Shimizu N, Lander ES: DNA sequence and analysis of human chromosome 8. Nature. 2006 Jan 19;439(7074):331-5. [PubMed Link Image]
  4. 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]
  5. Naiki Y, Kawamoto T, Mitsuuchi Y, Miyahara K, Toda K, Orii T, Imura H, Shizuta Y: A nonsense mutation (TGG [Trp116]-->TAG [Stop]) in CYP11B1 causes steroid 11 beta-hydroxylase deficiency. J Clin Endocrinol Metab. 1993 Dec;77(6):1677-82. [PubMed Link Image]
  6. Chua SC, Szabo P, Vitek A, Grzeschik KH, John M, White PC: Cloning of cDNA encoding steroid 11 beta-hydroxylase (P450c11). Proc Natl Acad Sci U S A. 1987 Oct;84(20):7193-7. [PubMed Link Image]
  7. Kawamoto T, Mitsuuchi Y, Toda K, Yokoyama Y, Miyahara K, Miura S, Ohnishi T, Ichikawa Y, Nakao K, Imura H, et al.: Role of steroid 11 beta-hydroxylase and steroid 18-hydroxylase in the biosynthesis of glucocorticoids and mineralocorticoids in humans. Proc Natl Acad Sci U S A. 1992 Feb 15;89(4):1458-62. [PubMed Link Image]
  8. White PC, Dupont J, New MI, Leiberman E, Hochberg Z, Rosler A: A mutation in CYP11B1 (Arg-448----His) associated with steroid 11 beta-hydroxylase deficiency in Jews of Moroccan origin. J Clin Invest. 1991 May;87(5):1664-7. [PubMed Link Image]
  9. Joehrer K, Geley S, Strasser-Wozak EM, Azziz R, Wollmann HA, Schmitt K, Kofler R, White PC: CYP11B1 mutations causing non-classic adrenal hyperplasia due to 11 beta-hydroxylase deficiency. Hum Mol Genet. 1997 Oct;6(11):1829-34. [PubMed Link Image]
  10. Loidi L, Quinteiro C, Barros F, Dominguez F, Barreiro J, Pombo M: The C494F variant in the CYP11B1 gene is a sequence polymorphism in the Spanish population. J Clin Endocrinol Metab. 1999 Dec;84(12):4749. [PubMed Link Image]
  11. Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed Link Image]
  12. 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 Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5808
Enzyme 2 Name Cytochrome P450 11B2, mitochondrial
Enzyme 2 Synonyms
  1. Aldosterone synthase
  2. ALDOS
  3. Aldosterone-synthesizing enzyme
  4. CYPXIB2
  5. Cytochrome P-450Aldo
  6. Cytochrome P-450C18
  7. Steroid 18-hydroxylase
Enzyme 2 Gene Name CYP11B2
Enzyme 2 Protein Sequence >Cytochrome P450 11B2, mitochondrial
MALRAKAEVCVAAPWLSLQRARALGTRAARAPRTVLPFEAMPQHPGNRWLRLLQIWREQG
YEHLHLEMHQTFQELGPIFRYNLGGPRMVCVMLPEDVEKLQQVDSLHPCRMILEPWVAYR
QHRGHKCGVFLLNGPEWRFNRLRLNPDVLSPKAVQRFLPMVDAVARDFSQALKKKVLQNA
RGSLTLDVQPSIFHYTIEASNLALFGERLGLVGHSPSSASLNFLHALEVMFKSTVQLMFM
PRSLSRWISPKVWKEHFEAWDCIFQYGDNCIQKIYQELAFNRPQHYTGIVAELLLKAELS
LEAIKANSMELTAGSVDTTAFPLLMTLFELARNPDVQQILRQESLAAAASISEHPQKATT
ELPLLRAALKETLRLYPVGLFLERVVSSDLVLQNYHIPAGTLVQVFLYSLGRNAALFPRP
ERYNPQRWLDIRGSGRNFHHVPFGFGMRQCLGRRLAEAEMLLLLHHVLKHFLVETLTQED
IKMVYSFILRPGTSPLLTFRAIN
Enzyme 2 Number of Residues 503
Enzyme 2 Molecular Weight 57559.6
Enzyme 2 Theoretical pI 9.78
Enzyme 2 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • mitochondrion
  • organelle
Enzyme 2 General Function Involved in monooxygenase activity
Enzyme 2 Specific Function Preferentially catalyzes the conversion of 11- deoxycorticosterone to aldosterone via corticosterone and 18- hydroxycorticosterone
Enzyme 2 Pathways
Enzyme 2 Reactions
  • corticosterone + reduced adrenal ferredoxin + O2 = 18-hydroxycorticosterone + oxidized adrenal ferredoxin + H2O [RN:R03262]
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 119829183 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P19099 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name C11B2_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1512 bp
ATGGCACTCAGGGCAAAGGCAGAGGTGTGCGTGGCAGCGCCCTGGCTGTCCCTGCAAAGG
GCACGGGCACTGGGCACTAGAGCCGCTCGGGCCCCTAGGACGGTGCTGCCGTTTGAAGCC
ATGCCCCAGCATCCAGGCAACAGGTGGCTGAGGCTGCTGCAGATCTGGAGGGAGCAGGGT
TATGAGCACCTGCACCTGGAGATGCACCAGACCTTCCAGGAGCTGGGGCCCATTTTCAGG
TACAACTTGGGAGGACCACGCATGGTGTGTGTGATGCTGCCGGAGGATGTGGAGAAGCTG
CAACAGGTGGACAGCCTGCATCCCTGCAGGATGATCCTGGAGCCCTGGGTGGCCTACAGA
CAACATCGTGGGCACAAATGTGGCGTGTTCTTGTTGAATGGGCCTGAATGGCGCTTCAAC
CGATTGCGGCTGAACCCAGATGTGCTGTCGCCCAAGGCCGTGCAGAGGTTCCTCCCGATG
GTGGATGCAGTGGCCAGGGACTTCTCCCAGGCCCTGAAGAAGAAGGTGCTGCAGAACGCC
CGGGGGAGCCTGACCCTGGACGTCCAGCCCAGCATCTTCCACTACACCATAGAAGCCAGC
AACTTAGCTCTTTTTGGAGAGCGGCTGGGCCTGGTTGGCCACAGCCCCAGTTCTGCCAGC
CTGAACTTCCTCCATGCCCTGGAGGTCATGTTCAAATCCACCGTCCAGCTCATGTTCATG
CCCAGGAGCCTGTCTCGCTGGATCAGCCCCAAGGTGTGGAAGGAGCACTTTGAGGCCTGG
GACTGCATCTTCCAGTACGGTGACAACTGTATCCAGAAAATCTACCAGGAACTGGCCTTC
AACCGCCCTCAACACTACACAGGCATCGTGGCGGAGCTCCTGTTGAAGGCGGAACTGTCA
CTAGAAGCCATCAAGGCCAACTCTATGGAACTCACTGCAGGGAGCGTGGACACGACAGCG
TTTCCCTTGCTGATGACGCTCTTTGAGCTGGCTCGGAACCCCGACGTGCAGCAGATCCTG
CGCCAGGAGAGCCTGGCCGCCGCAGCCAGCATCAGTGAACATCCCCAGAAGGCAACCACC
GAGCTGCCCTTGCTGCGGGCGGCCCTCAAGGAGACCTTGCGGCTCTACCCTGTGGGTCTG
TTTTTGGAGCGAGTGGTGAGCTCAGACTTGGTGCTTCAGAACTACCACATCCCAGCTGGG
ACATTGGTACAGGTTTTCCTCTACTCGCTGGGTCGCAATGCCGCCTTGTTCCCGAGGCCT
GAGCGGTATAATCCCCAGCGCTGGCTAGACATCAGGGGCTCCGGCAGGAACTTCCACCAC
GTGCCCTTTGGCTTTGGCATGCGCCAGTGCCTCGGGCGGCGCCTGGCAGAGGCAGAGATG
CTGCTGCTGCTGCACCACGTGCTGAAGCACTTCCTGGTGGAGACACTAACTCAAGAGGAC
ATAAAGATGGTCTACAGCTTCATATTGAGGCCTGGCACGTCCCCCCTCCTCACTTTCAGA
GCGATTAACTAG
Enzyme 2 GenBank Gene ID NM_000498.3 Link Image
Enzyme 2 GeneCard ID CYP11B2 Link Image
Enzyme 2 GenAtlas ID CYP11B2 Link Image
Enzyme 2 HGNC ID HGNC:2592 Link Image
Enzyme 2 Chromosome Location 8
Enzyme 2 Locus 8q21-q22
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Mornet E, Dupont J, Vitek A, White PC: Characterization of two genes encoding human steroid 11 beta-hydroxylase (P-450(11) beta). J Biol Chem. 1989 Dec 15;264(35):20961-7. [PubMed Link Image]
