KEGG   ENZYME: 1.1.1.112Help
Entry
EC 1.1.1.112                Enzyme                                 

Name
indanol dehydrogenase
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With NAD+ or NADP+ as acceptor
BRITE hierarchy
Sysname
indan-1-ol:NAD(P)+ 1-oxidoreductase
Reaction(IUBMB)
indan-1-ol + NAD(P)+ = indanone + NAD(P)H + H+ [RN:R03582 R03583]
Reaction(KEGG)
Substrate
indan-1-ol [CPD:C01710];
NAD+ [CPD:C00003];
NADP+ [CPD:C00006]
Product
indanone [CPD:C01504];
NADH [CPD:C00004];
NADPH [CPD:C00005];
H+ [CPD:C00080]
Comment
3(20)alpha-Hydroxysteroids are also oxidized, more slowly.
History
EC 1.1.1.112 created 1972
Reference
1  [PMID:4397102]
  Authors
Billings RE, Sullivan HR, McMahon RE.
  Title
The dehydrogenation of 1-indanol by a soluble oxidoreductase from bovine liver.
  Journal
J Biol Chem 246:3512-7 (1971)
Reference
2  [PMID:2559080]
  Authors
Hara A, Nakagawa M, Taniguchi H, Sawada H.
  Title
3(20)alpha-hydroxysteroid dehydrogenase activity of monkey liver indanol dehydrogenase.
  Journal
J Biochem (Tokyo) 106:900-3 (1989)
Other DBs
ExplorEnz - The Enzyme Database: 1.1.1.112
IUBMB Enzyme Nomenclature: 1.1.1.112
ExPASy - ENZYME nomenclature database: 1.1.1.112
BRENDA, the Enzyme Database: 1.1.1.112
CAS: 37250-43-4

KEGG   ENZYME: 1.1.1.188Help
Entry
EC 1.1.1.188                Enzyme                                 

Name
prostaglandin-F synthase;
prostaglandin-D2 11-reductase;
reductase, 15-hydroxy-11-oxoprostaglandin;
PGD2 11-ketoreductase;
PGF2alpha synthetase;
prostaglandin 11-ketoreductase;
prostaglandin D2-ketoreductase;
prostaglandin F synthase;
prostaglandin F synthetase;
synthetase, prostaglandin F2alpha;
PGF synthetase;
NADPH-dependent prostaglandin D2 11-keto reductase;
prostaglandin 11-keto reductase
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With NAD+ or NADP+ as acceptor
BRITE hierarchy
Sysname
(5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate:NADP+ 11-oxidoreductase
Reaction(IUBMB)
(5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate + NADP+ = (5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADPH + H+ [RN:R02684]
Reaction(KEGG)
R02684;
(other) R02799
Show
Substrate
(5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate [CPD:C00639];
NADP+ [CPD:C00006]
Product
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate [CPD:C00696];
NADPH [CPD:C00005];
H+ [CPD:C00080]
Comment
Reduces prostaglandin D2 and prostaglandin H2 to prostaglandin F2; prostaglandin D2 is not an intermediate in the reduction of prostaglandin H2. Also catalyses the reduction of a number of carbonyl compounds, such as 9,10-phenanthroquinone and 4-nitroacetophenone.
History
EC 1.1.1.188 created 1984, modified 1989, modified 1990
Pathway
ec00590  Arachidonic acid metabolism
Orthology
K04119  aldo-keto reductase family 1 member C3
Genes
HSA: 8644(AKR1C3)
PTR: 100612718(AKR1C3)
PPS: 100986388(AKR1C3)
GGO: 101144878
PON: 100174617(AKR1C3)
NLE: 100604844(AKR1C3)
MCC: 711440(AKR1C3)
MCF: 102142023(HSD17B5)
RBB: 108532990
SBQ: 101041594
CFA: 497070(AKR1C3)
FCA: 100510801(AKR1C3)
PTG: 102963188
AJU: 106988139
BTA: 100139386(20ALPHA-HSD) 282138(AKR1C4) 506594 527068 538060 617917(AKR1C3) 782884 785762
BOM: 102269337
BIU: 109568087
SSC: 733634(AKR1C1)
LVE: 103069218
ECB: 100070616
MYB: 102255491
MYD: 102751586
TMU: 101342771
OAA: 100085065
PSS: 102446010
PVT: 110088827
XLA: 100049750(LOC100490956.L) 443571(akr1c3.L)
XTR: 105946859 779627(akr1c3)
 » show all
Taxonomy
Reference
1  [PMID:7248318]
  Authors
Reingold DF, Kawasaki A, Needleman P.
  Title
A novel prostaglandin 11-keto reductase found in rabbit liver.
