S00551
type: Enzyme
cath: Rossmann fold
ec: https://purl.uniprot.org/enzyme/1.1.1.53
uniprot: P69167
kegg enzyme: 3alpha(or 20beta)-hydroxysteroid dehydrogenase
kegg enzyme: cortisone reductase
kegg enzyme: (R)-20-hydroxysteroid dehydrogenase
kegg enzyme: dehydrogenase, 20beta-hydroxy steroid
kegg enzyme: Delta4-3-ketosteroid hydrogenase
kegg enzyme: 20beta-hydroxysteroid dehydrogenase
kegg enzyme: 3alpha,20beta-hydroxysteroid:NAD+-oxidoreductase
kegg enzyme: NADH-20beta-hydroxysteroid dehydrogenase
kegg enzyme: 20beta-HSD
kegg pathway: Bile acid biosynthesis
kegg pathway: C21-Steroid hormone metabolism
kegg substrate: NAD+
kegg substrate: Androstan-3alpha,17beta-diol
kegg product: NADH
kegg product: 17beta-Hydroxyandrostan-3-one
kegg product: H+
pdb: 1nffA
pdb: 1nffB
pdb: 1nfqA
pdb: 1nfqB
pdb: 1nfqC
pdb: 1nfqD
pdb: 1nfrA
pdb: 1nfrB
pdb: 1nfrC
pdb: 1nfrD
pdb bound state: Unbound
  compound: NAD+
  pdb: 1nfqA
pdb bound state: Unbound
  compound: NAD+
  pdb: 1nfqB
pdb bound state: Unbound
  compound: NAD+
  pdb: 1nfqC
pdb bound state: Unbound
  compound: NAD+
  pdb: 1nfqD
pdb bound state: Unbound
  compound: Androstan-3alpha,17beta-diol
  pdb: 1nffA
pdb bound state: Unbound
  compound: Androstan-3alpha,17beta-diol
  pdb: 1nffB
pdb bound state: Unbound
  compound: Androstan-3alpha,17beta-diol
  pdb: 1nfrA
pdb bound state: Unbound
  compound: Androstan-3alpha,17beta-diol
  pdb: 1nfrB
pdb bound state: Unbound
  compound: Androstan-3alpha,17beta-diol
  pdb: 1nfrC
pdb bound state: Unbound
  compound: Androstan-3alpha,17beta-diol
  pdb: 1nfrD
pdb bound state: Unbound
  compound: NADH
  pdb: 1nffA
pdb bound state: Unbound
  compound: NADH
  pdb: 1nffB
pdb bound state: Unbound
  compound: NADH
  pdb: 1nfrA
pdb bound state: Unbound
  compound: NADH
  pdb: 1nfrB
pdb bound state: Unbound
  compound: NADH
  pdb: 1nfrC
pdb bound state: Unbound
  compound: NADH
  pdb: 1nfrD
pdb bound state: Unbound
  compound: 17beta-Hydroxyandrostan-3-one
  pdb: 1nffA
pdb bound state: Unbound
  compound: 17beta-Hydroxyandrostan-3-one
  pdb: 1nffB
pdb bound state: Unbound
  compound: 17beta-Hydroxyandrostan-3-one
  pdb: 1nfqA
pdb bound state: Unbound
  compound: 17beta-Hydroxyandrostan-3-one
  pdb: 1nfqB
pdb bound state: Unbound
  compound: 17beta-Hydroxyandrostan-3-one
  pdb: 1nfqC
pdb bound state: Unbound
  compound: 17beta-Hydroxyandrostan-3-one
  pdb: 1nfqD
pdb bound state: Unbound
  compound: 17beta-Hydroxyandrostan-3-one
  pdb: 1nfrA
pdb bound state: Unbound
  compound: 17beta-Hydroxyandrostan-3-one
  pdb: 1nfrB
pdb bound state: Unbound
  compound: 17beta-Hydroxyandrostan-3-one
  pdb: 1nfrC
pdb bound state: Unbound
  compound: 17beta-Hydroxyandrostan-3-one
  pdb: 1nfrD
active site residues resources: http://ezcatdb.cbrc.jp/EzCatDB/reference/S00551#17
reference for catalytic mechanism: ReferenceForCatalyticMechanism
  reference index: 12
reference for catalytic mechanism: ReferenceForCatalyticMechanism
  reference index: 13
  reference section: Fig.8b, p.632-637
reference for catalytic mechanism: ReferenceForCatalyticMechanism
  reference index: 15
  reference section: Fig.3
reference for catalytic mechanism: ReferenceForCatalyticMechanism
  reference index: 16
  reference section: p.458-460
references: The altered specificity of cortisone reductase with certain retroandrostan-3-one substrates.
references: The functioning of a nicotinamide--adenine dinucleotide-dependent dehydrogenase and the structure adjacent to the reacting carbon atom of the substrate.
references: Cortisone reductase and some small non-steroid analogues of its steroid substrates.
references: Renaturation and urea-induced denaturation of 20 beta-hydroxysteroid dehydrogenase studied in solution and in the immobilized state.
references: Structural requirements in 20-oxo-steroids for interaction with the catalytic site of 20 beta-hydroxysteroid dehydrogenase.
references: Bifunctional enzyme activity at the same active site: competitive inhibition kinetics with 3 alpha/20 beta-hydroxysteroid dehydrogenase.
references: Structural requirements in 20-oxo-steroids for interaction with the binding site of 20beta-hydroxysteroid dehydrogenase.
references: Crystallization and preliminary crystallographic study of 3 alpha, 20 beta-hydroxysteroid dehydrogenase from Streptomyces hydrogenans.
references: Crystals of active tetramers of 3 alpha, 20 beta-hydroxysteroid dehydrogenase.
references: 20 beta-hydroxysteroid dehydrogenase of neonatal pig testis: 3 alpha/beta-hydroxysteroid dehydrogenase activities catalyzed by highly purified enzyme.
references: Three-dimensional structure of holo 3 alpha,20 beta-hydroxysteroid dehydrogenase: a member of a short-chain dehydrogenase family.
references: Mechanism of inhibition of 3 alpha, 20 beta-hydroxysteroid dehydrogenase by a licorice-derived steroidal inhibitor.
references: The refined three-dimensional structure of 3 alpha,20 beta-hydroxysteroid dehydrogenase and possible roles of the residues conserved in short-chain dehydrogenases.
references: The rat 17 alpha-hydroxylase-17,20-desmolase (CYP17) active site: computerized homology modeling and site directed mutagenesis.
references: Structure and function of steroid dehydrogenases involved in hypertension, fertility, and cancer.
references: Directed evolution approach to a structural genomics project: Rv2002 from Mycobacterium tuberculosis.
comment: This enzyme belongs to the short-chain dehydrogenase/reductase (SDR) superfamily, along with its homologous enzyme (S00326 in EzCatDB) and Drosophia alcohol dehydrogenase (S00319 in EzCatDB). However, this enzyme has got an additional catalytic residue, Glu142, in addition to a classical catalytic triad composed of conserved residues, Ser, Tyr, and Lys. Moreover, the conformation of these residues, compared to that of the NAD molecule and substrate, seems to be slightly different from that of the homologous enzymes. Glu142 seems to interact with the substrate oxygen atom, whereas Ser140 does not interact with the oxygen atom, unlike those catalytic Ser residues in the other homologous enzymes (see [16]). According to the literature [16], Glu142 might reverse the effect of Lys157, which is supposed to modulate the pKa of Tyr153 in the homologous enzymes.