  2. Kawainoto T, Mitsuuchi Y, Ohnishi T, Ichikawa Y, Yokoyama Y, Sumimoto H, Toda K, Miyahara K, Kuribayashi I, Nakao K, et al.: Cloning and expression of a cDNA for human cytochrome P-450aldo as related to primary aldosteronism. Biochem Biophys Res Commun. 1990 Nov 30;173(1):309-16. [PubMed Link Image]
  3. Pascoe L, Curnow KM, Slutsker L, Rosler A, White PC: Mutations in the human CYP11B2 (aldosterone synthase) gene causing corticosterone methyloxidase II deficiency. Proc Natl Acad Sci U S A. 1992 Jun 1;89(11):4996-5000. [PubMed Link Image]
  4. Mitsuuchi Y, Kawamoto T, Naiki Y, Miyahara K, Toda K, Kuribayashi I, Orii T, Yasuda K, Miura K, Nakao K, et al.: Congenitally defective aldosterone biosynthesis in humans: the involvement of point mutations of the P-450C18 gene (CYP11B2) in CMO II deficient patients. Biochem Biophys Res Commun. 1992 Jan 31;182(2):974-9. [PubMed Link Image]
  5. Mitsuuchi Y, Kawamoto T, Miyahara K, Ulick S, Morton DH, Naiki Y, Kuribayashi I, Toda K, Hara T, Orii T, et al.: Congenitally defective aldosterone biosynthesis in humans: inactivation of the P-450C18 gene (CYP11B2) due to nucleotide deletion in CMO I deficient patients. Biochem Biophys Res Commun. 1993 Feb 15;190(3):864-9. [PubMed Link Image]
  6. Nomoto S, Massa G, Mitani F, Ishimura Y, Miyahara K, Toda K, Nagano I, Yamashiro T, Ogoshi S, Fukata J, Onishi S, Hashimoto K, Doi Y, Imura H, Shizuta Y: CMO I deficiency caused by a point mutation in exon 8 of the human CYP11B2 gene encoding steroid 18-hydroxylase (P450C18). Biochem Biophys Res Commun. 1997 May 19;234(2):382-5. [PubMed Link Image]
  7. Peter M, Bunger K, Solyom J, Sippell WG: Mutation THR-185 ILE is associated with corticosterone methyl oxidase deficiency type II. Eur J Pediatr. 1998 May;157(5):378-81. [PubMed Link Image]
  8. Portrat-Doyen S, Tourniaire J, Richard O, Mulatero P, Aupetit-Faisant B, Curnow KM, Pascoe L, Morel Y: Isolated aldosterone synthase deficiency caused by simultaneous E198D and V386A mutations in the CYP11B2 gene. J Clin Endocrinol Metab. 1998 Nov;83(11):4156-61. [PubMed Link Image]
  9. Tamaki S, Iwai N, Tsujita Y, Kinoshita M: Genetic polymorphism of CYP11B2 gene and hypertension in Japanese. Hypertension. 1999 Jan;33(1 Pt 2):266-70. [PubMed Link Image]
  10. Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed Link Image]
  11. 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 Link Image]
  12. Kayes-Wandover KM, Schindler RE, Taylor HC, White PC: Type 1 aldosterone synthase deficiency presenting in a middle-aged man. J Clin Endocrinol Metab. 2001 Mar;86(3):1008-12. [PubMed Link Image]
  13. Dunlop FM, Crock PA, Montalto J, Funder JW, Curnow KM: A compound heterozygote case of type II aldosterone synthase deficiency. J Clin Endocrinol Metab. 2003 Jun;88(6):2518-26. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5992
Enzyme 3 Name Corticosteroid 11-beta-dehydrogenase isozyme 1
Enzyme 3 Synonyms
  1. 11-beta-hydroxysteroid dehydrogenase 1
  2. 11-DH
  3. 11-beta-HSD1
Enzyme 3 Gene Name HSD11B1
Enzyme 3 Protein Sequence >Corticosteroid 11-beta-dehydrogenase isozyme 1
MAFMKKYLLPILGLFMAYYYYSANEEFRPEMLQGKKVIVTGASKGIGREMAYHLAKMGAH
VVVTARSKETLQKVVSHCLELGAASAHYIAGTMEDMTFAEQFVAQAGKLMGGLDMLILNH
ITNTSLNLFHDDIHHVRKSMEVNFLSYVVLTVAALPMLKQSNGSIVVVSSLAGKVAYPMV
AAYSASKFALDGFFSSIRKEYSVSRVNVSITLCVLGLIDTETAMKAVSGIVHMQAAPKEE
CALEIIKGGALRQEEVYYDSSLWTTLLIRNPCRKILEFLYSTSYNMDRFINK
Enzyme 3 Number of Residues 292
Enzyme 3 Molecular Weight 32400.7
Enzyme 3 Theoretical pI 8.77
Enzyme 3 GO Classification
Function
  • binding
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 3 General Function Involved in oxidoreductase activity
Enzyme 3 Specific Function Catalyzes reversibly the conversion of cortisol to the inactive metabolite cortisone. Catalyzes reversibly the conversion of 7-ketocholesterol to 7-beta-hydroxycholesterol. In intact cells, the reaction runs only in one direction, from 7- ketocholesterol to 7-beta-hydroxycholesterol
Enzyme 3 Pathways
Enzyme 3 Reactions
  • an 11beta-hydroxysteroid + NADP+ = an 11-oxosteroid + NADPH + H+ [RN:R03203]
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • 8-24
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein Not Available
Enzyme 3 UniProtKB/Swiss-Prot ID P28845 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name DHI1_HUMAN Link Image
Enzyme 3 PDB ID 1XU9 Link Image
Enzyme 3 PDB File Show
Enzyme 3 3D Structure
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >879 bp
ATGGCTTTTATGAAAAAATATCTCCTCCCCATTCTGGGGCTCTTCATGGCCTACTACTAC
TATTCTGCAAACGAGGAATTCAGACCAGAGATGCTCCAAGGAAAGAAAGTGATTGTCACA
GGGGCCAGCAAAGGGATCGGAAGAGAGATGGCTTATCATCTGGCGAAGATGGGAGCCCAT
GTGGTGGTGACAGCGAGGTCAAAAGAAACTCTACAGAAGGTGGTATCCCACTGCCTGGAG
CTTGGAGCAGCCTCAGCACACTACATTGCTGGCACCATGGAAGACATGACCTTCGCAGAG
CAATTTGTTGCCCAAGCAGGAAAGCTCATGGGAGGACTAGACATGCTCATTCTCAACCAC
ATCACCAACACTTCTTTGAATCTTTTTCATGATGATATTCACCATGTGCGCAAAAGCATG
GAAGTCAACTTCCTCAGTTACGTGGTCCTGACTGTAGCTGCCTTGCCCATGCTGAAGCAG
AGCAATGGAAGCATTGTTGTCGTCTCCTCTCTGGCTGGGAAAGTGGCTTATCCAATGGTT
GCTGCCTATTCTGCAAGCAAGTTTGCTTTGGATGGGTTCTTCTCCTCCATCAGAAAGGAA
TATTCAGTGTCCAGGGTCAATGTATCAATCACTCTCTGTGTTCTTGGCCTCATAGACACA
GAAACAGCCATGAAGGCAGTTTCTGGGATAGTCCATATGCAAGCAGCTCCAAAGGAGGAA
TGTGCCCTGGAGATCATCAAAGGGGGAGCTCTGCGCCAAGAAGAAGTGTATTATGACAGC
TCACTCTGGACCACTCTTCTGATCAGAAATCCATGCAGGAAGATCCTGGAATTTCTCTAC
TCAACGAGCTATAATATGGACAGATTCATAAACAAGTAG
Enzyme 3 GenBank Gene ID AK313973 Link Image
Enzyme 3 GeneCard ID HSD11B1 Link Image