  Journal
Biochim Biophys Acta 659:179-88 (1981)
DOI:10.1016/0005-2744(81)90282-5
Reference
2
  Authors
Watanabe, K., Shimizu, T. and Hayaishi, O.
  Title
Enzymatic conversion of prostaglandin-D2 to prostaglandin-F2alpha in the rat lung.
  Journal
Biochem Int 2:603-610 (1981)
Reference
3  [PMID:3858278]
  Authors
Watanabe K, Yoshida R, Shimizu T, Hayaishi O.
  Title
Enzymatic formation of prostaglandin F2 alpha from prostaglandin H2 and D2. Purification and properties of prostaglandin F synthetase from bovine lung.
  Journal
J Biol Chem 260:7035-41 (1985)
Reference
4  [PMID:7248317]
  Authors
Wong PY.
  Title
Purification and partial characterization of prostaglandin D2 11-keto reductase in rabbit liver.
  Journal
Biochim Biophys Acta 659:169-78 (1981)
DOI:10.1016/0005-2744(81)90281-3
Reference
5  [PMID:7132748]
  Authors
Wong PY.
  Title
Purification of PGD2 11-ketoreductase from rabbit liver.
  Journal
Methods Enzymol 86:117-25 (1982)
Other DBs
ExplorEnz - The Enzyme Database: 1.1.1.188
IUBMB Enzyme Nomenclature: 1.1.1.188
ExPASy - ENZYME nomenclature database: 1.1.1.188
BRENDA, the Enzyme Database: 1.1.1.188
CAS: 55976-95-9

KEGG   ENZYME: 1.1.1.239Help
Entry
EC 1.1.1.239                Enzyme                                 

Name
3alpha(17beta)-hydroxysteroid dehydrogenase (NAD+);
3alpha,17beta-hydroxy steroid dehydrogenase;
3alpha(17beta)-HSD;
17-ketoreductase (ambiguous);
17beta-HSD (ambiguous);
HSD17B6 (gene name);
HSD17B8 (gene name)
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With NAD+ or NADP+ as acceptor
BRITE hierarchy
Sysname
3alpha(or 17beta)-hydroxysteroid:NAD+ oxidoreductase
Reaction(IUBMB)
testosterone + NAD+ = androstenedione + NADH + H+ [RN:R01836]
Reaction(KEGG)
Substrate
testosterone [CPD:C00535];
NAD+ [CPD:C00003]
Product
androstenedione [CPD:C00280];
NADH [CPD:C00004];
H+ [CPD:C00080]
Comment
Also acts on other 17beta-hydroxysteroids and on the 3alpha-hydroxy group of pregnanes and bile acids. Different from EC 1.1.1.50 3alpha-hydroxysteroid dehydrogenase (Si-specific) or EC 1.1.1.213 3alpha-hydroxysteroid dehydrogenase (Re-specific).
History
EC 1.1.1.239 created 1992, modified 2012 (EC 1.1.1.63 created 1965, incorporated 2012)
Pathway
ec00140  Steroid hormone biosynthesis
ec01100  Metabolic pathways
Orthology
K13368  17beta-estradiol 17-dehydrogenase / 3alpha(17beta)-hydroxysteroid dehydrogenase (NAD+)
K13369  17beta-estradiol 17-dehydrogenase / all-trans-retinol dehydrogenase (NAD+) / 3alpha(17beta)-hydroxysteroid dehydrogenase (NAD+)
K13370  17beta-estradiol 17-dehydrogenase / 3alpha(17beta)-hydroxysteroid dehydrogenase (NAD+)
Genes
HSA: 3294(HSD17B2) 7923(HSD17B8) 8630(HSD17B6)
PTR: 454269(HSD17B2) 746685(HSD17B8)
PPS: 100983435(HSD17B2) 100993294(HSD17B8) 100996145(HSD17B6)
GGO: 101131453(HSD17B2) 101143846(HSD17B8) 101153072(HSD17B6)
PON: 100456547(HSD17B2) 100458219(HSD17B6) 100461538(HSD17B8)
NLE: 100588757(HSD17B2) 100606923(HSD17B6) 100607728(HSD17B8)
MCC: 713549(HSD17B6) 714282(HSD17B2) 718119(HSD17B8)
MCF: 101926544(HSD17B6) 102119721(HSD17B2) 102134563(HSD17B8)
CSAB: 103221677(HSD17B8) 103233373(HSD17B2) 103238543(HSD17B6)
RRO: 104657981(HSD17B8) 104671622(HSD17B2) 104673659(HSD17B6)
RBB: 108516069(HSD17B6) 108521311(HSD17B2) 108540288(HSD17B8)
CJC: 100387390(HSD17B6) 100390710(HSD17B2) 100415565(HSD17B8)
SBQ: 101030366(HSD17B2) 101042328(HSD17B8) 101054253(HSD17B6)
MMU: 14979(H2-Ke6) 15486(Hsd17b2) 27400(Hsd17b6)
RNO: 100362350 286964(Hsd17b6) 361802(Hsd17b8) 79243(Hsd17b2)
CGE: 100751897(Hsd17b2) 100762147(Hsd17b6) 100766230(Hsd17b8)
NGI: 103730224(Hsd17b6) 103739734(Hsd17b8) 103748738(Hsd17b2)
HGL: 101699287(Hsd17b6) 101719685(Hsd17b2) 101726130(Hsd17b8)
OCU: 100353430(HSD17B8) 100358604(HSD17B2)
TUP: 102481564(HSD17B2) 102485005(HSD17B6) 102494154(HSD17B8)
CFA: 481118(HSD17B6) 489690(HSD17B2) 607895(HSD17B8)
AML: 100474694(HSD17B6) 100475452(HSD17B8) 100484508(HSD17B2)
UMR: 103656323(HSD17B6) 103662132(HSD17B2) 103665501(HSD17B8)
ORO: 101368715(HSD17B6) 101374521(HSD17B8) 101379076(HSD17B2)
FCA: 101085592(HSD17B2) 101086309 101088341(HSD17B6) 111556166
PTG: 102958819(HSD17B2) 102968797(HSD17B8) 102971783(HSD17B6)
AJU: 106976117(HSD17B8) 106984011(HSD17B2) 106986922(HSD17B6)
BTA: 515710(HSD17B2) 532422(HSD17B8) 533086(HSD17B6)
BOM: 102278674(HSD17B2) 102283510(HSD17B6) 102286352(HSD17B8)
BIU: 109559345 109572993(HSD17B2) 109576549(HSD17B8)
PHD: 102332625(HSD17B6) 102336871(HSD17B2) 102340413(HSD17B8)
CHX: 102182621(HSD17B2) 102185066(HSD17B6) 102189913(HSD17B8)
OAS: 100913161(HSD17B2) 101105400(HSD17B6) 101116612(HSD17B8)
SSC: 100154372(HSD17B8) 100312973(HSD17B2) 100620470
CFR: 102504651(HSD17B8) 102508382 102514993(HSD17B2)
BACU: 103006419(HSD17B8) 103008169(HSD17B6) 103014202(HSD17B2)
LVE: 103070446(HSD17B2) 103076064(HSD17B6) 103088201(HSD17B8)
OOR: 101278484(HSD17B6) 101284697(HSD17B2) 101287044(HSD17B8)
ECB: 100052840 100052892 100061414(HSD17B8) 100146214(HSD17B2)
EPZ: 103541177(HSD17B8) 103545357 103558215(HSD17B2) 103565330(HSD17B6)
EAI: 106832532(HSD17B2) 106832977(HSD17B6) 106834606(HSD17B8)
MYB: 102252900(HSD17B8) 102260774(HSD17B2)
MYD: 102751454(HSD17B2) 102766664(HSD17B8)
HAI: 109378375(HSD17B2) 109392392(HSD17B8)
RSS: 109450930(HSD17B8) 109452917 109453728(HSD17B2)
PALE: 102882881(HSD17B2) 102883634(HSD17B6) 102889883(HSD17B8)
LAV: 100657790 100673988(HSD17B2) 104847005(HSD17B8)
MDO: 100025234(HSD17B8) 100031815(HSD17B2)
SHR: 100914913(HSD17B8) 100921563(HSD17B2) 100931687
OAA: 100076931(HSD17B2)
GGA: 415807(HSD17B2)
MGP: 100549838(HSD17B2)
CJO: 107319415(HSD17B2)
APLA: 101792379(HSD17B2)
ACYG: 106044875(HSD17B2)
TGU: 100228039(HSD17B2) 100231423
GFR: 102039377(HSD17B2)
FAB: 101810951(HSD17B2)
PHI: 102103079(HSD17B2)
PMAJ: 107209789(HSD17B2)
CCAE: 111934744(HSD17B2)
CCW: 104691825(HSD17B2)
FPG: 101915382(HSD17B2)
FCH: 102048922(HSD17B2)
CLV: 102095570(HSD17B2)
EGZ: 104133743(HSD17B2)
AAM: 106483270(HSD17B2)
AMJ: 102567845 102571332 102574309(HSD17B2) 106737258(HSD17B8)
CMY: 102929636(HSD17B8) 102941631(HSD17B2) 102944543(HSD17B6)
CPIC: 101936532(HSD17B8) 101941193(HSD17B2)
ACS: 100564174(hsd17b6) 103281981(hsd17b8) 103282091
PVT: 110071325 110090097(HSD17B2) 110091148(HSD17B8) 110091362
PBI: 103058540(HSD17B2) 103063622
GJA: 107109831(HSD17B2) 107112070(HSD17B8) 107120904(HSD17B6)
XLA: 108700217(hsd17b8.S) 108714085(hsd17b2.L) 398882(rdh16.L)
XTR: 100135184(rdh16) 100497002(hsd17b2) 549425(hsd17b8)
NPR: 108786564(HSD17B2) 108788379(HSD17B8)
DRE: 449537(hsd17b2) 64815(hsd17b8)
SGH: 107555707 107575377(hsd17b8)
CCAR: 109101603 109101607 109111239(hsd17b8)
IPU: 108275401(Hsd17b2)
AMEX: 103023719(hsd17b8) 103032973(hsd17b2)
TRU: 101066298(hsd17b8) 101071919
LCO: 104933390(hsd17b8) 104938964(hsd17b2)
NCC: 104947942 104963938(hsd17b8)
MZE: 101480373(hsd17b8)
OLA: 101165741(hsd17b8)
XMA: 102218211
PRET: 103472946
NFU: 107392413
KMR: 108242645
CSEM: 103379612(hsd17b2) 103393879(hsd17b8)
SDU: 111233733 111239433(hsd17b8)
BPEC: 110162637(hsd17b2) 110173336(hsd17b8)
MALB: 109952509(hsd17b8) 109969153(hsd17b2)
SASA: 106561531(hsd17b2) 106569955(hsd17b8)
ELS: 105005658(hsd17b8) 105018101(hsd17b2)
SFM: 108935620(hsd17b8)
LCM: 102360275(HSD17B2) 102361445(HSD17B8)
CMK: 103191276
CIN: 100184861
DME: Dmel_CG3603(CG3603)
DSI: Dsimw501_GD16628(Dsim_GD16628)
MDE: 101889816
AAG: 5565619
AME: 552493
BIM: 100741146
BTER: 100645670
SOC: 105202077
AEC: 105146179
ACEP: 105623042
PBAR: 105425524
HST: 105192687
DQU: 106748579
LHU: 105678023
PGC: 109860596
PCF: 106786284
TCA: 103314459
DPA: 109535568
NVL: 108569323
BMOR: 101742305
PRAP: 110999152
HAW: 110379058
API: 100166278
DNX: 107168454
CLEC: 106662223
ZNE: 110831560
TUT: 107362798
CEL: CELE_F09E10.3(dhs-25) CELE_Y39A1A.11(dhs-11)
CBR: CBG18334(Cbr-dhs-11) CBG24510(Cbr-dhs-25)
EPA: 110245465
ADF: 107349767
HMG: 100199027
 » show all
Taxonomy
Reference
1  [PMID:15436478]
  Authors
SWEAT ML, SAMUELS LT, LUMRY R.
  Title
Preparation and characterization of the enzyme which converts testosterone to androstenedione.
  Journal
J Biol Chem 185:75-84 (1950)
Reference
2  [PMID:13781425]
  Authors
VILLEE CA, SPENCER JM.
  Title
Some properties of the pyridine nucleotide-specific 17 beta-hydroxy steroid dehydrogenases of guinea pig liver.
  Journal
J Biol Chem 235:3615-9 (1960)
Reference
3  [PMID:13696735]
  Authors
ENDAHL GL, KOCHAKIAN CD, HAMM D.
  Title
Separation of a triphosphopyridine nucleotide-specific from a diphosphopyridine nucleotide-specific 17 beta-hydroxy-(testosterone) dehydrogenase of guinea pig liver.
  Journal
J Biol Chem 235:2792-6 (1960)
Reference
4  [PMID:2317205]
  Authors
Ohmura M, Hara A, Nakagawa M, Sawada H.
  Title
Demonstration of 3 alpha(17 beta)-hydroxysteroid dehydrogenase distinct from 3 alpha-hydroxysteroid dehydrogenase in hamster liver.