Rossmann fold
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.40.50.720
catalytic domain: index.html

Bile acid biosynthesis
type: KeggPathway
references: KEGG:MAP00120

C21-Steroid hormone metabolism
type: KeggPathway
references: KEGG:MAP00140

NAD+
type: KeggSubstrate
references: KEGG:C00003
compound type: amide group
compound type: amine group
compound type: nucleotide
references: CHEBI:15846
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Androstan-3alpha,17beta-diol
type: KeggSubstrate
references: KEGG:C03852
compound type: carbohydrate
compound type: steroid
references: CHEBI:36713
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

NADH
type: KeggProduct
references: KEGG:C00004
compound type: amide group
compound type: amine group
compound type: nucleotide
references: CHEBI:16908
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

17beta-Hydroxyandrostan-3-one
type: KeggProduct
references: KEGG:C03917
compound type: carbohydrate
compound type: steroid
references: CHEBI:16330
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

H+
type: KeggProduct
references: KEGG:C00080
compound type: others
references: CHEBI:15378
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

1nffA
type: Pdb
references: 1nff
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1nff
catalytic residue: SER 140;GLU 142;TYR 153;LYS 157

1nffB
type: Pdb
references: 1nff
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1nff
catalytic residue: SER 140;GLU 142;TYR 153;LYS 157

1nfqA
type: Pdb
references: 1nfq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1nfq
catalytic residue: SER 140;GLU 142;TYR 153;LYS 157

1nfqB
type: Pdb
references: 1nfq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1nfq
catalytic residue: SER 140;GLU 142;TYR 153;LYS 157

1nfqC
type: Pdb
references: 1nfq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1nfq
catalytic residue: SER 140;GLU 142;TYR 153;LYS 157

1nfqD
type: Pdb
references: 1nfq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1nfq
catalytic residue: SER 140;GLU 142;TYR 153;LYS 157

1nfrA
type: Pdb
references: 1nfr
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1nfr
catalytic residue: SER 140;GLU 142;TYR 153;LYS 157

1nfrB
type: Pdb
references: 1nfr
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1nfr
catalytic residue: SER 140;GLU 142;TYR 153;LYS 157

1nfrC
type: Pdb
references: 1nfr
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1nfr
catalytic residue: SER 140;GLU 142;TYR 153;LYS 157

1nfrD
type: Pdb
references: 1nfr
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1nfr
catalytic residue: SER 140;GLU 142;TYR 153;LYS 157

The altered specificity of cortisone reductase with certain retroandrostan-3-one substrates.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/168869
journal: Biochem J
volume: 145
pages: 483-9
published year: 1975
authors:
  item: Gibb W
  item: Jeffery J