Enzyme 3 GenAtlas ID HSD11B1 Link Image
Enzyme 3 HGNC ID HGNC:5208 Link Image
Enzyme 3 Chromosome Location 1
Enzyme 3 Locus 1q32-q41
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Tannin GM, Agarwal AK, Monder C, New MI, White PC: The human gene for 11 beta-hydroxysteroid dehydrogenase. Structure, tissue distribution, and chromosomal localization. J Biol Chem. 1991 Sep 5;266(25):16653-8. [PubMed Link Image]
  2. Draper N, Echwald SM, Lavery GG, Walker EA, Fraser R, Davies E, Sorensen TI, Astrup A, Adamski J, Hewison M, Connell JM, Pedersen O, Stewart PM: Association studies between microsatellite markers within the gene encoding human 11beta-hydroxysteroid dehydrogenase type 1 and body mass index, waist to hip ratio, and glucocorticoid metabolism. J Clin Endocrinol Metab. 2002 Nov;87(11):4984-90. [PubMed Link Image]
  3. 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]
  4. 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]
  5. 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]
  6. Odermatt A, Arnold P, Stauffer A, Frey BM, Frey FJ: The N-terminal anchor sequences of 11beta-hydroxysteroid dehydrogenases determine their orientation in the endoplasmic reticulum membrane. J Biol Chem. 1999 Oct 1;274(40):28762-70. [PubMed Link Image]
  7. Draper N, Walker EA, Bujalska IJ, Tomlinson JW, Chalder SM, Arlt W, Lavery GG, Bedendo O, Ray DW, Laing I, Malunowicz E, White PC, Hewison M, Mason PJ, Connell JM, Shackleton CH, Stewart PM: Mutations in the genes encoding 11beta-hydroxysteroid dehydrogenase type 1 and hexose-6-phosphate dehydrogenase interact to cause cortisone reductase deficiency. Nat Genet. 2003 Aug;34(4):434-9. [PubMed Link Image]
  8. Frick C, Atanasov AG, Arnold P, Ozols J, Odermatt A: Appropriate function of 11beta-hydroxysteroid dehydrogenase type 1 in the endoplasmic reticulum lumen is dependent on its N-terminal region sharing similar topological determinants with 50-kDa esterase. J Biol Chem. 2004 Jul 23;279(30):31131-8. Epub 2004 May 19. [PubMed Link Image]
  9. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed Link Image]
  10. Hosfield DJ, Wu Y, Skene RJ, Hilgers M, Jennings A, Snell GP, Aertgeerts K: Conformational flexibility in crystal structures of human 11beta-hydroxysteroid dehydrogenase type I provide insights into glucocorticoid interconversion and enzyme regulation. J Biol Chem. 2005 Feb 11;280(6):4639-48. Epub 2004 Oct 28. [PubMed Link Image]
  11. Sorensen B, Winn M, Rohde J, Shuai Q, Wang J, Fung S, Monzon K, Chiou W, Stolarik D, Imade H, Pan L, Deng X, Chovan L, Longenecker K, Judge R, Qin W, Brune M, Camp H, Frevert EU, Jacobson P, Link JT: Adamantane sulfone and sulfonamide 11-beta-HSD1 Inhibitors. Bioorg Med Chem Lett. 2007 Jan 15;17(2):527-32. Epub 2006 Oct 7. [PubMed Link Image]
  12. Yuan C, St Jean DJ Jr, Liu Q, Cai L, Li A, Han N, Moniz G, Askew B, Hungate RW, Johansson L, Tedenborg L, Pyring D, Williams M, Hale C, Chen M, Cupples R, Zhang J, Jordan S, Bartberger MD, Sun Y, Emery M, Wang M, Fotsch C: The discovery of 2-anilinothiazolones as 11beta-HSD1 inhibitors. Bioorg Med Chem Lett. 2007 Nov 15;17(22):6056-61. Epub 2007 Sep 25. [PubMed Link Image]
  13. Wang H, Ruan Z, Li JJ, Simpkins LM, Smirk RA, Wu SC, Hutchins RD, Nirschl DS, Van Kirk K, Cooper CB, Sutton JC, Ma Z, Golla R, Seethala R, Salyan ME, Nayeem A, Krystek SR Jr, Sheriff S, Camac DM, Morin PE, Carpenter B, Robl JA, Zahler R, Gordon DA, Hamann LG: Pyridine amides as potent and selective inhibitors of 11beta-hydroxysteroid dehydrogenase type 1. Bioorg Med Chem Lett. 2008 Jun 1;18(11):3168-72. Epub 2008 May 1. [PubMed Link Image]
  14. Hale C, Veniant M, Wang Z, Chen M, McCormick J, Cupples R, Hickman D, Min X, Sudom A, Xu H, Matsumoto G, Fotsch C, St Jean DJ Jr, Wang M: Structural characterization and pharmacodynamic effects of an orally active 11beta-hydroxysteroid dehydrogenase type 1 inhibitor. Chem Biol Drug Des. 2008 Jan;71(1):36-44. Epub 2007 Dec 7. [PubMed Link Image]
  15. Julian LD, Wang Z, Bostick T, Caille S, Choi R, DeGraffenreid M, Di Y, He X, Hungate RW, Jaen JC, Liu J, Monshouwer M, McMinn D, Rew Y, Sudom A, Sun D, Tu H, Ursu S, Walker N, Yan X, Ye Q, Powers JP: Discovery of novel, potent benzamide inhibitors of 11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1) exhibiting oral activity in an enzyme inhibition ex vivo model. J Med Chem. 2008 Jul 10;51(13):3953-60. Epub 2008 Jun 14. [PubMed Link Image]
  16. Rew Y, McMinn DL, Wang Z, He X, Hungate RW, Jaen JC, Sudom A, Sun D, Tu H, Ursu S, Villemure E, Walker NP, Yan X, Ye Q, Powers JP: Discovery and optimization of piperidyl benzamide derivatives as a novel class of 11beta-HSD1 inhibitors. Bioorg Med Chem Lett. 2009 Mar 15;19(6):1797-801. Epub 2009 Jan 23. [PubMed Link Image]
  17. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 15188
Enzyme 4 Name Hydroxysteroid (11-beta) dehydrogenase 2
Enzyme 4 Synonyms Not Available
Enzyme 4 Gene Name HSD11B2
Enzyme 4 Protein Sequence >Hydroxysteroid (11-beta) dehydrogenase 2
MERWPWPSGGAWLLVAARALLQLLRSDLRLGRPLLAALALLAALDWLCQRLLPPPAALAV
LAAAGWIALSRLARPQRLPVATRAVLITGCDSGFGKETAKKLDSMGFTVLATVLELNSPG
AIELRTCCSPRLRLLQMDLTKPGDISRVLEFTKAHTTSTGLWGLVNNAGHNEVVADAELS
PVATFRSCMEVNFFGALELTKGLLPLLRSSRGRIVTVGSPAGDMPYPCLGAYGTSKAAVA
LLMDTFSCELLPWGVKVSIIQPGCFKTESVRNVGQWEKRKQLLLANLPQELLQAYGKDYI
EHLHGQFLHSLRLAMSDLTPVVDAITDALLAARPRRRYYPGQGLGLMYFIHYYLPEGLRR
RFLQAFFISHCLPRALQPGQPGTTPPQDAAQDPNLSPGPSPAVAR
Enzyme 4 Number of Residues 405
Enzyme 4 Molecular Weight 44127
Enzyme 4 Theoretical pI 9.58
Enzyme 4 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolism
  • physiological process
Component
Enzyme 4 General Function Lipid transport and metabolism
Enzyme 4 Specific Function Not Available
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions Not Available
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 152112970 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID A7LB28 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name A7LB28_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1218 bp
ATGGAGCGCTGGCCTTGGCCGTCGGGCGGCGCCTGGCTGCTCGTGGCTGCCCGCGCGCTG
CTGCAGCTGCTGCGCTCAGACCTGCGTCTGGGCCGCCCGCTGCTGGCGGCGCTGGCGCTG
CTGGCCGCGCTCGACTGGCTGTGCCAGCGCCTGCTGCCCCCGCCGGCCGCACTCGCCGTG
CTGGCCGCCGCCGGCTGGATCGCGTTGTCCCGCCTGGCGCGCCCGCAGCGCCTGCCGGTG
GCCACTCGCGCGGTGCTCATCACCGGCTGTGACTCTGGTTTTGGCAAGGAGACGGCCAAG
AAACTGGACTCCATGGGCTTCACGGTGCTGGCCACCGTATTGGAGTTGAACAGCCCCGGT
GCCATCGAGCTGCGTACCTGCTGCTCCCCTCGCCTAAGGCTGCTGCAGATGGACCTGACC
AAACCAGGAGACATTAGCCGCGTGCTAGAGTTCACCAAGGCCCACACCACCAGCACCGGC
CTGTGGGGCCTCGTCAACAACGCAGGCCACAATGAAGTAGTTGCTGATGCGGAGCTGTCT
CCAGTGGCCACTTTCCGTAGCTGCATGGAGGTGAATTTCTTTGGCGCGCTCGAGCTGACC
AAGGGCCTCCTGCCCCTGCTGCGCAGCTCAAGGGGCCGCATCGTGACTGTGGGGAGCCCA
GCGGGGGACATGCCATATCCGTGCTTGGGGGCCTATGGAACCTCCAAAGCGGCCGTGGCG
CTACTCATGGACACATTCAGCTGTGAACTCCTTCCCTGGGGGGTCAAGGTCAGCATCATC
CAGCCTGGCTGCTTCAAGACAGAGTCAGTGAGAAACGTGGGTCAGTGGGAAAAGCGCAAG
CAATTGCTGCTGGCCAACCTGCCTCAAGAGCTGCTGCAGGCCTACGGCAAGGACTACATC
GAGCACTTGCATGGGCAGTTCCTGCACTCGCTACGCCTGGCCATGTCCGACCTCACCCCA
GTTGTAGATGCCATCACAGATGCGCTGCTGGCAGCTCGGCCCCGCCGCCGCTATTACCCC
GGCCAGGGCCTGGGGCTCATGTACTTCATCCACTACTACCTGCCTGAAGGCCTGCGGCGC
CGCTTCCTGCAGGCCTTCTTCATCAGTCACTGTCTGCCTCGAGCACTGCAGCCTGGCCAG
CCTGGCACTACCCCACCACAGGACGCAGCCCAGGACCCAAACCTGAGCCCCGGCCCTTCC
CCAGCAGTGGCTCGGTGA
Enzyme 4 GenBank Gene ID EF694683 Link Image
Enzyme 4 GeneCard ID A7LB28 Link Image
Enzyme 4 GenAtlas ID Not Available
Enzyme 4 HGNC ID Not Available
Enzyme 4 Chromosome Location 16
Enzyme 4 Locus 16q22
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References Not Available
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 16423
Enzyme 5 Name Mitochondrial cytochrome P450, family 11, subfamily B, polypeptide 2 (Cytochrome P450, family 11, subfamily B, polypeptide 2)
Enzyme 5 Synonyms Not Available
Enzyme 5 Gene Name CYP11B2
Enzyme 5 Protein Sequence >Mitochondrial cytochrome P450, family 11, subfamily B, polypeptide 2 (Cytochrome P450, family 11, subfamily B, polypeptide 2)
MALRAKAEVCVAAPWLSLQRARALGTRAARAPRTVLPFEAMPQHPGNRWLRLLQIWREQG
YEHLHLEMHQTFQELGPIFRYNLGGPRMVCVMLPEDVEKLQQVDSLHPCRMILEPWVAYR
QHRGHKCGVFLLNGPEWRFNRLRLNPDVLSPKAVQRFLPMVDAVARDFSQALKKKVLQNA
RGSLTLDVQPSIFHYTIEASNLALFGERLGLVGHSPSSASLNFLHALEVMFKSTVQLMFM
PRSLSRWISPKVWKEHFEAWDCIFQYGDNCIQKIYQELAFNRPQHYTGIVAELLLKAELS
LEAIKANSMELTAGSVDTTAFPLLMTLFELARNPDVQQILRQESLAAAASISEHPQKATT
ELPLLRAALKETLRLYPVGLFLERVVSSDLVLQNYHIPAGTLVQVFLYSLGRNAALFPRP
ERYNPQRWLDIRGSGRNFHHVPFGFGMRQCLGRRLAEAEMLLLLHHVLKHFLVETLTQED
IKMVYSFILRPGTSPLLTFRAIN
Enzyme 5 Number of Residues 503
Enzyme 5 Molecular Weight 57561
Enzyme 5 Theoretical pI 9.78
Enzyme 5 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 5 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 5 Specific Function Not Available
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions Not Available
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein Not Available
Enzyme 5 UniProtKB/Swiss-Prot ID B0ZBE4 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name B0ZBE4_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence Not Available
Enzyme 5 GenBank Gene ID EU326306 Link Image
Enzyme 5 GeneCard ID B0ZBE4 Link Image
Enzyme 5 GenAtlas ID Not Available
Enzyme 5 HGNC ID Not Available
Enzyme 5 Chromosome Location Not Available
Enzyme 5 Locus Not Available
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References Not Available
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 16473
Enzyme 6 Name cDNA, FLJ94621, Homo sapiens hydroxysteroid (11-beta) dehydrogenase 1 (HSD11B1), mRNA (Hydroxysteroid (11-beta) dehydrogenase 1, isoform CRA_a)
Enzyme 6 Synonyms Not Available
Enzyme 6 Gene Name HSD11B1
Enzyme 6 Protein Sequence >cDNA, FLJ94621, Homo sapiens hydroxysteroid (11-beta) dehydrogenase 1 (HSD11B1), mRNA (Hydroxysteroid (11-beta) dehydrogenase 1, isoform CRA_a)
MAFMKKYLLPILGLFMAYYYYSANEEFRPEMLQGKKVIVTGASKGIGREMAYHLAKMGAH
VVVTARSKETLQKVVSHCLELGAASAHYIAGTMEDMTFAEQFVAQAGKLMGGLDMLILNH
ITNTSLNLFHDDIHHVRKSMEVNFLSYVVLTVAALPMLKQSNGSIVVVSSLAGKVAYPMV
AAYSASKFALDGFFSSIRKEYSVSRVNVSITLCVLGLIDTETAMKAVSGIVHMQAAPKEE
CALEIIKGGALRQEEVYYDSSLWTTLLIRNPCRKILEFLYSTSYNMDRFINK
Enzyme 6 Number of Residues 292
Enzyme 6 Molecular Weight 32401
Enzyme 6 Theoretical pI 8.77
Enzyme 6 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolism
  • physiological process
Component
Enzyme 6 General Function Lipid 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
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein Not Available
Enzyme 6 UniProtKB/Swiss-Prot ID B2R9Z1 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name B2R9Z1_HUMAN Link Image
Enzyme 6 PDB ID 1XU9 Link Image
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 AK313973 Link Image
Enzyme 6 GeneCard ID B2R9Z1 Link Image
Enzyme 6 GenAtlas ID Not Available
Enzyme 6 HGNC ID Not Available
Enzyme 6 Chromosome Location Not Available
Enzyme 6 Locus Not Available
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References Not Available
Enzyme 6 Metabolite References Not Available