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Human Metabolome Database Version 2.5

 

Showing metabocard for Dehydroepiandrosterone (HMDB00077)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2010-04-15 15:13:48
Accession Number HMDB00077
Secondary Accession Numbers Not Available
Common Name Dehydroepiandrosterone
Description Dehydroepiandrosterone (DHEA) is a natural steroid hormone produced from cholesterol by the adrenal glands. DHEA is also produced in the gonads, adipose tissue and the brain. DHEA is structurally similar to, and is a precursor of, androstenedione, testosterone, estradiol, estrone and estrogen. It is the most abundant hormone in the human body. Most of DHEA is sulfated (dehydroepiandrosterone sulfate- DEHAS) before secretion. DHEAS is the sulfated version of DHEA; - this conversion is reversibly catalyzed by sulfotransferase (SULT2A1) primarily in the adrenals, the liver, and small intestines. In blood, most DHEA is found as DHEAS with levels that are about 300 times higher than free DHEA. Blood measurements of DHEAS/DHEA are useful to detect excess adrenal activity as seen in adrenal cancer or hyperplasia, including certain forms of congenital adrenal hyperplasia. Women with polycystic ovary syndrome tend to have normal or mildly elevated levels of DHEAS.
Synonyms
  1. (+)-Dehydroisoandrosterone
  2. (3-beta)-3-Hydroxyandrost-5-en-17-one
  3. (3beta)-3-hydroxy-Androst-5-en-17-one
  4. (3beta,16alpha)-3,16-dihydroxy-androst-5-en-17-one
  5. 17-Chetovis
  6. 17-Hormoforin
  7. 3-beta-Hydroxy-5-androsten-17-one
  8. 3-beta-Hydroxyandrost-5-en-17-one
  9. 3b-Hydroxy-D5-androsten-17-one
  10. 3b-Hydroxyandrost-5-en-17-one
  11. 3beta-Hydroxy-D5-androsten-17-one
  12. 3beta-Hydroxyandrost-5-en-17-one
  13. 3beta-hydroxy-5-androsten-17-one
  14. 3beta-hydroxy-Androst-5-en-17-one
  15. 5,6-Dehydroisoandrosterone
  16. 5,6-Didehydroisoandrosterone
  17. 5-Androsten-3-beta-ol-17-one
  18. 5-Androsten-3b-ol-17-one
  19. 5-Androsten-3beta-ol-17-one
  20. 5-Dehydroepiandrosterone
  21. 5-dehydro-Epiandrosterone
  22. Andrestenol
  23. Androst-5-ene-3b-ol-17-one
  24. Androst-5-ene-3beta-ol-17-one
  25. Androsten-3beta-ol-17-one
  26. Androstenolone
  27. Astenile
  28. D5-Androsten-3b-ol-17-one
  29. D5-Androsten-3beta-ol-17-one
  30. Deandros
  31. Dehydro-epi-androsterone
  32. Dehydroepiandrosterone
  33. Dehydroisoandrosterone
  34. Diandron
  35. Diandrone
  36. Hydroxyandrostenone
  37. Prasterona
  38. Prasterone
  39. Prasteronum
  40. Prestara
  41. Psicosterone
  42. trans-Dehydroandrosterone
Chemical IUPAC Name (3S,8R,9S,10R,13S,14S)-3-hydroxy-10,13-dimethyl-1,2,3,4,7,8,9,11,12,14,15,16-dodecahydrocyclopenta[a]phenanthren-17-one
Chemical Formula C19H28O2
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
  • Component of Androgen and estrogen metabolism
Application
—
Source
  • Endogenous
Average Molecular Weight 288.424
Monoisotopic Molecular Weight 288.208923
Isomeric SMILES C[C@]12CCC3C(CC=C4C[C@@H](O)CC[C@]34C)C1CCC2=O
Canonical SMILES CC12CCC3C(CC=C4CC(O)CCC34C)C1CCC2=O
KEGG Compound ID C01227 Link Image
BioCyc ID DEHYDRO-EPIANDROSTERONE-SULFATE Link Image
BiGG ID 37131 Link Image
Wikipedia Link Dehydroepiandrosterone Link Image
NuGOwiki Link HMDB00077 Link Image
Metagene Link HMDB00077 Link Image
METLIN ID 5133 Link Image
PubChem Compound 5881 Link Image
PubChem Substance 8153636 Link Image
ChEBI ID 28689 Link Image
CAS Registry Number 53-43-0
InChI Identifier InChI=1/C19H28O2/c1-18-9-7-13(20)11-12(18)3-4-14-15-5-6-17(21)19(15,2)10-8-16(14)18/h3,13-16,20H,4-11H2,1-2H3/t13-,14?,15?,16?,18-,19-/m0/s1
Synthesis Reference Nguyen Xuan Cuong; Nguyen Van Dan. Synthesis of dehydroepiandrosterone (DHA) from 16-dehydropregnenolone acetate (DPA). Tap Chi Duoc Hoc (1983), (4), 12-14.
Melting Point (Experimental) 140-141 oC
Experimental Water Solubility 0.0635 mg/mL [YALKOWSKY,SH & DANNENFELSER,RM (1992)] Source: PhysProp
Predicted Water Solubility 0.0438 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity 3.23 [HANSCH,C ET AL. (1995)] Source: PhysProp
Predicted LogP/Hydrophobicity 3 [Predicted by PubChem via XLOGP]; 3.53 [Predicted by ALOGPS] 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 Download Spectrum
Download FID (Varian)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Membrane (Predicted from LogP)
  • Cytoplasm
  • endoplasmic reticulum
Biofluid Location
  • Blood
  • Cerebrospinal Fluid
  • Saliva
  • Urine
Tissue Location
Tissue References
Adipose Tissue —
Adrenal Cortex —
Adrenal Gland —
Brain —
Epidermis —
Fibroblasts —
Gonads —
Kidney —
Liver —
Muscle —
Neuron —
Placenta —
Platelet —
Prostate —
Testes —
Concentrations (Normal)
Biofluid Blood
Value 0.001 (0.00034-0.0017) uM
Age Children:1-13 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Shackleton C, Malunowicz E: Apparent pregnene hydroxylation deficiency (APHD): seeking the parentage of an orphan metabolome. Steroids. 2003 Oct;68(9):707-17. [PubMed Link Image]
Biofluid Blood
Value 0.0087 (0.0035-0.013) uM
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Shackleton C, Malunowicz E: Apparent pregnene hydroxylation deficiency (APHD): seeking the parentage of an orphan metabolome. Steroids. 2003 Oct;68(9):707-17. [PubMed Link Image]
Biofluid Blood
Value 0.023 (0.005-0.042) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • The Merck Manual, 17th ed. Mark H. Beers, MD, Robert Berkow, MD, eds. Whitehouse Station, NJ: Merck Research Labs, 1999.
Biofluid Blood
Value 0.020 +/- 0.011 uM
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Yamada Y, Sekihara H, Omura M, Yanase T, Takayanagi R, Mune T, Yasuda K, Ishizuka T, Ueshiba H, Miyachi Y, Iwasaki T, Nakajima A, Nawata H: Changes in serum sex hormone profiles after short-term low-dose administration of dehydroepiandrosterone (DHEA) to young and elderly persons. Endocr J. 2007 Feb;54(1):153-62. Epub 2006 Dec 21. [PubMed Link Image]
Biofluid CSF
Value 0.00101 (0.00002-0.002) uM
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Schwarz S, Pohl P: Steroid hormones and steroid hormone binding globulins in cerebrospinal fluid studied in individuals with intact and with disturbed blood-cerebrospinal fluid barrier. Neuroendocrinology. 1992 Feb;55(2):174-82. [PubMed Link Image]
Biofluid Saliva
Value 0.0033 (0.0024-0.0090) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Finlay EM, Morton MS, Gaskell SJ: Identification and quantification of dehydroepiandrosterone sulphate in saliva. Steroids. 1982 Jan;39(1):63-71. [PubMed Link Image]
Biofluid Urine
Value 0.13 +/- 0.057 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Poor V, Biro I, Bufa A, Gati A, Fenyvesi I, Juricskay S, Tenyi T, Kilar F: Urinary steroids in young women with eating disorders. J Biochem Biophys Methods. 2004 Oct 29;61(1-2):199-205. [PubMed Link Image]
Biofluid Urine
Value 0.0016 +/- 0.00026 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Straub RH, Weidler C, Demmel B, Herrmann M, Kees F, Schmidt M, Scholmerich J, Schedel J: Renal clearance and daily excretion of cortisol and adrenal androgens in patients with rheumatoid arthritis and systemic lupus erythematosus. Ann Rheum Dis. 2004 Aug;63(8):961-8. [PubMed Link Image]
Biofluid Urine
Value 0.10 (0.066-0.17) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Shamim W, Yousufuddin M, Bakhai A, Coats AJ, Honour JW: Gender differences in the urinary excretion rates of cortisol and androgen metabolites. Ann Clin Biochem. 2000 Nov;37 ( Pt 6):770-4. [PubMed Link Image]
Biofluid Urine
Value 0.022 (0.017-0.041) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Shamim W, Yousufuddin M, Bakhai A, Coats AJ, Honour JW: Gender differences in the urinary excretion rates of cortisol and androgen metabolites. Ann Clin Biochem. 2000 Nov;37 ( Pt 6):770-4. [PubMed Link Image]
Concentrations (Abnormal)
Biofluid Urine
Value 0.00032 +/- 0.000065 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Condition Rheumatoid arthritis
Comments Rheumatoid arthritis with prednisolone treatment
References
  • Straub RH, Weidler C, Demmel B, Herrmann M, Kees F, Schmidt M, Scholmerich J, Schedel J: Renal clearance and daily excretion of cortisol and adrenal androgens in patients with rheumatoid arthritis and systemic lupus erythematosus. Ann Rheum Dis. 2004 Aug;63(8):961-8. [PubMed Link Image]
Biofluid Urine
Value 0.00066 +/- 0.00021 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Condition Rheumatoid arthritis
Comments Rheumatoid arthritis without prednisolone treatment
References
  • Straub RH, Weidler C, Demmel B, Herrmann M, Kees F, Schmidt M, Scholmerich J, Schedel J: Renal clearance and daily excretion of cortisol and adrenal androgens in patients with rheumatoid arthritis and systemic lupus erythematosus. Ann Rheum Dis. 2004 Aug;63(8):961-8. [PubMed Link Image]
Biofluid Urine
Value 0.00034 +/- 0.000078 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Comments Systemic lupus erythematosus (SLE) with prednisolone treatment
References
  • Straub RH, Weidler C, Demmel B, Herrmann M, Kees F, Schmidt M, Scholmerich J, Schedel J: Renal clearance and daily excretion of cortisol and adrenal androgens in patients with rheumatoid arthritis and systemic lupus erythematosus. Ann Rheum Dis. 2004 Aug;63(8):961-8. [PubMed Link Image]
Biofluid Urine
Value 0.0011 +/- 0.00026 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Comments Systemic lupus erythematosus (SLE) without prednisolone treatment
References
  • Straub RH, Weidler C, Demmel B, Herrmann M, Kees F, Schmidt M, Scholmerich J, Schedel J: Renal clearance and daily excretion of cortisol and adrenal androgens in patients with rheumatoid arthritis and systemic lupus erythematosus. Ann Rheum Dis. 2004 Aug;63(8):961-8. [PubMed Link Image]
Associated Disorders
Condition References
Rheumatoid arthritis
  • Straub RH, Weidler C, Demmel B, Herrmann M, Kees F, Schmidt M, Scholmerich J, Schedel J: Renal clearance and daily excretion of cortisol and adrenal androgens in patients with rheumatoid arthritis and systemic lupus erythematosus. Ann Rheum Dis. 2004 Aug;63(8):961-8. [PubMed Link Image]
OMIM ID
Pathways
Name SMPDB Link KEGG Link
Androgen and Estrogen Metabolism SMP00068 Link Image map00150 Link Image
General References
  1. Robinzon B, Michael KK, Ripp SL, Winters SJ, Prough RA: Glucocorticoids inhibit interconversion of 7-hydroxy and 7-oxo metabolites of dehydroepiandrosterone: a role for 11beta-hydroxysteroid dehydrogenases? Arch Biochem Biophys. 2003 Apr 15;412(2):251-8. [PubMed Link Image]
  2. Rao MS, Subbarao V, Yeldandi AV, Reddy JK: Hepatocarcinogenicity of dehydroepiandrosterone in the rat. Cancer Res. 1992 May 15;52(10):2977-9. [PubMed Link Image]
  3. Saruc M, Yuceyar H, Ayhan S, Turkel N, Tuzcuoglu I, Can M: The association of dehydroepiandrosterone, obesity, waist-hip ratio and insulin resistance with fatty liver in postmenopausal women--a hyperinsulinemic euglycemic insulin clamp study. Hepatogastroenterology. 2003 May-Jun;50(51):771-4. [PubMed Link Image]
  4. Bamberg E, Aichinger A, Mitteregger G: In vitro metabolism of dehydroepiandrosterone and testosterone by canine hair follicle cells. Vet Dermatol. 2004 Feb;15(1):19-24. [PubMed Link Image]
  5. Gordon GB, Bush TL, Helzlsouer KJ, Miller SR, Comstock GW: Relationship of serum levels of dehydroepiandrosterone and dehydroepiandrosterone sulfate to the risk of developing postmenopausal breast cancer. Cancer Res. 1990 Jul 1;50(13):3859-62. [PubMed Link Image]
  6. Schwarz S, Pohl P: Steroid hormones and steroid hormone binding globulins in cerebrospinal fluid studied in individuals with intact and with disturbed blood-cerebrospinal fluid barrier. Neuroendocrinology. 1992 Feb;55(2):174-82. [PubMed Link Image]
  7. Weill-Engerer S, David JP, Sazdovitch V, Liere P, Schumacher M, Delacourte A, Baulieu EE, Akwa Y: In vitro metabolism of dehydroepiandrosterone (DHEA) to 7alpha-hydroxy-DHEA and Delta5-androstene-3beta,17beta-diol in specific regions of the aging brain from Alzheimer's and non-demented patients. Brain Res. 2003 Apr 18;969(1-2):117-25. [PubMed Link Image]
  8. Finlay EM, Morton MS, Gaskell SJ: Identification and quantification of dehydroepiandrosterone sulphate in saliva. Steroids. 1982 Jan;39(1):63-71. [PubMed Link Image]
  9. Uzieblo-Zyczkowska B, Sidlo E, Stelmaszuk T: [Dehydroepiandrosterone (DHEA)--slows down the aging process?] Pol Merkur Lekarski. 2005 Dec;19(114):831-4. [PubMed Link Image]
  10. Prost O, Nicollier M, Laurent R, Adessi GL: Estrone- and dehydroepiandrosterone-sulfatase activities in human female epidermis. Arch Dermatol Res. 1985;277(3):195-200. [PubMed Link Image]
  11. Friess E, Schiffelholz T, Steckler T, Steiger A: Dehydroepiandrosterone--a neurosteroid. Eur J Clin Invest. 2000 Dec;30 Suppl 3:46-50. [PubMed Link Image]
  12. Hakkinen A, Pakarinen A, Hannonen P, Kautiainen H, Nyman K, Kraemer WJ, Hakkinen K: Effects of prolonged combined strength and endurance training on physical fitness, body composition and serum hormones in women with rheumatoid arthritis and in healthy controls. Clin Exp Rheumatol. 2005 Jul-Aug;23(4):505-12. [PubMed Link Image]
  13. Shackleton C, Malunowicz E: Apparent pregnene hydroxylation deficiency (APHD): seeking the parentage of an orphan metabolome. Steroids. 2003 Oct;68(9):707-17. [PubMed Link Image]
  14. Kim SB, Hill M, Kwak YT, Hampl R, Jo DH, Morfin R: Neurosteroids: Cerebrospinal fluid levels for Alzheimer's disease and vascular dementia diagnostics. J Clin Endocrinol Metab. 2003 Nov;88(11):5199-206. [PubMed Link Image]
  15. Chalbot S, Morfin R: Human liver S9 fractions: metabolism of dehydroepiandrosterone, epiandrosterone, and related 7-hydroxylated derivatives. Drug Metab Dispos. 2005 Apr;33(4):563-9. Epub 2005 Jan 13. [PubMed Link Image]
  16. Miller KK, Cai J, Ripp SL, Pierce WM Jr, Rushmore TH, Prough RA: Stereo- and regioselectivity account for the diversity of dehydroepiandrosterone (DHEA) metabolites produced by liver microsomal cytochromes P450. Drug Metab Dispos. 2004 Mar;32(3):305-13. [PubMed Link Image]
  17. Martina V, Benso A, Gigliardi VR, Masha A, Origlia C, Granata R, Ghigo E: Short-term dehydroepiandrosterone treatment increases platelet cGMP production in elderly male subjects. Clin Endocrinol (Oxf). 2006 Mar;64(3):260-4. [PubMed Link Image]
  18. Wikipedia Link Image
Metabolic Enzymes
  1. Sulfotransferase family cytosolic 2B member 1
  2. Solute carrier organic anion transporter family member 1B3
  3. Solute carrier organic anion transporter family member 1B1
  4. 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type I
  5. Steryl-sulfatase precursor
  6. Cytochrome P450 17A1
  7. cDNA FLJ75712, highly similar to Homo sapiens hydroxy-delta-5-steroid dehydrogenase, 3 beta- and steroid delta-isomerase 1
  8. Solute carrier family 22 member 7
  9. HSD3B2 protein
  10. cDNA FLJ77905, highly similar to Homo sapiens sulfotransferase family, cytosolic, 2A, dehydroepiandrosterone (DHEA)-preferring, member 1 (SULT2A1), mRNA (Sulfotransferase family, cytosolic, 2A, dehydroepiandrosterone (DHEA)-preferring, member 1, isoform C
Enzyme 1 [top]
Enzyme 1 ID 5591
Enzyme 1 Name Sulfotransferase family cytosolic 2B member 1
Enzyme 1 Synonyms
  1. Sulfotransferase 2B1