  Journal
Biochem J 266:583-9 (1990)
Other DBs
ExplorEnz - The Enzyme Database: 1.1.1.239
IUBMB Enzyme Nomenclature: 1.1.1.239
ExPASy - ENZYME nomenclature database: 1.1.1.239
BRENDA, the Enzyme Database: 1.1.1.239
CAS: 126469-82-7

KEGG   ENZYME: 1.1.1.357Help
Entry
EC 1.1.1.357                Enzyme                                 

Name
3alpha-hydroxysteroid 3-dehydrogenase;
3alpha-hydroxysteroid dehydrogenase;
AKR1C4 (gene name);
AKR1C2 (gene name);
hsdA (gene name)
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With NAD+ or NADP+ as acceptor
BRITE hierarchy
Sysname
3alpha-hydroxysteroid:NAD(P)+ 3-oxidoreductase
Reaction(IUBMB)
a 3alpha-hydroxysteroid + NAD(P)+ = a 3-oxosteroid + NAD(P)H + H+ [RN:R10422 R10423]
Reaction(KEGG)
Substrate
3alpha-hydroxysteroid [CPD:C03072];
NAD+ [CPD:C00003];
NADP+ [CPD:C00006]
Product
3-oxosteroid [CPD:C01876];
NADH [CPD:C00004];
NADPH [CPD:C00005];
H+ [CPD:C00080]
Comment
The enzyme acts on multiple 3alpha-hydroxysteroids, such as androsterone and 5 alpha-dihydrotestosterone. The mammalian enzymes are involved in inactivation of steroid hormones, while the bacterial enzymes are involved in steroid degradation. This entry stands for enzymes whose stereo-specificity with respect to NAD+ or NADP+ is not known. [cf. EC 1.1.1.50, 3alpha-hydroxysteroid 3-dehydrogenase (Si-specific) and EC 1.1.1.213, 3alpha-hydroxysteroid 3-dehydrogenase (Re-specific)].
History
EC 1.1.1.357 created 2013
Orthology
K00037  3alpha-hydroxysteroid 3-dehydrogenase / chlordecone reductase
K00089  3alpha-hydroxysteroid 3-dehydrogenase
K00212  20alpha/3alpha-hydroxysteroid dehydrogenase / dihydrodiol dehydrogenase
K04119  aldo-keto reductase family 1 member C3
K19811  3alpha-hydroxysteroid 3-dehydrogenase
Genes
HSA: 1109(AKR1C4) 1645(AKR1C1) 1646(AKR1C2) 8644(AKR1C3)
PTR: 100607996 100612718(AKR1C3) 450274(AKR1C4)
PPS: 100986388(AKR1C3) 100986729(AKR1C1) 100987989 103783188
GGO: 101144878 101146324(AKR1C1) 101148343(AKR1C4)
PON: 100171658(AKR1C1) 100174617(AKR1C3) 100434557(AKR1C4)
NLE: 100604844(AKR1C3) 100605385(AKR1C4) 100605934(AKR1C1)
MCC: 711198(AKR1C1) 711440(AKR1C3)
MCF: 101865536(AKR1C1) 102117205(AKR1C4) 102142023(HSD17B5)
CSAB: 103237807 103237814
RRO: 104678924
CJC: 100404656(AKR1C1) 100405255 100405615(AKR1C4)
RNO: 307092(Akr1c1)
HGL: 101716553
CCAN: 109680485
CFA: 497070(AKR1C3)
FCA: 100510801(AKR1C3)
PTG: 102963188
AJU: 106988139
BTA: 100139386(20ALPHA-HSD) 282138(AKR1C4) 506594 527068 538060 617917(AKR1C3) 782884 785762
BOM: 102269337
BIU: 109568087
SSC: 733634(AKR1C1)
LVE: 103069218
EPZ: 103540778
MYB: 102255491
MYD: 102751586
TMU: 101342771
OAA: 100085065
PSS: 102446010
PVT: 110088827
XLA: 100049750(LOC100490956.L) 443571(akr1c3.L)
XTR: 105946859 779627(akr1c3)
CTES: O987_07590
 » show all
Taxonomy
Reference
1  [PMID:8172617]
  Authors
Deyashiki Y, Ogasawara A, Nakayama T, Nakanishi M, Miyabe Y, Sato K, Hara A
  Title
Molecular cloning of two human liver 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase isoenzymes that are identical with chlordecone reductase and bile-acid binder.
  Journal
Biochem J 299 ( Pt 2):545-52 (1994)
  Sequence
[hsa:1645 1109]
Reference
2  [PMID:7650035]
  Authors
Khanna M, Qin KN, Wang RW, Cheng KC
  Title
Substrate specificity, gene structure, and tissue-specific distribution of multiple human 3 alpha-hydroxysteroid dehydrogenases.
  Journal
J Biol Chem 270:20162-8 (1995)
DOI:10.1074/jbc.270.34.20162
  Sequence
[hsa:8644]
Reference
3  [PMID:8944761]
  Authors
Oppermann UC, Maser E
  Title
Characterization of a 3 alpha-hydroxysteroid dehydrogenase/carbonyl reductase from the gram-negative bacterium Comamonas testosteroni.
  Journal
Eur J Biochem 241:744-9 (1996)
DOI:10.1111/j.1432-1033.1996.00744.x
  Sequence
Reference
4  [PMID:9812981]
  Authors
Mobus E, Maser E
  Title
Molecular cloning, overexpression, and characterization of steroid-inducible 3alpha-hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni. A novel member of the short-chain dehydrogenase/reductase superfamily.
  Journal
J Biol Chem 273:30888-96 (1998)
DOI:10.1074/jbc.273.47.30888
  Sequence
Reference
5  [PMID:11514561]
  Authors
Nahoum V, Gangloff A, Legrand P, Zhu DW, Cantin L, Zhorov BS, Luu-The V, Labrie F, Breton R, Lin SX
  Title
Structure of the human 3alpha-hydroxysteroid dehydrogenase type 3 in complex with testosterone and NADP at 1.25-A resolution.
  Journal
J Biol Chem 276:42091-8 (2001)
DOI:10.1074/jbc.M105610200
  Sequence
[hsa:1646]
Other DBs
ExplorEnz - The Enzyme Database: 1.1.1.357
IUBMB Enzyme Nomenclature: 1.1.1.357
ExPASy - ENZYME nomenclature database: 1.1.1.357
BRENDA, the Enzyme Database: 1.1.1.357

KEGG   ENZYME: 1.1.1.64Help
Entry
EC 1.1.1.64                 Enzyme                                 

Name
testosterone 17beta-dehydrogenase (NADP+);
17-ketoreductase;
NADP-dependent testosterone-17beta-oxidoreductase;
testosterone 17beta-dehydrogenase (NADP)
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With NAD+ or NADP+ as acceptor
BRITE hierarchy
Sysname
17beta-hydroxysteroid:NADP+ 17-oxidoreductase
Reaction(IUBMB)
testosterone + NADP+ = androstenedione + NADPH + H+ [RN:R01838]
Reaction(KEGG)
Substrate
testosterone [CPD:C00535];
NADP+ [CPD:C00006]
Product
androstenedione [CPD:C00280];
NADPH [CPD:C00005];
H+ [CPD:C00080]
Comment
Also oxidizes 3-hydroxyhexobarbital to 3-oxohexobarbital.
History
EC 1.1.1.64 created 1965
Pathway
ec00140  Steroid hormone biosynthesis
ec01100  Metabolic pathways
Orthology
K10207  testosterone 17beta-dehydrogenase (NADP+)
Genes
HSA: 3293(HSD17B3)
PTR: 742116(HSD17B3)
PPS: 100972788(HSD17B3)
GGO: 101137034(HSD17B3)
PON: 100433175(HSD17B3)
NLE: 100584015(HSD17B3)
MCC: 709843(HSD17B3)
MCF: 102126699(HSD17B3)
CSAB: 103219820(HSD17B3)
RRO: 104658189(HSD17B3)
RBB: 108529285(HSD17B3)
CJC: 100414334(HSD17B3)
SBQ: 101030368(HSD17B3)
MMU: 15487(Hsd17b3)
RNO: 117182(Hsd17b3)
CGE: 100767644(Hsd17b3)
NGI: 103751616(Hsd17b3)
HGL: 101712135(Hsd17b3)
CCAN: 109683204(Hsd17b3)
OCU: 100346075(HSD17B3)
TUP: 102477731(HSD17B3)
CFA: 100856708(HSD17B3)
AML: 100468038(HSD17B3)
UMR: 103682216(HSD17B3)
ORO: 101379154(HSD17B3)
FCA: 101085324(HSD17B3)
PTG: 102972770(HSD17B3)
AJU: 106971466(HSD17B3)
BTA: 616934(HSD17B3)
BOM: 102284785(HSD17B3)
BIU: 109562717(HSD17B3)
PHD: 102341291(HSD17B3)
CHX: 102188501(HSD17B3)
OAS: 101111157(HSD17B3)
SSC: 100513224(HSD17B3)
CFR: 102514822(HSD17B3)
CDK: 105084686(HSD17B3)
BACU: 103006772(HSD17B3)
LVE: 103087691(HSD17B3)
OOR: 101283794(HSD17B3)
ECB: 100062795(HSD17B3)
EPZ: 103556464
EAI: 106841117(HSD17B3)
MYB: 102256012(HSD17B3)
MYD: 102755784(HSD17B3)
HAI: 109371900(HSD17B3)
RSS: 109434745(HSD17B3)
PALE: 102883847(HSD17B3)
LAV: 100661701(HSD17B3)
TMU: 101353253
MDO: 100014335(HSD17B3)
SHR: 100935109(HSD17B3)
GGA: 427474(HSD17B3)
CJO: 107306280(HSD17B3)
APLA: 101797428(HSD17B3)
ACYG: 106047350(HSD17B3)
GFR: 106631948(HSD17B3)
FAB: 107604273(HSD17B3)
PMAJ: 107215831(HSD17B3)
CCAE: 111941803(HSD17B3)
CCW: 109145194(HSD17B3)
FPG: 101920192(HSD17B3)
FCH: 102057185(HSD17B3)
CLV: 102098536(HSD17B3)
EGZ: 104125984(HSD17B3)
AAM: 106484155(HSD17B3) 106490054
ASN: 102387576(HSD17B3)
AMJ: 102576225(HSD17B3)
PSS: 102451036(HSD17B3)
CMY: 102936343(HSD17B3)
CPIC: 101953074(HSD17B3)
ACS: 100561157(hsd17b3)
PVT: 110084176(HSD17B3)
PBI: 103062335(HSD17B3)
GJA: 107111659(HSD17B3)
XLA: 108714716(hsd17b3.L)
XTR: 101730254(hsd17b3)
NPR: 108788141(HSD17B3)
DRE: 393335(hsd17b3)
CCAR: 109095009 109102469(hsd17b3)
IPU: 108265426(hsd17b3)
AMEX: 103031519(hsd17b3)
TRU: 101070933(hsd17b3)
LCO: 104920662(hsd17b3)
NCC: 104963114(hsd17b3)
MZE: 101468772(hsd17b3)
OLA: 100125485(hsd17b3)
XMA: 102216624(hsd17b3)
PRET: 103470152(hsd17b3)
NFU: 107394092(hsd17b3)
KMR: 108244792(hsd17b3)
CSEM: 103398902
LCF: 108882635
SDU: 111236157(hsd17b3)
BPEC: 110167040(hsd17b3)
MALB: 109956598(hsd17b3)
SASA: 106580550(DHB3) 106585149(hsd17b3)
ELS: 105014100(hsd17b3)
SFM: 108938393(hsd17b3)
LCM: 102364217(HSD17B3)
CMK: 103182831(hsd17b3)
 » show all
Taxonomy
Reference
1  [PMID:13696735]
  Authors
ENDAHL GL, KOCHAKIAN CD, HAMM D.
  Title
Separation of a triphosphopyridine nucleotide-specific from a diphosphopyridine nucleotide-specific 17 beta-hydroxy-(testosterone) dehydrogenase of guinea pig liver.
  Journal
J Biol Chem 235:2792-6 (1960)
Reference
2  [PMID:15436478]
  Authors
SWEAT ML, SAMUELS LT, LUMRY R.
  Title
Preparation and characterization of the enzyme which converts testosterone to androstenedione.
  Journal
J Biol Chem 185:75-84 (1950)
Reference
3  [PMID:13781425]
  Authors
VILLEE CA, SPENCER JM.
  Title
Some properties of the pyridine nucleotide-specific 17 beta-hydroxy steroid dehydrogenases of guinea pig liver.
  Journal
J Biol Chem 235:3615-9 (1960)
Other DBs
ExplorEnz - The Enzyme Database: 1.1.1.64
IUBMB Enzyme Nomenclature: 1.1.1.64
ExPASy - ENZYME nomenclature database: 1.1.1.64
BRENDA, the Enzyme Database: 1.1.1.64
CAS: 9028-63-1

KEGG   ENZYME: 1.3.1.20Help
Entry
EC 1.3.1.20                 Enzyme                                 

Name
trans-1,2-dihydrobenzene-1,2-diol dehydrogenase;
dihydrodiol dehydrogenase
Class
Oxidoreductases;
Acting on the CH-CH group of donors;
With NAD+ or NADP+ as acceptor
BRITE hierarchy
Sysname
trans-1,2-dihydrobenzene-1,2-diol:NADP+ oxidoreductase
Reaction(IUBMB)
trans-1,2-dihydrobenzene-1,2-diol + NADP+ = catechol + NADPH + H+ [RN:R00814]
Reaction(KEGG)
R00814;
(other) R07015 R09420
Show
Substrate
trans-1,2-dihydrobenzene-1,2-diol [CPD:C04221];
NADP+ [CPD:C00006]
Product
catechol [CPD:C00090];
NADPH [CPD:C00005];
H+ [CPD:C00080]
History
EC 1.3.1.20 created 1972
Pathway
ec00980  Metabolism of xenobiotics by cytochrome P450
Orthology
K00078  dihydrodiol dehydrogenase / D-xylose 1-dehydrogenase (NADP)
K00212  20alpha/3alpha-hydroxysteroid dehydrogenase / dihydrodiol dehydrogenase
Genes
HSA: 1645(AKR1C1) 27294(DHDH)
PTR: 100607996 456194(DHDH)
PPS: 100986729(AKR1C1) 100991467(DHDH)
GGO: 101146324(AKR1C1) 101152398(DHDH)
PON: 100171658(AKR1C1) 100174691(DHDH)
NLE: 100591778(DHDH) 100605934(AKR1C1)
MCC: 711198(AKR1C1) 718930(DHDH)
MCF: 101865536(AKR1C1) 102133381(DHDH)
CSAB: 103235003(DHDH) 103237807
RRO: 104666542(DHDH) 104678924
RBB: 108523635(DHDH) 108532991
CJC: 100390604(DHDH) 100404656(AKR1C1)
SBQ: 101042532 101049549(DHDH)
MMU: 71755(Dhdh)
RNO: 307092(Akr1c1) 691002(Dhdh)
CGE: 100753544(Dhdh)
NGI: 103743638(Dhdh)
HGL: 101713222(Dhdh) 101716553
CCAN: 109680485 109682683(Dhdh)
OCU: 100008610(DHDH)
TUP: 102470508(DHDH)
CFA: 403786(DHDH)
AML: 100477136(DHDH)
UMR: 103657108(DHDH)
ORO: 101371357(DHDH)
FCA: 101101272(DHDH)
PTG: 102948867(DHDH)
AJU: 106988698(DHDH)
BTA: 617564(DHDH)
BOM: 102280401(DHDH)
BIU: 109571974 109572213(DHDH)
PHD: 102323268(DHDH)
CHX: 102188075(DHDH)
OAS: 101103175(DHDH)
SSC: 397337(DHDH)
CFR: 102512639(DHDH)
CDK: 105102891(DHDH)
BACU: 103008204(DHDH)
ECB: 100051521(DHDH) 100070570
EPZ: 103540778 103553311(DHDH)
EAI: 106838267(DHDH)
MYB: 102262437(DHDH)
MYD: 102770117(DHDH)
HAI: 109391066(DHDH)
RSS: 109452566(DHDH)
PALE: 102885391(DHDH)
LAV: 100660549(DHDH)
TMU: 101355202
MDO: 100030403(DHDH)
SHR: 111720213(DHDH)
GGA: 777348(DHDH)
MGP: 104916162(DHDH)
CJO: 107325868(DHDH)
PHI: 102104923(DHDH)
PMAJ: 107199051(DHDH)
CCAE: 111946095(DHDH)
ASN: 102376323(DHDH)
AMJ: 102574630(DHDH)
PSS: 102447655(DHDH)
CMY: 102931206
XLA: 108697264 444539(dhdh)
XTR: 100145807(dhdh) 448579(dhdh)
DRE: 406433(dhdhl) 449558(zgc:101723)
SGH: 107553352 107595342(dhdh)
IPU: 100528487(dhdh)
MZE: 101466663
NFU: 107381267(dhdh) 107381268
MALB: 109955837(dhdh)
SFM: 108930140
LCM: 102353287(DHDH)
CMK: 103189533(dhdh)
CIN: 100186038
DME: Dmel_CG13280(CG13280) Dmel_CG3597(CG3597) Dmel_CG3609(CG3609)
DER: 6541604
DPE: 6589434
DSI: Dsimw501_GD11964(Dsim_GD11964) Dsimw501_GD22839(Dsim_GD22839) Dsimw501_GD22840(Dsim_GD22840)
DWI: 6641897
MDE: 101900891
AAG: 5572674
AME: 412231
BIM: 100740559
BTER: 100649548
SOC: 105208047
AEC: 105154186
ACEP: 105622679
HST: 105186645
DQU: 106741522
LHU: 105671479
PGC: 109857477
PCF: 106785709
NVI: 100117805
MDL: 103578346
NVL: 108560837
ZNE: 110838823
CRG: 105323672
EPA: 110244148
ADF: 107341873
HMG: 100210586
SPAR: SPRG_05860
 » show all
Taxonomy
Reference
1  [PMID:13651190]
  Authors
AYENGAR PK, HAYAISHI O, NAKAJIMA M, TOMIDA I.
  Title
Enzymic aromatization of 3,5-cyclohexadiene-1,2-diol.
  Journal
Biochim Biophys Acta 33:111-9 (1959)
DOI:10.1016/0006-3002(59)90504-9
Other DBs
ExplorEnz - The Enzyme Database: 1.3.1.20
IUBMB Enzyme Nomenclature: 1.3.1.20
ExPASy - ENZYME nomenclature database: 1.3.1.20
BRENDA, the Enzyme Database: 1.3.1.20
CAS: 37255-32-6

DBGET integrated database retrieval system