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Sequence of AK1C1_HUMAN

EC Number:1.1.1

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Q04828
Homo sapiens
323
36788
Reaction
Other sequences found for EC No. 1.1.1

EC Number:1.1.1.50

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
3alpha-hydroxysteroid 3-dehydrogenase (Si-specific)
Q04828
Homo sapiens
323
36788
Reaction
a 3alpha-hydroxysteroid + NAD(P)+ = a 3-oxosteroid + NAD(P)H + H+
Other sequences found for EC No. 1.1.1.50

EC Number:1.1.1.51

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
3(or 17)beta-hydroxysteroid dehydrogenase
Q04828
Homo sapiens
323
36788
Reaction
testosterone + NAD(P)+ = androstenedione + NAD(P)H + H+
Other sequences found for EC No. 1.1.1.51

EC Number:1.1.1.53

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
3alpha(or 20beta)-hydroxysteroid dehydrogenase
Q04828
Homo sapiens
323
36788
Reaction
androstan-3alpha,17beta-diol + NAD+ = 17beta-hydroxyandrostan-3-one + NADH + H+
Other sequences found for EC No. 1.1.1.53

EC Number:1.1.1.62

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
17beta-estradiol 17-dehydrogenase
Q04828
Homo sapiens
323
36788
Reaction
17beta-estradiol + NAD(P)+ = estrone + NAD(P)H + H+
Other sequences found for EC No. 1.1.1.62

EC Number:1.1.1.112

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
indanol dehydrogenase
Q04828
Homo sapiens
323
36788
Reaction
indan-1-ol + NAD(P)+ = indanone + NAD(P)H + H+
Other sequences found for EC No. 1.1.1.112

EC Number:1.1.1.149

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
20alpha-hydroxysteroid dehydrogenase
Q04828
Homo sapiens
323
36788
Reaction
17alpha,20alpha-dihydroxypregn-4-en-3-one + NAD(P)+ = 17alpha-hydroxyprogesterone + NAD(P)H + H+
Other sequences found for EC No. 1.1.1.149

EC Number:1.1.1.209

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
3(or 17)alpha-hydroxysteroid dehydrogenase
Q04828
Homo sapiens
323
36788
Reaction
androsterone + NAD(P)+ = 5alpha-androstane-3,17-dione + NAD(P)H + H+
Other sequences found for EC No. 1.1.1.209

EC Number:1.1.1.210

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
3beta(or 20alpha)-hydroxysteroid dehydrogenase
Q04828
Homo sapiens
323
36788
Reaction
5alpha-androstan-3beta,17beta-diol + NADP+ = 17beta-hydroxy-5alpha-androstan-3-one + NADPH + H+
Other sequences found for EC No. 1.1.1.210

EC Number:1.1.1.270

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
3beta-hydroxysteroid 3-dehydrogenase
Q04828
Homo sapiens
323
36788
Reaction
a 3beta-hydroxysteroid + NADP+ = a 3-oxosteroid + NADPH + H+
Other sequences found for EC No. 1.1.1.270

EC Number:1.1.1.357

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
3alpha-hydroxysteroid 3-dehydrogenase
Q04828
Homo sapiens
323
36788
Reaction
a 3alpha-hydroxysteroid + NAD(P)+ = a 3-oxosteroid + NAD(P)H + H+
Other sequences found for EC No. 1.1.1.357

EC Number:1.3.1.20

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
trans-1,2-dihydrobenzene-1,2-diol dehydrogenase
Q04828
Homo sapiens
323
36788
Reaction
trans-1,2-dihydrobenzene-1,2-diol + NADP+ = catechol + NADPH + H+
Other sequences found for EC No. 1.3.1.20

General information:

Sequence
show sequence in fasta format
  0 MDSKYQCVKL NDGHFMPVLG FGTYAPAEVP KSKALEATKL AIEAGFRHID SAHLYNNEEQ
 60 VGLAIRSKIA DGSVKREDIF YTSKLWCNSH RPELVRPALE RSLKNLQLDY VDLYLIHFPV
120 SVKPGEEVIP KDENGKILFD TVDLCATWEA VEKCKDAGLA KSIGVSNFNR RQLEMILNKP
180 GLKYKPVCNQ VECHPYFNQR KLLDFCKSKD IVLVAYSALG SHREEPWVDP NSPVLLEDPV
240 LCALAKKHKR TPALIALRYQ LQRGVVVLAK SYNEQRIRQN VQVFEFQLTS EEMKAIDGLN
300 RNVRYLTLDI FAGPPNYPFS DEY
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
512869
Stolz A.,Hammond L.,Lou H.,Takikawa H.,Ronk M.,Shively J.E.
cDNA cloning and expression of the human hepatic bile acid-binding protein. A member of the monomeric reductase gene family.
J. Biol. Chem.
268
10448-10457
1993
512870
Lou H.,Hammond L.,Sharma V.,Sparkes R.S.,Lusis A.J.,Stolz A.
Genomic organization and chromosomal localization of a novel human hepatic dihydrodiol dehydrogenase with high affinity bile acid binding.
J. Biol. Chem.
269
8416-8422
1994
512871
Ciaccio P.J.,Jaiswal A.K.,Tew K.D.
Regulation of human dihydrodiol dehydrogenase by Michael acceptor xenobiotics.
J. Biol. Chem.
269
15558-15562
1994
512872
Khanna M.,Qin K.-N.,Cheng K.-C.
Distribution of 3 alpha-hydroxysteroid dehydrogenase in rat brain and molecular cloning of multiple cDNAs encoding structurally related proteins in humans.
J. Steroid Biochem. Mol. Biol.
53
41-46
1995
512873
Nishizawa M.,Nakajima T.,Yasuda K.,Kanzaki H.,Sasaguri Y.,Watanabe K.,Ito S.
Close kinship of human 20alpha-hydroxysteroid dehydrogenase gene with three aldo-keto reductase genes.
Genes Cells
5
111-125
2000
512874
Zhang Y.,Dufort I.,Rheault P.,Luu-The V.
Characterization of a human 20alpha-hydroxysteroid dehydrogenase.
J. Mol. Endocrinol.
25
221-228
2000
512876
Deloukas P.,Earthrowl M.E.,Grafham D.V.,Rubenfield M.,French L.,Steward C.A.,Sims S.K.,Jones M.C.,Searle S.,Scott C.,Howe K.,Hunt S.E.,Andrews T.D.,Gilbert J.G.R.,Swarbreck D.,Ashurst J.L.,Taylor A.,Battles J.,Bird C.P.,Ainscough R.,Almeida J.P.,Ashwell R.I.S.,Ambrose K.D.,Babbage A.K.,Bagguley C.L.,Bailey J.,Banerjee R.,Bates K.,Beasley H.,Bray-Allen S.,Brown A.J.,Brown J.Y.,Burford D.C.,Burrill W.,Burton J.,Cahill P.,Camire D.,Carter N.P.,Chapman J.C.,Clark S.Y.,Clarke G.,Clee C.M.,Clegg S.,Corby N.,Coulson A.,Dhami P.,Dutta I.,Dunn M.,Faulkner L.,Frankish A.,Frankland J.A.,Garner P.,Garnett J.,Gribble S.,Griffiths C.,Grocock R.,Gustafson E.,Hammond S.,Harley J.L.,Hart E.,Heath P.D.,Ho T.P.,Hopkins B.,Horne J.,Howden P.J.,Huckle E.,Hynds C.,Johnson C.,Johnson D.,Kana A.,Kay M.,Kimberley A.M.,Kershaw J.K.,Kokkinaki M.,Laird G.K.,Lawlor S.,Lee H.M.,Leongamornlert D.A.,Laird G.,Lloyd C.,Lloyd D.M.,Loveland J.,Lovell J.,McLaren S.,McLay K.E.,McMurray A.,Mashreghi-Mohammadi M.,Matthews L.,Milne S.,Nickerson T.,Nguyen M.,Overton-Larty E.,Palmer S.A.,Pearce A.V.,Peck A.I.,Pelan S.,Phillimore B.,Porter K.,Rice C.M.,Rogosin A.,Ross M.T.,Sarafidou T.,Sehra H.K.,Shownkeen R.,Skuce C.D.,Smith M.,Standring L.,Sycamore N.,Tester J.,Thorpe A.,Torcasso W.,Tracey A.,Tromans A.,Tsolas J.,Wall M.,Walsh J.,Wang H.,Weinstock K.,West A.P.,Willey D.L.,Whitehead S.L.,Wilming L.,Wray P.W.,Young L.,Chen Y.,Lovering R.C.,Moschonas N.K.,Siebert R.,Fechtel K.,Bentley D.,Durbin R.M.,Hubbard T.,Doucette-Stamm L.,Beck S.,Smith D.R.,Rogers J.
The DNA sequence and comparative analysis of human chromosome 10.
Nature
429
375-381
2004
512877
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Genome Res.
14
2121-2127
2004
512878
Qin K.-N.,New M.I.,Cheng K.-C.
Molecular cloning of multiple cDNAs encoding human enzymes structurally related to 3 alpha-hydroxysteroid dehydrogenase.
J. Steroid Biochem. Mol. Biol.
46
673-679
1993
512879
Hara A.,Matsuura K.,Tamada Y.,Sato K.,Miyabe Y.,Deyashiki Y.,Ishida N.
Relationship of human liver dihydrodiol dehydrogenases to hepatic bile-acid-binding protein and an oxidoreductase of human colon cells.
Biochem. J.
313
373-376
1996
512880
Deyashiki Y.,Ogasawara A.,Nakayama T.,Nakanishi M.,Miyabe Y.,Sato K.,Hara A.
Molecular cloning of two human liver 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase isoenzymes that are identical with chlordecone reductase and bile-acid binder.
Biochem. J.
299
545-552
1994
512881
Penning T.M.,Burczynski M.E.,Jez J.M.,Hung C.F.,Lin H.K.,Ma H.,Moore M.,Palackal N.,Ratnam K.
Human 3alpha-hydroxysteroid dehydrogenase isoforms (AKR1C1-AKR1C4) of the aldo-keto reductase superfamily: functional plasticity and tissue distribution reveals roles in the inactivation and formation of male and female sex hormones.
Biochem. J.
351
67-77
2000
512882
Steckelbroeck S.,Jin Y.,Gopishetty S.,Oyesanmi B.,Penning T.M.
Human cytosolic 3alpha-hydroxysteroid dehydrogenases of the aldo-keto reductase superfamily display significant 3beta-hydroxysteroid dehydrogenase activity: implications for steroid hormone metabolism and action.
J. Biol. Chem.
279
10784-10795
2004
512883
Jin Y.,Duan L.,Lee S.H.,Kloosterboer H.J.,Blair I.A.,Penning T.M.
Human cytosolic hydroxysteroid dehydrogenases of the aldo-ketoreductase superfamily catalyze reduction of conjugated steroids: implications for phase I and phase II steroid hormone metabolism.
J. Biol. Chem.
284
10013-10022
2009
512884
Couture J.-F.,Legrand P.,Cantin L.,Luu-The V.,Labrie F.,Breton R.
Human 20alpha-hydroxysteroid dehydrogenase: crystallographic and site-directed mutagenesis studies lead to the identification of an alternative binding site for C21-steroids.
J. Mol. Biol.
331
593-604
2003
512885
El-Kabbani O.,Dhagat U.,Soda M.,Endo S.,Matsunaga T.,Hara A.
Probing the inhibitor selectivity pocket of human 20alpha-hydroxysteroid dehydrogenase (AKR1C1) with X-ray crystallography and site-directed mutagenesis.
Bioorg. Med. Chem. Lett.
21
2564-2567
2011