  2. Alcohol sulfotransferase
  3. Hydroxysteroid sulfotransferase 2
Enzyme 1 Gene Name SULT2B1
Enzyme 1 Protein Sequence >Sulfotransferase family cytosolic 2B member 1 
MDGPAEPQIPGLWDTYEDDISEISQKLPGEYFRYKGVPFPVGLYSLESISLAENTQDVRD
DDIFIITYPKSGTTWMIEIICLILKEGDPSWIRSVPIWERAPWCETIVGAFSLPDQYSPR
LMSSHLPIQIFTKAFFSSKAKVIYMGRNPRDVVVSLYHYSKIAGQLKDPGTPDQFLRDFL
KGEVQFGSWFDHIKGWLRMKGKDNFLFITYEELQQDLQGSVERICGFLGRPLGKEALGSV
VAHSTFSAMKANTMSNYTLLPPSLLDHRRGAFLRKGVCGDWKNHFTVAQSEAFDRAYRKQ
MRGMPTFPWDEDPEEDGSPDPEPSPEPEPKPSLEPNTSLEREPRPNSSPSPSPGQASETP
HPRPS
Enzyme 1 Number of Residues 365
Enzyme 1 Molecular Weight 41308
Enzyme 1 Theoretical pI 5.05
Enzyme 1 GO Classification
Function
  • catalytic activity
  • sulfotransferase activity
  • transferase activity
  • transferase activity, transferring sulfur-containing groups
Process
—
Component
—
Enzyme 1 General Function Not Available
Enzyme 1 Specific Function Catalyzes the sulfate conjugation of many hormones, neurotransmitters, drugs and xenobiotic compounds. Sulfonation increases the water solubility of most compounds, and therefore their renal excretion, but it can also result in bioactivation to form active metabolites. Sulfates hydroxysteroids like DHEA. Isoform 1 preferentially sulfonates cholesterol, and isoform 2 avidly sulfonates pregnenolone but not cholesterol
Enzyme 1 Pathways
Enzyme 1 Reactions
  • 3'-phosphoadenylyl sulfate + an alcohol = adenosine 3',5'-bisphosphate + an alkyl sulfate
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 1923291 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID O00204 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name ST2B1_HUMAN Link Image
Enzyme 1 PDB ID 1Q1Q Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1053 bp 
ATGGCGTCTCCCCCACCTTTCCACAGCCAGAAGTTGCCAGGTGAATACTTCCGGTACAAG
GGCGTCCCCTTCCCCGTCGGCCTGTACTCGCTCGAGAGCATCAGCTTGGCGGAGAACACC
CAAGATGTGCGGGACGACGACATCTTTATCATCACCTACCCCAAGTCAGGCACGACCTGG
ATGATCGAGATCATCTGCTTAATCCTGAAGGAAGGGGATCCATCCTGGATCCGCTCCGTG
CCCATCTGGGAGCGGGCACCCTGGTGTGAGACCATTGTGGGTGCTTTCAGCCTCCCGGAC
CAGTACAGCCCCCGCCTCATGAGCTCCCATCTTCCCATCCAGATCTTCACCAAGGCCTTC
TTCAGCTCCAAGGCCAAGGTGATCTACATGGGCCGCAACCCCCGGGACGTTGTGGTCTCC
CTCTATCATTACTCCAAGATCGCCGGGCAGTTAAAGGACCCGGGCACACCCGACCAGTTC
CTGAGGGACTTCCTCAAAGGCGAAGTGCAGTTTGGCTCCTGGTTCGACCACATTAAGGGC
TGGCTTCGGATGAAGGGCAAAGACAACTTCCTATTTATCACCTACGAGGAGCTGCAGCAG
GACTTACAGGGCTCCGTGGAGCGCATCTGTGGGTTCCTGGGCCGTCCGCTGGGCAAGGAG
GCACTGGGCTCCGTCGTGGCACACTCAACCTTCAGCGCCATGAAGGCCAACACCATGTCC
AACTACACGCTGCTGCCTCCCAGCCTGCTGGACCACCGTCGCGGGGCCTTCCTCCGGAAA
GGGGTCTGCGGCGACTGGAAGAACCACTTCACGGTGGCCCAGAGCGAAGCCTTCGATCGT
GCCTACCGCAAGCAGATGCGGGGGATGCCGACCTTCCCCTGGGATGAAGACCCGGAGGAG
GATGGCAGCCCAGATCCTGAGCCCAGCCCTGAGCCTGAGCCCAAGCCCAGCCTTGAGCCC
AACACCAGCCTGGAGCGTGAGCCCAGACCCAACTCCAGCCCCAACCCCAGCCCCGGCCAG
GCCTCTGAGACCCCGCACCCACGACCCTCATAA
Enzyme 1 GenBank Gene ID U92314 Link Image
Enzyme 1 GeneCard ID SULT2B1 Link Image
Enzyme 1 GenAtlas ID SULT2B1 Link Image
Enzyme 1 HGNC ID HGNC:11459 Link Image
Enzyme 1 Chromosome Location 19
Enzyme 1 Locus 19q13.3
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Her C, Wood TC, Eichler EE, Mohrenweiser HW, Ramagli LS, Siciliano MJ, Weinshilboum RM: Human hydroxysteroid sulfotransferase SULT2B1: two enzymes encoded by a single chromosome 19 gene. Genomics. 1998 Nov 1;53(3):284-95. [PubMed Link Image]
  2. Fuda H, Lee YC, Shimizu C, Javitt NB, Strott CA: Mutational analysis of human hydroxysteroid sulfotransferase SULT2B1 isoforms reveals that exon 1B of the SULT2B1 gene produces cholesterol sulfotransferase, whereas exon 1A yields pregnenolone sulfotransferase. J Biol Chem. 2002 Sep 27;277(39):36161-6. Epub 2002 Jul 26. [PubMed Link Image]
  3. Lee KA, Fuda H, Lee YC, Negishi M, Strott CA, Pedersen LC: Crystal structure of human cholesterol sulfotransferase (SULT2B1b) in the presence of pregnenolone and 3'-phosphoadenosine 5'-phosphate. Rationale for specificity differences between prototypical SULT2A1 and the SULT2BG1 isoforms. J Biol Chem. 2003 Nov 7;278(45):44593-9. Epub 2003 Aug 14. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5684
Enzyme 2 Name Solute carrier organic anion transporter family member 1B3
Enzyme 2 Synonyms
  1. Solute carrier family 21 member 8
  2. Organic anion transporter 8
  3. Organic anion-transporting polypeptide 8
  4. OATP8
  5. Liver-specific organic anion transporter 2
  6. LST-2
Enzyme 2 Gene Name SLCO1B3
Enzyme 2 Protein Sequence >Solute carrier organic anion transporter family member 1B3 
MDQHQHLNKTAESASSEKKKTRRCNGFKMFLAALSFSYIAKALGGIIMKISITQIERRFD
ISSSLAGLIDGSFEIGNLLVIVFVSYFGSKLHRPKLIGIGCLLMGTGSILTSLPHFFMGY
YRYSKETHINPSENSTSSLSTCLINQTLSFNGTSPEIVEKDCVKESGSHMWIYVFMGNML
RGIGETPIVPLGISYIDDFAKEGHSSLYLGSLNAIGMIGPVIGFALGSLFAKMYVDIGYV
DLSTIRITPKDSRWVGAWWLGFLVSGLFSIISSIPFFFLPKNPNKPQKERKISLSLHVLK
TNDDRNQTANLTNQGKNVTKNVTGFFQSLKSILTNPLYVIFLLLTLLQVSSFIGSFTYVF
KYMEQQYGQSASHANFLLGIITIPTVATGMFLGGFIIKKFKLSLVGIAKFSFLTSMISFL
FQLLYFPLICESKSVAGLTLTYDGNNSVASHVDVPLSYCNSECNCDESQWEPVCGNNGIT
YLSPCLAGCKSSSGIKKHTVFYNCSCVEVTGLQNRNYSAHLGECPRDNTCTRKFFIYVAI
QVINSLFSATGGTTFILLTVKIVQPELKALAMGFQSMVIRTLGGILAPIYFGALIDKTCM
KWSTNSCGAQGACRIYNSVFFGRVYLGLSIALRFPALVLYIVFIFAMKKKFQGKDTKASD
NERKVMDEANLEFLNNGEHFVPSAGTDSKTCNLDMQDNAAAN
Enzyme 2 Number of Residues 702
Enzyme 2 Molecular Weight 77404
Enzyme 2 Theoretical pI 8.95
Enzyme 2 GO Classification
Function
  • transporter activity
Process
  • cellular physiological process
  • physiological process
  • transport
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 2 General Function Not Available
Enzyme 2 Specific Function Mediates the Na(+)-independent transport of organic anions such as 17-beta-glucuronosyl estradiol, taurocholate, triiodothyronine (T3), leukotriene C4, dehydroepiandrosterone sulfate (DHEAS), methotrexate and sulfobromophthalein (BSP)
Enzyme 2 Pathways Not Available
Enzyme 2 Reactions Not Available
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • 30-50 65-85 97-117 171-191 207-227 259-279 336-356 377-397 410-430 538-558 575-595 626-646
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 9188300 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q9NPD5 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name SO1B3_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >84 bp 
ATGGACCAACATCAACATTTGAATAAAACAGCAGAGTCAGCATCTTCAGAGAAAAAGAAA
ACAAGACGCTGCAATGGATTCAAG
Enzyme 2 GenBank Gene ID AJ400763 Link Image
Enzyme 2 GeneCard ID SLCO1B3 Link Image
Enzyme 2 GenAtlas ID SLCO1B3 Link Image
Enzyme 2 HGNC ID HGNC:10961 Link Image
Enzyme 2 Chromosome Location 12
Enzyme 2 Locus 12p12
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Konig J, Cui Y, Nies AT, Keppler D: Localization and genomic organization of a new hepatocellular organic anion transporting polypeptide. J Biol Chem. 2000 Jul 28;275(30):23161-8. [PubMed Link Image]
  2. Abe T, Unno M, Onogawa T, Tokui T, Kondo TN, Nakagomi R, Adachi H, Fujiwara K, Okabe M, Suzuki T, Nunoki K, Sato E, Kakyo M, Nishio T, Sugita J, Asano N, Tanemoto M, Seki M, Date F, Ono K, Kondo Y, Shiiba K, Suzuki M, Ohtani H, Shimosegawa T, Iinuma K, Nagura H, Ito S, Matsuno S: LST-2, a human liver-specific organic anion transporter, determines methotrexate sensitivity in gastrointestinal cancers. Gastroenterology. 2001 Jun;120(7):1689-99. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5692
Enzyme 3 Name Solute carrier organic anion transporter family member 1B1
Enzyme 3 Synonyms
  1. Solute carrier family 21 member 6
  2. Sodium-independent organic anion- transporting polypeptide 2
  3. OATP 2
  4. Liver-specific organic anion transporter 1
  5. LST-1
  6. OATP-C
Enzyme 3 Gene Name SLCO1B1
Enzyme 3 Protein Sequence >Solute carrier organic anion transporter family member 1B1 
MDQNQHLNKTAEAQPSENKKTRYCNGLKMFLAALSLSFIAKTLGAIIMKSSIIHIERRFE
ISSSLVGFIDGSFEIGNLLVIVFVSYFGSKLHRPKLIGIGCFIMGIGGVLTALPHFFMGY
YRYSKETNINSSENSTSTLSTCLINQILSLNRASPEIVGKGCLKESGSYMWIYVFMGNML
RGIGETPIVPLGLSYIDDFAKEGHSSLYLGILNAIAMIGPIIGFTLGSLFSKMYVDIGYV
DLSTIRITPTDSRWVGAWWLNFLVSGLFSIISSIPFFFLPQTPNKPQKERKASLSLHVLE
TNDEKDQTANLTNQGKNITKNVTGFFQSFKSILTNPLYVMFVLLTLLQVSSYIGAFTYVF
KYVEQQYGQPSSKANILLGVITIPIFASGMFLGGYIIKKFKLNTVGIAKFSCFTAVMSLS
FYLLYFFILCENKSVAGLTMTYDGNNPVTSHRDVPLSYCNSDCNCDESQWEPVCGNNGIT
YISPCLAGCKSSSGNKKPIVFYNCSCLEVTGLQNRNYSAHLGECPRDDACTRKFYFFVAI
QVLNLFFSALGGTSHVMLIVKIVQPELKSLALGFHSMVIRALGGILAPIYFGALIDTTCI
KWSTNNCGTRGSCRTYNSTSFSRVYLGLSSMLRVSSLVLYIILIYAMKKKYQEKDINASE
NGSVMDEANLESLNKNKHFVPSAGADSETHC
Enzyme 3 Number of Residues 691
Enzyme 3 Molecular Weight 76450
Enzyme 3 Theoretical pI 8.68
Enzyme 3 GO Classification
Function
  • transporter activity
Process
  • cellular physiological process
  • physiological process
  • transport
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 3 General Function Carbohydrate transport and metabolism
Enzyme 3 Specific Function Mediates the Na(+)-independent transport of organic anions such as pravastatin, taurocholate, methotrexate, dehydroepiandrosterone sulfate, 17-beta-glucuronosyl estradiol, estrone sulfate, prostaglandin E2, thromboxane B2, leukotriene C3, leukotriene E4, thyroxine and triiodothyronine. May play an important role in the clearance of bile acids and organic anions from the liver
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions Not Available
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • 97-117 207-227 259-279 336-356 376-396 410-430 575-595
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 5051630 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q9Y6L6 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name SO1B1_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >2076 bp 
ATGGACCAAAATCAACATTTGAATAAAACAGCAGAGGCACAACCTTCAGAGAATAAGAAA
ACAAGATACTGCAATGGATTGAAGATGTTCTTGGCAGCTCTGTCACTCAGCTTTATTGCT
AAGACACTAGGTGCAATTATTATGAAAAGTTCCATCATTCATATAGAACGGAGATTTGAG
ATATCCTCTTCTCTTGTTGGTTTTATTGACGGAAGCTTTGAAATTGGAAATTTGCTTGTG
ATTGTATTTGTGAGTTACTTTGGATCCAAACTACATAGACCAAAGTTAATTGGAATCGGT
TGTTTCATTATGGGAATTGGAGGTGTTTTGACTGCTTTGCCACATTTCTTCATGGGATAT
TACAGGTATTCTAAAGAAACTAATATCAATTCATCAGAAAATTCAACATCGACCTTATCC
ACTTGTTTAATTAATCAAATTTTATCACTCAATAAAGCATCACCTGAGATAGTGGGAAAA
GGTTGTTTAAAGGAATCTGGGTCATACATGTGGATATATGTGTTCATGGGTAATATGCTT
CGTGGAATAGGGGAGACTCCCATAGTACCACTGGGGCTTTCTTACATTGATGATTTCGCT
AAAGAAGGACATTCTTCTTTGTATTTAGGTATATTGAATGCAATAGCAATGATTGGTCCA
ATCATTGGCTTTACCCTGGGATCTCTGTTTTCTAAAATGTACGTGGATATTGGATATGTT
AATCTAAGCACTATCAGGATAACTCCTACTGATTCTCGATGGGTTGGAGCTTGGTGGCTT
AATTTCCTTGTGTCTGGACTATTCTCCATTATTTCTTCCATACCATTCTTTTTCTTGCCC
CAAACTCCAAATAAACCACAAAAAGAAAGAAAAGCTTCACTGTCTTTGCATGTGCTGGAA
ACAAATGATGAAAAGGATCAAACAGCTAATTTGACCAATCAAGGAAAAAATATTACCAAA
AATGTGACTGGTTTTTTCCAGTCTTTTAAAAGCATCCTTACTAATCCCCTGTATGTTATG
TTTGTGCTTTTGACGTTGTTACAAGTAAGCAGCTATATTGGTGCTTTTACTTATGTCTTC
AAATACGTAGAGCAACAGTATGGTCAGCCTTCATCTAAGGCTAACATCTTATTGGGAGTC
ATAACCATACCTATTTTTGCAAGTGGAATGTTTTTAGGAGGATATATCATTAAAAAATTC
AAACTGAACACCGTTGGAATTGCCAAATTCTCATGTTTTACTGCTGTGATGTCATTGTCC
TTTTACCTATTATATTTTTTCATACTCTGTGAAAACAAATCAGTTGCCGGACTAACCATG
ACCTATGATGGAAATAATCCAGTGACATCTCATAGAGATGTACCACTTTCTTATTGCAAC
TCAGACTGCAATTGTGATGAAAGTCAATGGGAACCAGTCTGTGGAAACAATGGAATAACT
TACATCTCACCCTGTCTAGCAGGTTGCAAATCTTCAAGTGGCAATAAAAAGCCTATAGTG
TTTTACAACTGCAGTTGTTTGGAAGTAACTGGTCTCCAGAACAGAAATTACTCAGCCCAT
TTGGGTGAATGCCCAAGAGATGATGCTTGTACAAGGAAATTTTACTTTTTTGTTGCAATA
CAAGTCTTGAATTTATTTTTCTCTGCACTTGGAGGCACCTCACATGTCATGCTGATTGTT
AAAATTGTTCAACCTGAATTGAAATCACTTGCACTGGGTTTCCACTCAATGGTTATACGA
GCACTAGGAGGAATTCTAGCTCCTATATATTTTGGGGCTCTGATTGATACAACGTGTATA
AAGTGGTCCACCAACAACTGTGGCACACGTGGGTCATGTAGGACATATAATTCCACATCA
TTTTCAAGGGTCTACTTGGGCTTGTCTTCAATGTTAAGAGTCTCATCACTTGTTTTATAT
ATTATATTAATTTATGCCATGAAGAAAAAATATCAAGAGAAAGATATCAATGCATCAGAA
AATGGAAGTGTCATGGATGAAGCAAACTTAGAATCCTTAAATAAAAATAAACATTTTGTC
CCTTCTGCTGGGGCAGATAGTGAAACACATTGTTAA
Enzyme 3 GenBank Gene ID AF060500 Link Image
Enzyme 3 GeneCard ID SLCO1B1 Link Image
Enzyme 3 GenAtlas ID SLCO1B1 Link Image
Enzyme 3 HGNC ID HGNC:10959 Link Image
Enzyme 3 Chromosome Location 12
Enzyme 3 Locus 12p
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Abe T, Kakyo M, Tokui T, Nakagomi R, Nishio T, Nakai D, Nomura H, Unno M, Suzuki M, Naitoh T, Matsuno S, Yawo H: Identification of a novel gene family encoding human liver-specific organic anion transporter LST-1. J Biol Chem. 1999 Jun 11;274(24):17159-63. [PubMed Link Image]
  2. Hsiang B, Zhu Y, Wang Z, Wu Y, Sasseville V, Yang WP, Kirchgessner TG: A novel human hepatic organic anion transporting polypeptide (OATP2). Identification of a liver-specific human organic anion transporting polypeptide and identification of rat and human hydroxymethylglutaryl-CoA reductase inhibitor transporters. J Biol Chem. 1999 Dec 24;274(52):37161-8. [PubMed Link Image]
  3. Konig J, Cui Y, Nies AT, Keppler D: A novel human organic anion transporting polypeptide localized to the basolateral hepatocyte membrane. Am J Physiol Gastrointest Liver Physiol. 2000 Jan;278(1):G156-64. [PubMed Link Image]
  4. Konig J, Cui Y, Nies AT, Keppler D: Localization and genomic organization of a new hepatocellular organic anion transporting polypeptide. J Biol Chem. 2000 Jul 28;275(30):23161-8. [PubMed Link Image]
  5. Tirona RG, Leake BF, Merino G, Kim RB: Polymorphisms in OATP-C: identification of multiple allelic variants associated with altered transport activity among European- and African-Americans. J Biol Chem. 2001 Sep 21;276(38):35669-75. Epub 2001 Jul 26. [PubMed Link Image]
  6. Michalski C, Cui Y, Nies AT, Nuessler AK, Neuhaus P, Zanger UM, Klein K, Eichelbaum M, Keppler D, Konig J: A naturally occurring mutation in the SLC21A6 gene causing impaired membrane localization of the hepatocyte uptake transporter. J Biol Chem. 2002 Nov 8;277(45):43058-63. Epub 2002 Aug 23. [PubMed Link Image]
  7. Nozawa T, Nakajima M, Tamai I, Noda K, Nezu J, Sai Y, Tsuji A, Yokoi T: Genetic polymorphisms of human organic anion transporters OATP-C (SLC21A6) and OATP-B (SLC21A9): allele frequencies in the Japanese population and functional analysis. J Pharmacol Exp Ther. 2002 Aug;302(2):804-13. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5738
Enzyme 4 Name 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type I
Enzyme 4 Synonyms
  1. 3- beta-HSD I
  2. Trophoblast antigen FDO161G[Includes: 3-beta-hydroxy- Delta(5-steroid dehydrogenase
  3. 3-beta-hydroxy-5-ene steroid dehydrogenase
  4. Progesterone reductase
  5. Steroid Delta- isomerase
  6. Delta-5-3-ketosteroid isomerase]
Enzyme 4 Gene Name HSD3B1
Enzyme 4 Protein Sequence >4-isomerase type I 
MTGWSCLVTGAGGFLGQRIIRLLVKEKELKEIRVLDKAFGPELREEFSKLQNKTKLTVLE
GDILDEPFLKRACQDVSVIIHTACIIDVFGVTHRESIMNVNVKGTQLLLEACVQASVPVF
IYTSSIEVAGPNSYKEIIQNGHEEEPLENTWPAPYPHSKKLAEKAVLAANGWNLKNGGTL
YTCALRPMYIYGEGSRFLSASINEALNNNGILSSVGKFSTVNPVYVGNVAWAHILALRAL
QDPKKAPSIRGQFYYISDDTPHQSYDNLNYTLSKEFGLRLDSRWSFPLSLMYWIGFLLEI
VSFLLRPIYTYRPPFNRHIVTLSNSVFTFSYKKAQRDLAYKPLYSWEEAKQKTVEWVGSL
VDRHKETLKSKTQ
Enzyme 4 Number of Residues 373
Enzyme 4 Molecular Weight 42252
Enzyme 4 Theoretical pI 8.98
Enzyme 4 GO Classification
Function
  • 3-beta-hydroxy-delta5-steroid dehydrogenase activity
  • catalytic activity
  • intramolecular oxidoreductase activity
  • intramolecular oxidoreductase activity, transposing C=C bonds
  • isomerase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
  • steroid dehydrogenase activity
  • steroid delta-isomerase activity
Process
  • cellular lipid metabolism
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
  • steroid biosynthesis
  • steroid metabolism
Component
—
Enzyme 4 General Function Cell wall/membrane/envelope biogenesis
Enzyme 4 Specific Function 3-beta-HSD is a bifunctional enzyme, that catalyzes the oxidative conversion of Delta(5)-ene-3-beta-hydroxy steroid, and the oxidative conversion of ketosteroids. The 3-beta-HSD enzymatic system plays a crucial role in the biosynthesis of all classes of hormonal steroids
Enzyme 4 Pathways
Enzyme 4 Reactions
  • A 3-oxo-delta5-steroid = a 3-oxo-delta4-steroid
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • 1-13
Enzyme 4 Transmembrane Regions
  • 288-308
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 306889 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID P14060 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name 3BHS1_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1122 bp 
ATGACGGGCTGGAGCTGCCTTGTGACAGGAGCAGGAGGGTTTCTGGGACAGAGGATCATC
CGCCTCTTGGTGAAGGAGAAGGAGCTGAAGGAGATCAGGGTCTTGGACAAGGCCTTCGGA
CCAGAATTGAGAGAGGAATTTTCTAAACTCCAGAACAAGACCAAGCTGACAGTGCTGGAA
GGAGACATTCTGGATGAGCCATTCCTGAAGAGAGCCTGCCAGGACGTCTCGGTCATCATC
CACACCGCCTGTATCATTGATGTCTTCGGTGTCACTCACAGAGAGTCTATCATGAATGTC
AATGTGAAAGGTACCCAGCTCCTGTTAGAGGCCTGTGTCCAAGCTAGTGTGCCAGTCTTC
ATCTACACCAGTAGCATAGAGGTAGCCGGGCCCAACTCCTACAAGGAAATCATCCAGAAT
GGCCATGAAGAAGAGCCTCTGGAAAACACATGGCCCGCTCCATACCCACACAGCAAAAAG
CTTGCTGAGAAGGCTGTACTGGCGGCTAACGGGTGGAATCTGAAAAACGGCGGCACCCTG
TACACTTGTGCCTTACGACCCATGTATATCTATGGGGAAGGAAGCCGATTCCTTTCTGCT
AGTATAAACGAGGCCCTGAACAACAATGGGATCCTGTCAAGTGTTGGAAAGTTCTCCACT
GTTAACCCAGTCTATGTTGGCAATGTGGCCTGGGCCCACATTCTGGCCTTGAGGGCCCTG
CAGGACCCCAAGAAGGCCCCAAGCATCCGAGGACAGTTCTACTATATCTCAGATGACACG
CCTCACCAAAGCTATGATAACCTTAATTACACCCTGAGCAAAGAGTTCGGCCTCCGCCTT
GATTCCAGATGGAGCTTTCCTTTATCCCTGATGTATTGGATTGGCTTCCTGCTGGAAATA
GTGAGCTTCCTACTCAGGCCAATTTACACCTATCGACCGCCCTTCAACCGCCACATAGTC
ACATTGTCAAATAGCGTATTCACCTTCTCTTATAAGAAGGCTCAGCGAGATCTGGCGTAT
AAGCCACTCTACAGCTGGGAGGAAGCCAAGCAGAAAACGGTGGAGTGGGTTGGTTCCCTT
GTGGACCGGCACAAGGAGACCCTGAAGTCCAAGACTCAGTGA
Enzyme 4 GenBank Gene ID M27137 Link Image
Enzyme 4 GeneCard ID HSD3B1 Link Image
Enzyme 4 GenAtlas ID HSD3B1 Link Image
Enzyme 4 HGNC ID HGNC:5217 Link Image
Enzyme 4 Chromosome Location Not Available
Enzyme 4 Locus Not Available
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Luu The V, Lachance Y, Labrie C, Leblanc G, Thomas JL, Strickler RC, Labrie F: Full length cDNA structure and deduced amino acid sequence of human 3 beta-hydroxy-5-ene steroid dehydrogenase. Mol Endocrinol. 1989 Aug;3(8):1310-2. [PubMed Link Image]
  2. Lorence MC, Murry BA, Trant JM, Mason JI: Human 3 beta-hydroxysteroid dehydrogenase/delta 5----4isomerase from placenta: expression in nonsteroidogenic cells of a protein that catalyzes the dehydrogenation/isomerization of C21 and C19 steroids. Endocrinology. 1990 May;126(5):2493-8. [PubMed Link Image]
  3. Lorence MC, Corbin CJ, Kamimura N, Mahendroo MS, Mason JI: Structural analysis of the gene encoding human 3 beta-hydroxysteroid dehydrogenase/delta 5----4-isomerase. Mol Endocrinol. 1990 Dec;4(12):1850-5. [PubMed Link Image]
  4. Lachance Y, Luu-The V, Labrie C, Simard J, Dumont M, de Launoit Y, Guerin S, Leblanc G, Labrie F: Characterization of human 3 beta-hydroxysteroid dehydrogenase/delta 5-delta 4-isomerase gene and its expression in mammalian cells. J Biol Chem. 1990 Nov 25;265(33):20469-75. [PubMed Link Image]
  5. Nickson DA, McBride MW, Zeinali S, Hawes CS, Petropoulos A, Mueller UW, Sutcliffe RG: Molecular cloning and expression of human trophoblast antigen FDO161G and its identification as 3 beta-hydroxy-5-ene steroid dehydrogenase. J Reprod Fertil. 1991 Sep;93(1):149-56. [PubMed Link Image]
  6. Dumont M, Luu-The V, Dupont E, Pelletier G, Labrie F: Characterization, expression, and immunohistochemical localization of 3 beta-hydroxysteroid dehydrogenase/delta 5-delta 4 isomerase in human skin. J Invest Dermatol. 1992 Oct;99(4):415-21. [PubMed Link Image]
  7. 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]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5740
Enzyme 5 Name Steryl-sulfatase precursor
Enzyme 5 Synonyms
  1. Steroid sulfatase
  2. Steryl- sulfate sulfohydrolase
  3. Arylsulfatase C
  4. ASC
Enzyme 5 Gene Name STS
Enzyme 5 Protein Sequence >Steryl-sulfatase precursor 
MPLRKMKIPFLLLFFLWEAESHAASRPNIILVMADDLGIGDPGCYGNKTIRTPNIDRLAS
GGVKLTQHLAASPLCTPSRAAFMTGRYPVRSGMASWSRTGVFLFTASSGGLPTDEITFAK
LLKDQGYSTALIGKWHLGMSCHSKTDFCHHPLHHGFNYFYGISLTNLRDCKPGEGSVFTT
GFKRLVFLPLQIVGVTLLTLAALNCLGLLHVPLGVFFSLLFLAALILTLFLGFLHYFRPL
NCFMMRNYEIIQQPMSYDNLTQRLTVEAAQFIQRNTETPFLLVLSYLHVHTALFSSKDFA
GKSQHGVYGDAVEEMDWSVGQILNLLDELRLANDTLIYFTSDQGAHVEEVSSKGEIHGGS
NGIYKGGKANNWEGGIRVPGILRWPRVIQAGQKIDEPTSNMDIFPTVAKLAGAPLPEDRI
IDGRDLMPLLEGKSQRSDHEFLFHYCNAYLNAVRWHPQNSTSIWKAFFFTPNFNPVGSNG
CFATHVCFCFGSYVTHHDPPLLFDISKDPRERNPLTPASEPRFYEILKVMQEAADRHTQT
LPEVPDQFSWNNFLWKPWLQLCCPSTGLSCQCDREKQDKRLSR
Enzyme 5 Number of Residues 583
Enzyme 5 Molecular Weight 65493
Enzyme 5 Theoretical pI 7.71
Enzyme 5 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • sulfuric ester hydrolase activity
Process
  • metabolism
  • physiological process
Component
—
Enzyme 5 General Function Inorganic ion transport and metabolism
Enzyme 5 Specific Function Conversion of sulfated steroid precursors to estrogens during pregnancy
Enzyme 5 Pathways
  • Androgen and Estrogen Metabolism (map00150 Link Image)
Enzyme 5 Reactions
  • 3beta-hydroxyandrost-5-en-17-one 3-sulfate + H2O = 3beta-hydroxyandrost-5-en-17-one + sulfate
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • 1-21
Enzyme 5 Transmembrane Regions
  • 185-208 213-234
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 338565 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P08842 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name STS_HUMAN Link Image
Enzyme 5 PDB ID 1P49 Link Image
Enzyme 5 PDB File Show
Enzyme 5 3D Structure
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1752 bp 
ATGCCTTTAAGGAAGATGAAGATCCCTTTCCTCCTACTGTTCTTTCTGTGGGAAGCCGAG
AGCCACGCAGCATCAAGGCCGAACATCATCCTGGTGATGGCTGACGACCTCGGCATTGGA
GATCCTGGGTGCTATGGGAACAAAACTATCAGGACTCCCAATATCGACCGGTTGGCCAGT
GGGGGAGTGAAACTCACTCAGCACCTGGCAGCATCACCGCTGTGCACACCAAGCAGGGCA
GCCTTCATGACTGGCCGGTACCCTGTCCGATCAGGAATGGCATCTTGGTCCCGCACTGGA
GTTTTCCTCTTCACAGCCTCTTCGGGAGGACTTCCCACCGATGAGATTACCTTTGCTAAG
CTTCTGAAGGATCAAGGTTATTCAACAGCACTGATAGGGAAATGGCACCTTGGGATGAGC
TGTCACAGCAAGACTGACTTCTGTCACCACCCTTTACATCACGGCTTCAATTATTTCTAT
GGGATCTCTTTGACCAATCTGAGAGACTGCAAGCCCGGAGAGGGCAGTGTCTTCACCACG
GGCTTCAAGAGGCTGGTCTTCCTCCCCCTGCAGATCGTCGGGGTCACCCTCCTTACCCTT
GCTGCACTCAATTGTCTGGGGCTACTCCACGTGCCTCTAGGCGTTTTTTTCAGCCTTCTC
TTCCTAGCAGCCCTAATCCTGACCCTTTTCTTGGGCTTCCTTCATTACTTCCGGCCCCTG
AACTGCTTCATGATGAGGAACTACGAGATCATTCAGCAGCCCATGTCCTATGACAATCTC
ACCCAGAGGCTAACGGTGGAGGCGGCCCAGTTCATACAGCGGAACACTGAGACTCCGTTC
CTGCTTGTCTTGTCCTACCTCCACGTGCACACAGCCCTGTTCTCCAGCAAAGACTTTGCT
GGCAAAAGTCAACACGGAGTCTACGGGGATGCTGTTGAGGAAATGGACTGGAGTGTGGGG
CAGATCTTGAACCTTCTGGATGAGCTGAGATTGGCTAATGATACCCTCATCTACTTCACA
TCGGACCAGGGAGCACATGTAGAGGAGGTGTCTTCCAAAGGAGAAATTCATGGCGGAAGT
AATGGGATCTATAAAGGAGGAAAAGCAAACAACTGGGAAGGAGGTATCCGGGTTCCAGGC
ATCCTTCGTTGGCCCAGGGTGATACAGGCTGGCCAGAAGATTGATGAGCCCACTAGCAAC
ATGGACATATTTCCTACAGTAGCCAAGCTGGCTGGAGCTCCCTTGCCTGAGGACAGGATC
ATTGATGGACGTGATCTGATGCCCCTGCTTGAAGGAAAAAGCCAACGCTCCGATCATGAG
TTTCTCTTCCATTACTGCAACGCCTACTTAAATGCTGTGCGCTGGCACCCTCAGAACAGC
ACATCCATCTGGAAGGCCTTTTTCTTCACCCCCAACTTCAACCCCGTGGGTTCCAACGGA
TGCTTTGCCACACACGTGTGCTTCTGTTTCGGGAGTTATGTCACCCATCACGACCCACCT
TTACTCTTTGATATTTCCAAAGATCCCAGAGAGAGAAACCCACTAACTCCAGCATCCGAG
CCCCGGTTTTATGAAATCCTCAAAGTCATGCAGGAAGCTGCGGACAGACACACCCAGACC
CTGCCAGAGGTGCCCGATCAGTTTTCATGGAACAACTTTCTTTGGAAGCCCTGGCTTCAG
CTGTGCTGTCCTTCCACCGGCCTGTCTTGCCAGTGTGATAGAGAAAAACAGGATAAGAGA
CTGAGCCGCTAG
Enzyme 5 GenBank Gene ID J04964 Link Image
Enzyme 5 GeneCard ID STS Link Image
Enzyme 5 GenAtlas ID STS Link Image
Enzyme 5 HGNC ID HGNC:11425 Link Image
Enzyme 5 Chromosome Location Not Available
Enzyme 5 Locus Not Available
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Stein C, Hille A, Seidel J, Rijnbout S, Waheed A, Schmidt B, Geuze H, von Figura K: Cloning and expression of human steroid-sulfatase. Membrane topology, glycosylation, and subcellular distribution in BHK-21 cells. J Biol Chem. 1989 Aug 15;264(23):13865-72. [PubMed Link Image]
  2. Yen PH, Allen E, Marsh B, Mohandas T, Wang N, Taggart RT, Shapiro LJ: Cloning and expression of steroid sulfatase cDNA and the frequent occurrence of deletions in STS deficiency: implications for X-Y interchange. Cell. 1987 May 22;49(4):443-54. [PubMed Link Image]
  3. Yen PH, Marsh B, Allen E, Tsai SP, Ellison J, Connolly L, Neiswanger K, Shapiro LJ: The human X-linked steroid sulfatase gene and a Y-encoded pseudogene: evidence for an inversion of the Y chromosome during primate evolution. Cell. 1988 Dec 23;55(6):1123-35. [PubMed Link Image]
  4. Kawano J, Kotani T, Ohtaki S, Minamino N, Matsuo H, Oinuma T, Aikawa E: Characterization of rat and human steroid sulfatases. Biochim Biophys Acta. 1989 Aug 31;997(3):199-205. [PubMed Link Image]
  5. Hernandez-Guzman FG, Higashiyama T, Pangborn W, Osawa Y, Ghosh D: Structure of human estrone sulfatase suggests functional roles of membrane association. J Biol Chem. 2003 Jun 20;278(25):22989-97. Epub 2003 Mar 25. [PubMed Link Image]
  6. Basler E, Grompe M, Parenti G, Yates J, Ballabio A: Identification of point mutations in the steroid sulfatase gene of three patients with X-linked ichthyosis. Am J Hum Genet. 1992 Mar;50(3):483-91. [PubMed Link Image]
  7. Alperin ES, Shapiro LJ: Characterization of point mutations in patients with X-linked ichthyosis. Effects on the structure and function of the steroid sulfatase protein. J Biol Chem. 1997 Aug 15;272(33):20756-63. [PubMed Link Image]
  8. Sugawara T, Shimizu H, Hoshi N, Fujimoto Y, Nakajima A, Fujimoto S: PCR diagnosis of X-linked ichthyosis: identification of a novel mutation (E560P) of the steroid sulfatase gene. Hum Mutat. 2000 Mar;15(3):296. [PubMed Link Image]
  9. Oyama N, Satoh M, Iwatsuki K, Kaneko F: Novel point mutations in the steroid sulfatase gene in patients with X-linked ichthyosis: transfection analysis using the mutated genes. J Invest Dermatol. 2000 Jun;114(6):1195-9. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 6332
Enzyme 6 Name Cytochrome P450 17A1
Enzyme 6 Synonyms
  1. CYPXVII
  2. P450-C17
  3. P450c17
  4. Steroid 17-alpha-monooxygenase
  5. Steroid 17-alpha-hydroxylase/17,20 lyase
Enzyme 6 Gene Name CYP17A1
Enzyme 6 Protein Sequence >Cytochrome P450 17A1 
MWELVALLLLTLAYLFWPKRRCPGAKYPKSLLSLPLVGSLPFLPRHGHMHNNFFKLQKKY
GPIYSVRMGTKTTVIVGHHQLAKEVLIKKGKDFSGRPQMATLDIASNNRKGIAFADSGAH
WQLHRRLAMATFALFKDGDQKLEKIICQEISTLCDMLATHNGQSIDISFPVFVAVTNVIS
LICFNTSYKNGDPELNVIQNYNEGIIDNLSKDSLVDLVPWLKIFPNKTLEKLKSHVKIRN
DLLNKILENYKEKFRSDSITNMLDTLMQAKMNSDNGNAGPDQDSELLSDNHILTTIGDIF
GAGVETTTSVVKWTLAFLLHNPQVKKKLYEEIDQNVGFSRTPTISDRNRLLLLEATIREV
LRLRPVAPMLIPHKANVDSSIGEFAVDKGTEVIINLWALHHNEKEWHQPDQFMPERFLNP
AGTQLISPSVSYLPFGAGPRSCIGEILARQELFLIMAWLLQRFDLEVPDDGQLPSLEGIP
KVVFLIDSFKVKIKVRQAWREAQAEGST
Enzyme 6 Number of Residues 508
Enzyme 6 Molecular Weight 57371
Enzyme 6 Theoretical pI 8.87
Enzyme 6 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 6 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 6 Specific Function Conversion of pregnenolone and progesterone to their 17- alpha-hydroxylated products and subsequently to dehydroepiandrosterone (DHEA) and androstenedione. Catalyzes both the 17-alpha-hydroxylation and the 17,20-lyase reaction. Involved in sexual development during fetal life and at puberty
Enzyme 6 Pathways
Enzyme 6 Reactions
  • a steroid + AH2 + O2 = a 17alpha-hydroxysteroid + A + H2O
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • 1-24
Enzyme 6 Transmembrane Regions Not Available
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 181342 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P05093 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name CP17A_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1527 bp 
ATGTGGGAGCTCGTGGCTCTCTTGCTGCTTACCCTAGCTTATTTGTTTTGGCCCAAGAGA
AGGTGCCCTGGTGCCAAGTACCCCAAGAGCCTCCTGTCCCTGCCCCTGGTGGGCAGCCTG
CCATTCCTCCCCAGACATGGCCATATGCATAACAACTTCTTCAAGCTGCAGAAAAAATAT
GGCCCCATCTATTCTGTTCGTATGGGCACCAAGACTACAGTGATTGTCGGCCACCACCAG
CTGGCCAAGGAGGTGCTTATTAAGAAGGGCAAGGACTTCTCTGGGCGGCCTCAAATGGCA
ACTCTAGACATCGCGTCCAACAACCGTAAGGGTATCGCCTTCGCTGACTCTGGCGCACAC
TGGCAGCTGCATCGAAGGCTGGCGATGGCCACCTTTGCCCTGTTCAAGGATGGCGATCAG
AAGCTGGAGAAGATCATTTGTCAGGAAATCAGTACATTGTGTGATATGCTGGCCACCCAC
AACGGACAGTCCATAGACATCTCCTTTCCTGTCTTCGTGGCGGTAACCAATGTCATCTCC
TTGATCTGCTTCAATACCTCCTACAAGAATGGGGACCCTGAGTTGAATGTCATACAGAAT
TACAATGAAGGCATCATAGACAACCTGAGCAAAGACAGCCTGGTGGACCTAGTCCCCTGG
TTGAAGATTTTCCCCAACAAAACCCTGGAAAAATTAAAGAGCCATGTTAAAATACGAAAT
GATCTGCTGAATAAAATACTTGAAAATTACAAGGAGAAATTCCGGAGTGACTCTATCACC
AACATGCTGGACACACTGATGCAAGCCAAGATGAACTCAGATAATGGCAATGCTGGCCCA
GATCAAGATTCAGAGCTGCTTTCAGATAACCACATTCTCACCACCATAGGGGACATCTTT
GGGGCTGGCGTGGAGACCACCACCTCTGTGGTTAAATGGACCCTGGCCTTCCTGCTGCAC
AATCCTCAGGTGAAGAAGAAGCTCTACGAGGAGATTGACCAGAATGTGGGTTTCAGCCGC
ACACCAACTATCAGTGACCGTAACCGTCTCCTCCTGCTGGAGGCCACCATCCGAGAGGTG
CTTCGCCTCAGGCCCGTGGCCCCTATGCTCATCCCCCACAAGGCCAACGTTGACTCCAGC
ATCGGTGAGTTTGCTGTGGACAAGGGCACAGAAGTTATCATCAATCTGTGGGCGCTGCAT
CACAATGAGAAGGAGTGGCACCAGCCGGATCAGTTCATGCCTGAGCGTTTCTTGAATCCA
GCGGGGACCCAGCTCATCTCACCGTCAGTAAGCTATTTGCCCTTCGGAGCAGGACCTCGC
TCCTGTATAGGTGAGATCCTGGCCCGCCAGGAGCTCTTCCTCATCATGGCCTGGCTGCTG
CAGAGGTTCGACCTGGAGGTGCCAGATGATGGGCAGCTGCCCTCCCTGGAAGGCATCCCC
AAGGTGGTCTTTCTGATCGACTCTTTCAAAGTGAAGATCAAGGTGCGCCAGGCCTGGAGG
GAAGCCCAGGCTGAGGGTAGCACCTAA
Enzyme 6 GenBank Gene ID M14564 Link Image
Enzyme 6 GeneCard ID CYP17A1 Link Image
Enzyme 6 GenAtlas ID CYP17A1 Link Image
Enzyme 6 HGNC ID HGNC:2593 Link Image
Enzyme 6 Chromosome Location 10
Enzyme 6 Locus 10q24.3
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Chung BC, Picado-Leonard J, Haniu M, Bienkowski M, Hall PF, Shively JE, Miller WL: Cytochrome P450c17 (steroid 17 alpha-hydroxylase/17,20 lyase): cloning of human adrenal and testis cDNAs indicates the same gene is expressed in both tissues. Proc Natl Acad Sci U S A. 1987 Jan;84(2):407-11. [PubMed Link Image]
  2. Picado-Leonard J, Miller WL: Cloning and sequence of the human gene for P450c17 (steroid 17 alpha-hydroxylase/17,20 lyase): similarity with the gene for P450c21. DNA. 1987 Oct;6(5):439-48. [PubMed Link Image]
  3. Bradshaw KD, Waterman MR, Couch RT, Simpson ER, Zuber MX: Characterization of complementary deoxyribonucleic acid for human adrenocortical 17 alpha-hydroxylase: a probe for analysis of 17 alpha-hydroxylase deficiency. Mol Endocrinol. 1987 May;1(5):348-54. [PubMed Link Image]
  4. Brentano ST, Picado-Leonard J, Mellon SH, Moore CC, Miller WL: Tissue-specific, cyclic adenosine 3',5'-monophosphate-induced, and phorbol ester-repressed transcription from the human P450c17 promoter in mouse cells. Mol Endocrinol. 1990 Dec;4(12):1972-9. [PubMed Link Image]
  5. Kagimoto M, Winter JS, Kagimoto K, Simpson ER, Waterman MR: Structural characterization of normal and mutant human steroid 17 alpha-hydroxylase genes: molecular basis of one example of combined 17 alpha-hydroxylase/17,20 lyase deficiency. Mol Endocrinol. 1988 Jun;2(6):564-70. [PubMed Link Image]
  6. Auchus RJ, Miller WL: Molecular modeling of human P450c17 (17alpha-hydroxylase/17,20-lyase): insights into reaction mechanisms and effects of mutations. Mol Endocrinol. 1999 Jul;13(7):1169-82. [PubMed Link Image]
  7. Yanase T, Kagimoto M, Suzuki S, Hashiba K, Simpson ER, Waterman MR: Deletion of a phenylalanine in the N-terminal region of human cytochrome P-450(17 alpha) results in partial combined 17 alpha-hydroxylase/17,20-lyase deficiency. J Biol Chem. 1989 Oct 25;264(30):18076-82. [PubMed Link Image]
  8. Lin D, Harikrishna JA, Moore CC, Jones KL, Miller WL: Missense mutation serine106----proline causes 17 alpha-hydroxylase deficiency. J Biol Chem. 1991 Aug 25;266(24):15992-8. [PubMed Link Image]
  9. Yanase T, Waterman MR, Zachmann M, Winter JS, Simpson ER, Kagimoto M: Molecular basis of apparent isolated 17,20-lyase deficiency: compound heterozygous mutations in the C-terminal region (Arg(496)----Cys, Gln(461)----Stop) actually cause combined 17 alpha-hydroxylase/17,20-lyase deficiency. Biochim Biophys Acta. 1992 Aug 25;1139(4):275-9. [PubMed Link Image]
  10. Ahlgren R, Yanase T, Simpson ER, Winter JS, Waterman MR: Compound heterozygous mutations (Arg 239----stop, Pro 342----Thr) in the CYP17 (P45017 alpha) gene lead to ambiguous external genitalia in a male patient with partial combined 17 alpha-hydroxylase/17,20-lyase deficiency. J Clin Endocrinol Metab. 1992 Mar;74(3):667-72. [PubMed Link Image]
  11. Imai T, Globerman H, Gertner JM, Kagawa N, Waterman MR: Expression and purification of functional human 17 alpha-hydroxylase/17,20-lyase (P450c17) in Escherichia coli. Use of this system for study of a novel form of combined 17 alpha-hydroxylase/17,20-lyase deficiency. J Biol Chem. 1993 Sep 15;268(26):19681-9. [PubMed Link Image]
  12. Monno S, Ogawa H, Date T, Fujioka M, Miller WL, Kobayashi M: Mutation of histidine 373 to leucine in cytochrome P450c17 causes 17 alpha-hydroxylase deficiency. J Biol Chem. 1993 Dec 5;268(34):25811-7. [PubMed Link Image]
  13. Fardella CE, Zhang LH, Mahachoklertwattana P, Lin D, Miller WL: Deletion of amino acids Asp487-Ser488-Phe489 in human cytochrome P450c17 causes severe 17 alpha-hydroxylase deficiency. J Clin Endocrinol Metab. 1993 Aug;77(2):489-93. [PubMed Link Image]
  14. Fardella CE, Hum DW, Homoki J, Miller WL: Point mutation of Arg440 to His in cytochrome P450c17 causes severe 17 alpha-hydroxylase deficiency. J Clin Endocrinol Metab. 1994 Jul;79(1):160-4. [PubMed Link Image]
  15. Laflamme N, Leblanc JF, Mailloux J, Faure N, Labrie F, Simard J: Mutation R96W in cytochrome P450c17 gene causes combined 17 alpha-hydroxylase/17-20-lyase deficiency in two French Canadian patients. J Clin Endocrinol Metab. 1996 Jan;81(1):264-8. [PubMed Link Image]
  16. Biason-Lauber A, Kempken B, Werder E, Forest MG, Einaudi S, Ranke MB, Matsuo N, Brunelli V, Schonle EJ, Zachmann M: 17alpha-hydroxylase/17,20-lyase deficiency as a model to study enzymatic activity regulation: role of phosphorylation. J Clin Endocrinol Metab. 2000 Mar;85(3):1226-31. [PubMed Link Image]
  17. Gupta MK, Geller DH, Auchus RJ: Pitfalls in characterizing P450c17 mutations associated with isolated 17,20-lyase deficiency. J Clin Endocrinol Metab. 2001 Sep;86(9):4416-23. [PubMed Link Image]
  18. Di Cerbo A, Biason-Lauber A, Savino M, Piemontese MR, Di Giorgio A, Perona M, Savoia A: Combined 17alpha-Hydroxylase/17,20-lyase deficiency caused by Phe93Cys mutation in the CYP17 gene. J Clin Endocrinol Metab. 2002 Feb;87(2):898-905. [PubMed Link Image]
  19. Van Den Akker EL, Koper JW, Boehmer AL, Themmen AP, Verhoef-Post M, Timmerman MA, Otten BJ, Drop SL, De Jong FH: Differential inhibition of 17alpha-hydroxylase and 17,20-lyase activities by three novel missense CYP17 mutations identified in patients with P450c17 deficiency. J Clin Endocrinol Metab. 2002 Dec;87(12):5714-21. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 12986
Enzyme 7 Name cDNA FLJ75712, highly similar to Homo sapiens hydroxy-delta-5-steroid dehydrogenase, 3 beta- and steroid delta-isomerase 1
Enzyme 7 Synonyms
  1. HSD3B1, mRNA
Enzyme 7 Gene Name Not Available
Enzyme 7 Protein Sequence >cDNA FLJ75712, highly similar to Homo sapiens hydroxy-delta-5-steroid dehydrogenase, 3 beta- and steroid delta-isomerase 1 
MTGWSCLVTGAGGFLGQRIIRLLVKEKELKEIRVLDKAFGPELREEFSKLQNKTKLTVLE
GDILDEPFLKRACQDVSVIIHTACIIDVFGVTHRESIMNVNVKGTQLLLEACVQASVPVF
IYTSSIEVAGPNSYKEIIQNGHEEEPLENTWPAPYPHSKKLAEKAVLAANGWNLKNGGTL
YTCALRPMYIYGEGSRFLSASINEALNNNGILSSVGKFSTVNPVYVGNVAWAHILALRAL
QDPKKAPSIRGQFYYISDDTPHQSYDNLNYTLSKEFGLRLDSRWSFPLSLMYWIGFLLEI
VSFLLRPIYTYRPPFNRHIVTLSNSVFTFSYKKAQRDLAYKPLYSWEEAKQKTVEWVGSL
VDRHKETLKSKTQ
Enzyme 7 Number of Residues 373
Enzyme 7 Molecular Weight 42252
Enzyme 7 Theoretical pI 8.98
Enzyme 7 GO Classification Not Available
Enzyme 7 General Function Cell wall/membrane/envelope biogenesis
Enzyme 7 Specific Function Not Available
Enzyme 7 Pathways Not Available
Enzyme 7 Reactions Not Available
Enzyme 7 Pfam Domain Function Not Available
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 158256544 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID A8K691 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name A8K691_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence Not Available
Enzyme 7 GenBank Gene ID AK291556 Link Image
Enzyme 7 GeneCard ID A8K691 Link Image
Enzyme 7 GenAtlas ID Not Available
Enzyme 7 HGNC ID Not Available
Enzyme 7 Chromosome Location Not Available
Enzyme 7 Locus Not Available
Enzyme 7 SNPs Not Available
Enzyme 7 General References Not Available
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 14810
Enzyme 8 Name Solute carrier family 22 member 7
Enzyme 8 Synonyms Not Available
Enzyme 8 Gene Name SLC22A7
Enzyme 8 Protein Sequence >Solute carrier family 22 member 7 
MGFEELLEQVGGFGPFQLRNVALLALPRVLLPLHFLLPIFLAAVPAHRCALPGAPANFSH
QDVWLEAHLPREPDGTLSSCLRFAYPQALPNTTLGEERQSRGELEDEPATVPCSQGWEYD
HSEFSSTIATESQWDLVCEQKGLNRAASTFFFAGVLVGAVAFGYLSDRFGRRRLLLVAYV
STLVLGLASAASVSYVMFAITRTLTGSALAGFTIIVMPLELEWLDVEHRTVAGVLSSTFW
TGGVMLLALVGYLIRDWRWLLLAVTLPCAPGILSLWWVPESARWLLTQGHVKEAHRYLLH
CARLNGRPVCEDSFSQEAVSKVAAGERVVRRPSYLDLFRTPRLRHISLCCVVVWFGVNFS
YYGLSLDVSGLGLNVYQTQLLFGAVELPSKLLVYLSVRYAGRRLTQAGTLLGTALAFGTR
LLVSSDMKSWSTVLAVMGKAFSEAAFTTAYLFTSELYPTVLRQTGMGLTALVGRLGGSLA
PLAALLDGVWLSLPKLTYGGIALLAAGTALLLPETRQAQLPETIQDVERKSAPTSLQEEE
MPMKQVQN
Enzyme 8 Number of Residues 548
Enzyme 8 Molecular Weight 60026
Enzyme 8 Theoretical pI 7.03
Enzyme 8 GO Classification
Function
  • ion transporter activity
  • transporter activity
Process
  • cellular physiological process
  • ion transport
  • physiological process
  • transport
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 8 General Function Carbohydrate transport and metabolism
Enzyme 8 Specific Function Not Available
Enzyme 8 Pathways Not Available
Enzyme 8 Reactions Not Available
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • 1-190
Enzyme 8 Transmembrane Regions
  • 22-44
  • 143-165
  • 175-197
  • 204-221
  • 231-253
  • 260-279
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 5001689 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID Q9Y694 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name Q9Y694_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >1647 bp 
ATGGGCTTTGAGGAGCTGCTGGAGCAGGTGGGCGGCTTTGGGCCCTTCCAACTGCGGAAT
GTGGCACTGCTGGCCCTGCCCCGAGTGCTGCTACCACTGCACTTCCTCCTGCCCATCTTC
CTGGCTGCCGTGCCTGCCCACCGATGTGCCCTGCCGGGTGCCCCTGCCAACTTCAGCCAT
CAGGATGTGTGGCTGGAGGCCCATCTTCCCCGGGAGCCTGATGGCACGCTCAGCTCCTGC
CTCCGCTTTGCCTATCCCCAGGCTCTCCCCAACACCACGTTGGGGGAAGAAAGGCAGAGC
CGTGGGGAGCTGGAGGATGAACCTGCCACAGTGCCCTGCTCTCAGGGCTGGGAGTACGAC
CACTCAGAATTCTCCTCTACCATTGCAACTGAGTCCCAGTGGGATCTGGTGTGTGAGCAG
AAAGGTCTGAACAGAGCTGCGTCCACTTTCTTCTTCGCCGGTGTGCTGGTGGGGGCTGTG
GCCTTTGGATATCTGTCCGACAGGTTTGGGCGGCGGCGTCTGCTGCTGGTAGCCTACGTG
AGTACCCTGGTGCTGGGCCTGGCATCTGCAGCCTCCGTCAGCTATGTAATGTTTGCCATC
ACCCGCACCCTTACTGGCTCAGCCCTGGCTGGTTTTACCATCATCGTGATGCCACTGGAG
CTGGAGTGGCTGGATGTGGAGCACCGCACCGTGGCTGGAGTCCTGAGCAGCACCTTCTGG
ACAGGGGGCGTGATGCTGCTGGCACTGGTTGGGTACCTGATACGGGACTGGCGATGGCTT
CTGCTAGCTGTCACCCTGCCTTGTGCCCCAGGCATCCTCAGCCTCTGGTGGGTGCCTGAG
TCTGCACGCTGGCTTCTGACCCAAGGCCATGTGAAAGAGGCCCACAGGTACTTGCTCCAC
TGTGCCAGGCTCAATGGGCGGCCAGTGTGTGAGGACAGCTTCAGCCAGGAGGCTGTGAGC
AAAGTGGCCGCCGGGGAACGGGTGGTCCGAAGACCTTCATACCTAGACCTGTTCCGCACA
CCACGGCTCCGACACATCTCACTGTGCTGCGTGGTGGTGTGGTTCGGAGTGAACTTCTCC
TATTACGGCCTGAGTCTGGATGTGTCGGGGCTGGGGCTGAACGTGTACCAGACACAGCTG
TTGTTCGGGGCTGTGGAACTGCCCTCCAAGCTGCTGGTCTACTTGTCGGTGCGCTACGCA
GGACGCCGCCTCACGCAAGCCGGGACACTGCTGGGCACGGCCCTGGCGTTCGGCACTAGA
CTGCTAGTGTCCTCCGATATGAAGTCCTGGAGCACTGTCCTGGCAGTGATGGGGAAAGCT
TTTTCTGAAGCTGCCTTCACCACTGCTTACCTGTTCACTTCAGAGTTGTACCCTACGGTG
CTCAGACAGACAGGGATGGGGCTGACTGCACTGGTGGGCCGGCTGGGGGGCTCTTTGGCC
CCACTGGCGGCCTTGCTAGATGGAGTGTGGCTGTCACTGCCCAAGCTTACTTATGGGGGG
ATCGCCCTGCTGGCTGCCGGCACCGCCCTCCTGCTGCCAGAGACGAGGCAGGCACAGCTG
CCAGAGACCATCCAGGACGTGGAGAGAAAGAGTGCCCCAACCAGTCTTCAGGAGGAAGAG
ATGCCCATGAAGCAGGTCCAGAACTAA
Enzyme 8 GenBank Gene ID AF097518 Link Image
Enzyme 8 GeneCard ID Q9Y694 Link Image
Enzyme 8 GenAtlas ID SLC22A7 Link Image
Enzyme 8 HGNC ID HGNC:10971 Link Image
Enzyme 8 Chromosome Location Not Available
Enzyme 8 Locus Not Available
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 14860
Enzyme 9 Name HSD3B2 protein
Enzyme 9 Synonyms
  1. Hydroxy-delta-5-steroid dehydrogenase, 3 beta-and steroid delta-isomerase 2, isoform CRA_a
Enzyme 9 Gene Name HSD3B2
Enzyme 9 Protein Sequence >HSD3B2 protein 
MGWSCLVTGAGGLLGQRIVRLLVEEKELKEIRALDKAFRPELREEFSKLQNRTKLTVLEG
DILDEPFLKRACQDVSVVIHTACIIDVFGVTHRESIMNVNVKGTQLLLEACVQASVPVFI
YTSSIEVAGPNSYKEIIQNGHEEEPLENTWPTPYPYSKKLAEKAVLAANGWNLKNGDTLY
TCALRPTYIYGEGGPFLSASINEALNNNGILSSVGKFSTVNPVYVGNVAWAHILALRALR
DPKKAPSVRGQFYYISDDTPHQSYDNLNYILSKEFGLRLDSRWSLPLTLMYWIGFLLEVV
SFLLSPIYSYQPPFNRHTVTLSNSVFTFSYKKAQRDLAYKPLYSWEEAKQKTVEWVGSLV
DRHKETLKSKTQ
Enzyme 9 Number of Residues 372
Enzyme 9 Molecular Weight 42053
Enzyme 9 Theoretical pI 8.17
Enzyme 9 GO Classification
Function
  • 3-beta-hydroxy-delta5-steroid dehydrogenase activity
  • catalytic activity
  • intramolecular oxidoreductase activity
  • intramolecular oxidoreductase activity, transposing C=C bonds
  • isomerase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
  • steroid dehydrogenase activity
  • steroid delta-isomerase activity
Process
  • cellular lipid metabolism
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
  • steroid biosynthesis
  • steroid metabolism
Component
—
Enzyme 9 General Function Cell wall/membrane/envelope biogenesis
Enzyme 9 Specific Function Not Available
Enzyme 9 Pathways Not Available
Enzyme 9 Reactions Not Available
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 124297709 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID A2RRA5 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name A2RRA5_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >1119 bp 
ATGGGCTGGAGCTGCCTTGTGACAGGAGCAGGAGGGCTTCTGGGTCAGAGGATCGTCCGC
CTGTTGGTGGAAGAGAAGGAACTGAAGGAGATCAGGGCCTTGGACAAGGCCTTCAGACCA
GAATTGAGAGAGGAATTTTCTAAGCTCCAGAACAGGACCAAGCTGACTGTACTTGAAGGA
GACATTCTGGATGAGCCATTCCTGAAAAGAGCCTGCCAGGACGTCTCGGTCGTCATCCAC
ACCGCCTGTATCATTGATGTCTTTGGTGTCACTCACAGAGAGTCCATCATGAATGTCAAT
GTGAAAGGTACCCAGCTACTGTTGGAGGCCTGTGTCCAAGCCAGTGTGCCAGTCTTCATC
TACACCAGTAGCATAGAGGTAGCCGGGCCCAACTCCTACAAGGAAATCATCCAGAACGGC
CACGAAGAAGAGCCTCTGGAAAACACATGGCCCACTCCATACCCGTACAGCAAAAAGCTT
GCTGAGAAGGCTGTGCTGGCGGCTAATGGGTGGAATCTAAAAAATGGTGATACCTTGTAC
ACTTGTGCGTTAAGACCCACATATATCTATGGGGAAGGAGGCCCATTCCTTTCTGCCAGT
ATAAATGAGGCCCTGAACAACAATGGGATCCTGTCAAGTGTTGGAAAGTTCTCTACAGTC
AACCCAGTCTATGTTGGCAACGTGGCCTGGGCCCACATTCTGGCCTTGAGGGCTCTGCGG
GACCCCAAGAAGGCCCCAAGTGTCCGAGGTCAATTCTATTACATCTCAGATGACACGCCT
CACCAAAGCTATGATAACCTTAATTACATCCTGAGCAAAGAGTTTGGCCTCCGCCTTGAT
TCCAGATGGAGCCTTCCTTTAACCCTGATGTACTGGATTGGCTTCCTGCTGGAAGTAGTG
AGCTTCCTACTCAGCCCAATTTACTCCTATCAACCCCCCTTCAACCGCCACACAGTCACA
TTATCAAATAGTGTGTTCACCTTCTCTTACAAGAAGGCTCAGCGAGATCTGGCGTATAAG
CCACTCTACAGCTGGGAGGAAGCCAAGCAGAAAACCGTGGAGTGGGTTGGTTCCCTTGTG
GACCGGCACAAGGAGACCCTGAAGTCCAAGACTCAGTGA
Enzyme 9 GenBank Gene ID BC131488 Link Image
Enzyme 9 GeneCard ID A2RRA5 Link Image
Enzyme 9 GenAtlas ID Not Available
Enzyme 9 HGNC ID Not Available
Enzyme 9 Chromosome Location Not Available
Enzyme 9 Locus Not Available
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 15181
Enzyme 10 Name cDNA FLJ77905, highly similar to Homo sapiens sulfotransferase family, cytosolic, 2A, dehydroepiandrosterone (DHEA)-preferring, member 1 (SULT2A1), mRNA (Sulfotransferase family, cytosolic, 2A, dehydroepiandrosterone (DHEA)-preferring, member 1, isoform C
Enzyme 10 Synonyms Not Available
Enzyme 10 Gene Name SULT2A1
Enzyme 10 Protein Sequence >cDNA FLJ77905, highly similar to Homo sapiens sulfotransferase family, cytosolic, 2A, dehydroepiandrosterone (DHEA)-preferring, member 1 (SULT2A1), mRNA (Sulfotransferase family, cytosolic, 2A, dehydroepiandrosterone (DHEA)-preferring, member 1, isoform CRA_a) 
MSDDFLWFEGIAFPTMGFRSETLRKVRDEFVIRDEDVIILTYPKSGTNWLAEILCLMHSK
GDAKWIQSVPIWERSPWVESEIGYTALSETESPRLFSSHLPIQLFPKSFFSSKAKVIYLM
RNPRDVLVSGYFFWKNMKFIKKPKSWEEYFEWFCQGTVLYGSWFDHIHGWMPMREEKNFL
LLSYEELKQDTGRTIEKICQFLGKTLEPEELNLILKNSSFQSMKENKMSNYSLLSVDYVV
DKAQLLRKGVSGDWKNHFTVAQAEDFDKLFQEKMADLPRELFPWE
Enzyme 10 Number of Residues 285
Enzyme 10 Molecular Weight 33780
Enzyme 10 Theoretical pI 5.76
Enzyme 10 GO Classification Not Available
Enzyme 10 General Function Not Available
Enzyme 10 Specific Function Not Available
Enzyme 10 Pathways Not Available
Enzyme 10 Reactions Not Available
Enzyme 10 Pfam Domain Function Not Available
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 158259783 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID A8K015 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name A8K015_HUMAN Link Image
Enzyme 10 PDB ID 1OV4 Link Image
Enzyme 10 PDB File Show
Enzyme 10 3D Structure
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >858 bp 
ATGTCGGACGATTTCTTATGGTTTGAAGGCATAGCTTTCCCTACTATGGGTTTCAGATCC
GAAACCTTAAGAAAAGTACGTGATGAGTTCGTGATAAGGGATGAAGATGTAATAATATTG
ACTTACCCCAAATCAGGAACAAACTGGTTGGCTGAGATTCTCTGCCTGATGCACTCCAAG
GGGGATGCCAAGTGGATCCAATCTGTGCCCATCTGGGAGCGATCACCCTGGGTAGAGAGT
GAGATTGGGTATACAGCACTCAGTGAAACGGAGAGTCCACGTTTATTCTCCTCCCACCTC
CCCATCCAGTTATTCCCCAAGTCTTTCTTCAGTTCCAAGGCCAAGGTGATTTATCTCATG
AGAAATCCCAGAGATGTTTTGGTGTCTGGTTATTTTTTCTGGAAAAACATGAAGTTTATT
AAGAAACCAAAGTCATGGGAAGAATATTTTGAATGGTTTTGTCAAGGAACTGTGCTATAT
GGGTCATGGTTTGACCACATTCATGGCTGGATGCCCATGAGAGAGGAGAAAAACTTCCTG
TTACTGAGTTATGAGGAGCTGAAACAGGACACAGGAAGAACCATAGAGAAGATCTGTCAA
TTCCTGGGAAAGACGTTAGAACCCGAAGAACTGAACTTAATTCTCAAGAACAGCTCCTTT
CAGAGCATGAAAGAAAACAAGATGTCCAATTATTCCCTCCTGAGTGTTGATTATGTAGTG
GACAAAGCACAACTTCTGAGAAAAGGTGTATCTGGGGACTGGAAAAATCACTTCACAGTG
GCCCAAGCTGAAGACTTTGATAAATTGTTCCAAGAGAAGATGGCAGATCTTCCTCGAGAG
CTGTTCCCATGGGAATAA
Enzyme 10 GenBank Gene ID AK289380 Link Image
Enzyme 10 GeneCard ID A8K015 Link Image
Enzyme 10 GenAtlas ID Not Available
Enzyme 10 HGNC ID Not Available
Enzyme 10 Chromosome Location 19
Enzyme 10 Locus 19q13.3
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References Not Available
Enzyme 10 Metabolite References Not Available