The functioning of a nicotinamide--adenine dinucleotide-dependent dehydrogenase and the structure adjacent to the reacting carbon atom of the substrate.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/172381
journal: Biochem Soc Trans
volume: 3
pages: 674-5
published year: 1975
authors:
  item: White IH
  item: Jeffery J

Cortisone reductase and some small non-steroid analogues of its steroid substrates.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/902901
journal: Biochem Soc Trans
volume: 5
pages: 723-4
published year: 1977
authors:
  item: White IH
  item: Jeffery J

Renaturation and urea-induced denaturation of 20 beta-hydroxysteroid dehydrogenase studied in solution and in the immobilized state.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/6938245
journal: Biochim Biophys Acta
volume: 616
pages: 143-52
published year: 1980
authors:
  item: Pasta P
  item: Carrea G
  item: Longhi R
  item: Antonini E

Structural requirements in 20-oxo-steroids for interaction with the catalytic site of 20 beta-hydroxysteroid dehydrogenase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/6930328
journal: Chem Pharm Bull (Tokyo)
volume: 28
pages: 730-6
published year: 1980
authors:
  item: Hayakawa T
  item: Tanimoto T
  item: Kawamura J

Bifunctional enzyme activity at the same active site: competitive inhibition kinetics with 3 alpha/20 beta-hydroxysteroid dehydrogenase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/6929616
journal: Steroids
volume: 35
pages: 111-8
published year: 1980
authors:
  item: Sweet F
  item: Ahmed R
  item: Morgan TE
  item: Sweet BC

Structural requirements in 20-oxo-steroids for interaction with the binding site of 20beta-hydroxysteroid dehydrogenase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/6944159
journal: Chem Pharm Bull (Tokyo)
volume: 29
pages: 476-84
published year: 1981
authors:
  item: Kawamura J
  item: Tanimoto T
  item: Fukuda H
  item: Hayakawa T

Crystallization and preliminary crystallographic study of 3 alpha, 20 beta-hydroxysteroid dehydrogenase from Streptomyces hydrogenans.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/6587118
journal: J Mol Biol
volume: 175
pages: 225-7
published year: 1984
authors:
  item: Fitzgerald PM
  item: Duax WL
  item: Punzi JS
  item: Orr JC

Crystals of active tetramers of 3 alpha, 20 beta-hydroxysteroid dehydrogenase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/3455925
journal: J Biol Chem
volume: 261
pages: 1306-8
published year: 1986
authors:
  item: Ghosh D
  item: Punzi JS
  item: Duax WL

20 beta-hydroxysteroid dehydrogenase of neonatal pig testis: 3 alpha/beta-hydroxysteroid dehydrogenase activities catalyzed by highly purified enzyme.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2064995
journal: J Steroid Biochem Mol Biol
volume: 38
pages: 787-94
published year: 1991
authors:
  item: Ohno S
  item: Nakajin S
  item: Shinoda M

Three-dimensional structure of holo 3 alpha,20 beta-hydroxysteroid dehydrogenase: a member of a short-chain dehydrogenase family.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS)
medline id: 92052211
references: http://www.ncbi.nlm.nih.gov/pubmed/1946424
journal: Proc Natl Acad Sci U S A
volume: 88
pages: 10064-8
published year: 1991
authors:
  item: Ghosh D
  item: Weeks CM
  item: Grochulski P
  item: Duax WL
  item: Erman M
  item: Rimsay RL
  item: Orr JC
references: P19992

Mechanism of inhibition of 3 alpha, 20 beta-hydroxysteroid dehydrogenase by a licorice-derived steroidal inhibitor.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/7866748
journal: Structure
volume: 2
pages: 973-80
published year: 1994
authors:
  item: Ghosh D
  item: Erman M
  item: Wawrzak Z
  item: Duax WL
  item: Pangborn W
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

The refined three-dimensional structure of 3 alpha,20 beta-hydroxysteroid dehydrogenase and possible roles of the residues conserved in short-chain dehydrogenases.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/7922040
journal: Structure
volume: 2
pages: 629-40
published year: 1994
authors:
  item: Ghosh D
  item: Wawrzak Z
  item: Weeks CM
  item: Duax WL
  item: Erman M
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

The rat 17 alpha-hydroxylase-17,20-desmolase (CYP17) active site: computerized homology modeling and site directed mutagenesis.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7696141
journal: J Steroid Biochem Mol Biol
volume: 52
pages: 209-18
published year: 1995
authors:
  item: Buczko E
  item: Koh YC
  item: Miyagawa Y
  item: Dufau ML

Structure and function of steroid dehydrogenases involved in hypertension, fertility, and cancer.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9029722
journal: Steroids
volume: 62
pages: 95-100
published year: 1997
authors:
  item: Duax WL
  item: Ghosh D

Directed evolution approach to a structural genomics project: Rv2002 from Mycobacterium tuberculosis.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12524453
journal: Proc Natl Acad Sci U S A
volume: 100
pages: 455-60
published year: 2003
authors:
  item: Yang JK
  item: Park MS
  item: Waldo GS
  item: Suh SW
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl