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Information on EC 1.1.1.239 - 3alpha(17beta)-hydroxysteroid dehydrogenase (NAD+)
for references in articles please use BRENDA:EC1.1.1.239
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.239 3alpha(17beta)-hydroxysteroid dehydrogenase (NAD+)
IUBMB Comments
Also acts on other 17β-hydroxysteroids and on the 3α-hydroxy group of pregnanes and bile acids. Different from EC 1.1.1.50 3α-hydroxysteroid dehydrogenase (Si-specific) or EC 1.1.1.213 3α-hydroxysteroid dehydrogenase (Re-specific).
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 1.1.1.239
- androgen
- estradiol
-
steroidogenic
- akr1c3
- androstenedione
- prostate
- 3beta-hsd
-
3beta-hydroxysteroid
- estrone
- aromatase
-
steroidogenesis
-
5alpha-reductase
- dehydroepiandrosterone
- leydig
- 3alpha-hsds
-
3alpha-hydroxysteroid
- p450scc
- 5alpha-dihydrotestosterone
-
cochliobolus
-
4-dione
- androsterone
- lunatus
- delta5-3beta-hsd
-
intracrine
- coumestrol
-
5alpha-dht
- pseudohermaphroditism
- p450arom
- 4-androstene-3,17-dione
- medicine
showSynonyms
17beta-hsd, aldo-keto reductase 1c3, type 5 17beta-hsd, 17beta-hydroxysteroid dehydrogenase type 5, 17-ketoreductase, type 3 17beta-hydroxysteroid dehydrogenase, type 5 17beta-hydroxysteroid dehydrogenase, type 2 3alpha-hsd, akr1c28, testosterone 17beta-dehydrogenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
17-ketoreductase
-
-
-
-
17beta-HSD
-
-
-
-
3,17beta-HSD
3,17beta-hydroxysteroid dehydrogenase
3alpha(17beta)-HSD
-
-
-
-
AKR1C3
aldo-keto reductase 1C3
dehydrogenase, 3alpha,17beta-hydroxy steroid
-
-
-
-
EC 1.1.1.63
-
-
formerly
-
NAD+-dependent 3alpha(17beta)-hydroxysteroid dehydrogenase
-
NAD+-dependent 3beta(17beta)-hydroxysteroid dehydrogenase
-
PGER6
type 2 3alpha-hxdroxysteroid dehydrogenase/type 5 17beta-hydroxysteroid dehydrogenase
-
-
type 2 3alppha-hydroxysteroid dehydrogenase/type 5 17beta-hydroxysteroid dehydrogenase
additional information
AKR1C3
-
multi-functional enzyme that possesses 3alpha-, 17beta-, 20alpha-hydroxysteroid dehydrogenase, as well as prostaglandine F synthase activities and catalyzes androgen, estrogen, progestin and prostaglandin metabolism. It is a member of the aldo-keto reductase superfamily.
type 2 3alppha-hydroxysteroid dehydrogenase/type 5 17beta-hydroxysteroid dehydrogenase
-
-
type 2 3alppha-hydroxysteroid dehydrogenase/type 5 17beta-hydroxysteroid dehydrogenase
-
-
additional information
cf. EC 1.1.1.218, morphine 6-dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
testosterone + NAD+ = androstenedione + NADH + H+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
3alpha(or 17beta)-hydroxysteroid:NAD+ oxidoreductase
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).
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CAS REGISTRY NUMBER
COMMENTARY
126469-82-7
-
9028-62-0
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(R)-1,2,3,4-tetrahydro-1-naphthol + NAD+
3,4-dihydronaphthalen-1(2H)-one + NADH + H+
Substrates: i.e. (R)-tetralol
Products: -
Products: -
?
(S)-1,2,3,4-tetrahydro-1-naphthol + NADP+
3,4-dihydronaphthalen-1(2H)-one + NADPH + H+
Substrates: i.e. (S)-tetralol
Products: -
Products: -
?
(S)-alpha-tetralol + NADP+
alpha-tetralone + NADPH + H+
Substrates: -
Products: -
Products: -
?
(S)-camphorquinone + NADPH + H+
? + NADP+
Substrates: -
Products: -
Products: -
?
1-acenaphthenol + NAD+
acenaphthylen-1(2H)-one + NADH + H+
Substrates: -
Products: -
Products: -
?
1-phenyl-1,2-propanedione + NADH + H+
? + NAD+
Substrates: -
Products: -
Products: -
?
11alpha-hydroxytestosterone + NAD+
11alpha-hydroxyandrost-4-ene-3,17-dione + NADH
-
Substrates: 156% velocity compared to testosterone
Products: -
Products: -
r
15alpha-hydroxytestosterone + NAD+
15alpha-hydroxyandrost-4-ene-3,17-dione + NADH
-
Substrates: 131% velocity compared to testosterone
Products: -
Products: -
r
16-oxoestrone + NADH + H+
? + NAD+
Substrates: -
Products: -
Products: -
?
17beta-estradiol + NAD+
? + NADH + H+
Substrates: -
Products: -
Products: -
r
17beta-hydroxy-1alpha-methyl-5alpha-androstan-3-one + NAD+
1alpha-methyl-5alpha-androstane-3,17-dione + NADH
-
Substrates: 192% velocity compared to testosterone
Products: -
Products: -
r
17beta-hydroxy-5beta-androstan-3-one + NAD+
5beta-androstane-3,17-dione + NADH
-
Substrates: 86% velocity compared to testosterone
Products: -
Products: -
r
2,3-butanedione + NADH + H+
? + NAD+
Substrates: -
Products: -
Products: -
?
2-[(2-bromoethyl)(2-[[(2-hydroxyethyl)amino]methyl]-4,6-dinitrophenyl)amino]ethyl methanesulfonate + 2 NADH + 2 H+
2-[(2-bromoethyl)[4-(hydroxyamino)-2-[[(2-hydroxyethyl)amino]methyl]-6-nitrophenyl]amino]ethyl methanesulfonate + 2 NAD+ + H2O
-
Substrates: i.e. PR-104A, phosphate ester prodrug designed to exploit tumor hypoxia
Products: i.e. PR-104H, enzyme acts as nitroreductase for activation of PR-104A
Products: i.e. PR-104H, enzyme acts as nitroreductase for activation of PR-104A
?
20alpha-hydroxyprogesterone + NADH + H+
? + NAD+
Substrates: -
Products: -
Products: -
?
3alpha-hydroxyprogesterone + NADH + H+
? + NAD+
Substrates: -
Products: -
Products: -
?
3beta-hydroxy-5alpha-androstane-17-one + NAD+
5alpha-androstane-3,17-dione + NADH
-
Substrates: 75% velocity compared to testosterone
Products: -
Products: -
r
3beta-hydroxyprogesterone + NADH + H+
? + NAD+
Substrates: -
Products: -
Products: -
?
4-androstenedione + NADPH + H+
testosterone + NADP+
-
Substrates: -
Products: -
Products: -
?
4-oxo-2-nonenal + NADPH + H+
4-hydroxy-2-nonenal + NADP+
Substrates: -
Products: -
Products: -
?
4-pregnen-3alpha-ol-2-one + NAD+
4-pregnen-3,20-dione + NADH + H+
Substrates: -
Products: -
Products: -
r
4-pregnen-3alpha-ol-20-one + NAD+
4-pregnen-3,20-dione + NADH + H+
Substrates: -
Products: -
Products: -
?
5alpha-androstan-17beta-ol-3-one + NAD+
5alpha-androstan-3,17-dione + NADH + H+
Substrates: -
Products: -
Products: -
?
5alpha-androstan-3alpha,17beta-diol + NAD+
5alpha-androstan-3alpha-ol-17-one + NADH
-
Substrates: -
Products: -
Products: -
?
5alpha-androstan-3beta-ol-17-one + NAD+
5alpha-androstan-3,17-dione + NADH + H+
Substrates: -
Products: -
Products: -
?
5alpha-androstane-17beta-ol-3-one + NAD+
5alpha-androstan-3,17-dione + NADH + H+
Substrates: -
Products: -
Products: -
r
5alpha-androstane-3,17-dione + NADH + H+
? + NAD+
Substrates: -
Products: -
Products: -
?
5alpha-androstane-3alpha,17beta-diol + NAD+
?
Substrates: -
Products: -
Products: -
?
5alpha-androstane-3beta,17beta-diol + NAD+
?
Substrates: -
Products: -
Products: -
?
5alpha-dihydrotestosterone + NAD+
androstandione + NADH + H+
-
Substrates: -
Products: -
Products: -
r
5alpha-pregnan-20alpha-ol-3-one + NAD+
5alpha-pregnan-3,20-dione + NADH + H+
Substrates: -
Products: -
Products: -
?
5alpha-pregnan-3,21alpha-diol-20-one + NAD+
5alpha-pregnan-21-ol-3,20-dione + NADH
-
Substrates: -
Products: -
Products: -
?
5alpha-pregnan-3beta-ol-20-one + NAD+
5alpha-pregnan-3,20-dione + NADH + H+
Substrates: -
Products: -
Products: -
?
5beta-androstan-17beta-ol-3-one + NAD+
5beta-androstan-3,17-dione + NADH
-
Substrates: -
Products: -
Products: -
?
5beta-androstan-3alpha,17beta-diol + NAD+
5beta-androstan-3alpha-ol-17-one + NADH
-
Substrates: -
Products: -
Products: -
?
5beta-androstane-17beta-ol-3-one + NAD+
5beta-androstan-3,17-dione + NADH + H+
Substrates: -
Products: -
Products: -
r
5beta-androstane-3,17-dione + NADH + H+
? + NAD+
Substrates: -
Products: -
Products: -
?
5beta-androstane-3alpha,17beta-diol + NAD+
5beta-androstane-3alpha-ol-17-one + NADH
-
Substrates: 57% velocity compared to testosterone
Products: -
Products: -
r
5beta-androstane-3alpha,17beta-diol + NAD+
?
Substrates: -
Products: -
Products: -
?
5beta-androstane-3beta,17beta-diol + NAD+
?
Substrates: -
Products: -
Products: -
?
5beta-pregnan-20alpha-ol-3-one + NAD+
5beta-pregnan-3,20-dione + NADH + H+
Substrates: -
Products: -
Products: -
?
5beta-pregnan-3alpha,21-diol-20-one + NAD+
5beta-pregnan-21-ol-3,20-dione + NADH
-
Substrates: -
Products: -
Products: -
?
5beta-pregnan-3alpha-ol-20-one + NAD+
5beta-pregnan-3,20-dione + NADH
-
Substrates: -
Products: -
Products: -
?
5beta-pregnan-3beta,21-diol-20-one + NAD+
?
Substrates: -
Products: -
Products: -
?
5beta-pregnan-3beta-ol-20-one + NAD+
5beta-pregnan-3,20-dione + NADH + H+
Substrates: -
Products: -
Products: -
?
6-tert-butyl-2,3-epoxy-4-hydroxy-5-cyclohexen-1-one + NADH + H+
? + NAD+
Substrates: -
Products: -
Products: -
?
6beta-hydroxytestosterone + NAD+
6beta-hydroxyandrost-4-ene-3,17-dione + NADH
-
Substrates: 84% velocity compared to testosterone
Products: -
Products: -
r
9,10-phenanthrenequinone + NADH + H+
? + NAD+
Substrates: -
Products: -
Products: -
?
alpha-3-hydroxyhexobarbital + NAD+
?
Substrates: -
Products: -
Products: -
?
alpha-tetralone + NADH + H+
? + NAD+
Substrates: -
Products: -
Products: -
?
androst-4-ene-3beta,17beta-diol + NAD+
androst-4-ene-3beta-ol-17-one + NADH
-
Substrates: 75% velocity compared to testosterone
Products: -
Products: -
r
androst-4-ene-3beta,17beta-diol + NAD+
androst-4-ene-3beta-ol-17-one + NADH + H+
-
Substrates: -
Products: -
Products: -
?
androst-5-ene-3beta,17beta-diol + NAD+
androst-5-ene-3beta-ol-17-one + NADH
-
Substrates: 33% velocity compared to testosterone
Products: -
Products: -
r
benzene dihydrodiol + NAD+
?
Substrates: -
Products: -
Products: -
?
benzene dihydrodiol + NAD+
? + NADH + H+
Substrates: -
Products: -
Products: -
?
beta-3-hydroxyhexobarbital + NAD+
?
Substrates: -
Products: -
Products: -
?
dehydroepiandrosterone + NAD+
? + NADH + H+
Substrates: -
Products: -
Products: -
?
farnesol + NAD+
? + NADH + H+
Substrates: -
Products: -
Products: -
?
farnesol + NAD+
farnesal + NADH + H+
Substrates: -
Products: -
Products: -
?
geraniol + NAD+
? + NADH + H+
Substrates: -
Products: -
Products: -
?
geraniol + NAD+
geranial + NADH + H+
Substrates: -
Products: -
Products: -
?
geranylgeraniol + NAD+
?
Substrates: -
Products: -
Products: -
?
geranylgeraniol + NAD+
? + NADH + H+
Substrates: -
Products: -
Products: -
?
geranylgeraniol + NAD+
geranylgeranial + NADH + H+
Substrates: -
Products: -
Products: -
?
glycochenodeoxycholic acid + NAD+
7alpha-hydroxy-3-oxo-5-beta-cholanoyl glycine + NADH
-
Substrates: -
Products: -
Products: -
?
glycolithocholic acid + NAD+
3-oxo-5beta-cholanoyl glycine + NADH
-
Substrates: -
Products: -
Products: -
?
isatin + NADH + H+
? + NAD+
Substrates: -
Products: -
Products: -
?
lithocholic acid
5beta-cholan-3-one-24-oic acid + NADH + H+
Substrates: -
Products: -
Products: -
?
lithocholic acid + NAD+
5-beta-cholan-3-one-24-oic acid + NADH + H+
Substrates: -
Products: -
Products: -
?
lithocholic acid + NAD+
5beta-cholan-3-one-24-oic acid + NADH
-
Substrates: -
Products: -
Products: -
?
lithocholic acid + NAD+
5beta-cholan-3-one-24-oic acid + NADH + H+
Substrates: -
Products: -
Products: -
?
morphine + NAD+
morphinone + NADH + H+
Substrates: reaction of EC 1.1.1.218
Products: -
Products: -
?
naphthalene dihydrodiol + NAD+
? + NADH + H+
Substrates: -
Products: -
Products: -
?
progesterone + NADPH + H+
20alpha-hydroxyprogesterone + NADP+
-
Substrates: -
Products: -
Products: -
?
prostaglandin D2 + NADPH + H+
9alpha,11beta-prostaglandin F2 + NADP+
-
Substrates: -
Products: -
Products: -
?
pyridine-3-aldehyde + NADH + H+
? + NAD+
Substrates: -
Products: -
Products: -
?
testosterone + NADP+
androst-4-ene-3,17-dione + NADPH + H+
-
Substrates: NADP is 3fold less efficient as cofactor
Products: -
Products: -
r
testosterone + NADP+
androstenedione + NADPH + H+
Substrates: -
Products: -
Products: -
r
trans-benzene dihydrodiol + NAD+
?
Substrates: -
Products: -
Products: -
?
(S)-1,2,3,4-tetrahydro-1-naphthol + NAD+
3,4-dihydronaphthalen-1(2H)-one + NADH + H+
Substrates: i.e. (S)-tetralol
Products: -
Products: -
r
(S)-1,2,3,4-tetrahydro-1-naphthol + NAD+
3,4-dihydronaphthalen-1(2H)-one + NADH + H+
Substrates: i.e. (S)-tetralol
Products: -
Products: -
?
(S)-1,2,3,4-tetrahydro-1-naphthol + NAD+
3,4-dihydronaphthalen-1(2H)-one + NADH + H+
Substrates: i.e. (S)-tetralol
Products: -
Products: -
?
(S)-1-indanol + NAD+
2,3-dihydro-1H-inden-1-one + NADH + H+
Substrates: -
Products: -
Products: -
?
(S)-1-indanol + NAD+
2,3-dihydro-1H-inden-1-one + NADH + H+
Substrates: -
Products: -
Products: -
?
(S)-camphorquinone + NADH + H+
? + NAD+
Substrates: -
Products: -
Products: -
?
(S)-camphorquinone + NADH + H+
? + NAD+
Substrates: -
Products: -
Products: -
?
11beta-hydroxytestosterone + NAD+
11beta-hydroxyandrost-4-ene-3,17-dione + NADH
-
Substrates: 136% velocity compared to testosterone
Products: -
Products: -
r
11beta-hydroxytestosterone + NAD+
11beta-hydroxyandrost-4-ene-3,17-dione + NADH
-
Substrates: -
Products: -
Products: -
r
11beta-hydroxytestosterone + NAD+
11beta-hydroxyandrost-4-ene-3,17-dione + NADH
-
Substrates: 76% of testosterone oxidation rate
Products: -
Products: -
r
17beta-estradiol + NAD+
estrone + NADH + H+
Substrates: -
Products: -
Products: -
?
17beta-estradiol + NAD+
estrone + NADH + H+
Substrates: -
Products: -
Products: -
?
2-cyclohexen-1-ol + NAD+
2-cyclohexen-1-one + NADH + H+
Substrates: -
Products: -
Products: -
?
2-cyclohexen-1-ol + NAD+
2-cyclohexen-1-one + NADH + H+
Substrates: -
Products: -
Products: -
?
5alpha-androstan-3alpha-ol-17-one + NAD+
5alpha-androstan-3,17-dione + NADH + H+
Substrates: -
Products: -
Products: -
?
5alpha-androstan-3alpha-ol-17-one + NAD+
5alpha-androstan-3,17-dione + NADH + H+
Substrates: -
Products: -
Products: -
r
5alpha-androstan-3alpha-ol-17-one + NAD+
5alpha-androstan-3,17-dione + NADH + H+
Substrates: -
Products: -
Products: -
?
5alpha-androstane-3alpha,17beta-diol + NAD+
5alpha-androstane-3alpha-ol-17-one + NADH
-
Substrates: 72% velocity compared to testosterone
Products: -
Products: -
r
5alpha-androstane-3alpha,17beta-diol + NAD+
5alpha-androstane-3alpha-ol-17-one + NADH
-
Substrates: 204% velocity compared to testosterone
Products: -
Products: -
r
5alpha-androstane-3alpha,17beta-diol + NAD+
? + NADH + H+
Substrates: -
Products: -
Products: -
r
5alpha-androstane-3alpha,17beta-diol + NAD+
? + NADH + H+
Substrates: -
Products: -
Products: -
?
5alpha-androstane-3beta,17beta-diol + NAD+
5alpha-androstane-3beta-ol-17-one + NADH
-
Substrates: 72% velocity compared to testosterone
Products: -
Products: -
r
5alpha-androstane-3beta,17beta-diol + NAD+
5alpha-androstane-3beta-ol-17-one + NADH
-
Substrates: 17% velocity compared to testosterone
Products: -
Products: -
r
5alpha-dihydrotestosterone + NAD+
5alpha-androstane-3,17-dione + NADH + H+
-
Substrates: 133% velocity compared to testosterone
Products: -
Products: -
r
5alpha-dihydrotestosterone + NAD+
5alpha-androstane-3,17-dione + NADH + H+
Substrates: -
Products: -
Products: -
?
5alpha-dihydrotestosterone + NAD+
androstanedione + NADH + H+
-
Substrates: -
Products: -
Products: -
r
5alpha-dihydrotestosterone + NAD+
androstanedione + NADH + H+
-
Substrates: 119% initial velocity compared to testosterone
Products: -
Products: -
r
5alpha-pregnan-3alpha-ol-20-one + NAD+
5alpha-pregnan-3,20-dione + NADH + H+
Substrates: -
Products: -
Products: -
?
5alpha-pregnan-3alpha-ol-20-one + NAD+
5alpha-pregnan-3,20-dione + NADH + H+
Substrates: -
Products: -
Products: -
r
5alpha-pregnan-3alpha-ol-20-one + NAD+
5alpha-pregnan-3,20-dione + NADH + H+
Substrates: -
Products: -
Products: -
?
5beta-androstan-17beta-ol-3-one + NAD+
5beta-androstan-3,17-dione + NADH + H+
Substrates: -
Products: -
Products: -
?
5beta-androstan-17beta-ol-3-one + NAD+
5beta-androstan-3,17-dione + NADH + H+
Substrates: -
Products: -
Products: -
?
5beta-androstan-3alpha-ol-17-one + NAD+
5beta-androstan-3,17-dione + NADH + H+
Substrates: -
Products: -
Products: -
?
5beta-androstan-3alpha-ol-17-one + NAD+
5beta-androstan-3,17-dione + NADH + H+
Substrates: -
Products: -
Products: -
?
5beta-androstan-3alpha-ol-17-one + NAD+
5beta-androstan-3,17-dione + NADH + H+
Substrates: -
Products: -
Products: -
r
5beta-androstane-3alpha,17beta-diol + NAD+
? + NADH + H+
Substrates: -
Products: -
Products: -
r
5beta-androstane-3alpha,17beta-diol + NAD+
? + NADH + H+
Substrates: -
Products: -
Products: -
?
5beta-dihydrotestosterone + NAD+
androstanedione + NADH + H+
Substrates: -
Products: -
Products: -
?
5beta-dihydrotestosterone + NAD+
androstanedione + NADH + H+
-
Substrates: 50% initial velocity compared to testosterone
Products: -
Products: -
r
5beta-pregnan-3alpha-ol-20-one + NAD+
5beta-pregnan-3,20-dione + NADH + H+
Substrates: -
Products: -
Products: -
?
5beta-pregnan-3alpha-ol-20-one + NAD+
5beta-pregnan-3,20-dione + NADH + H+
Substrates: -
Products: -
Products: -
r
5beta-pregnan-3alpha-ol-20-one + NAD+
5beta-pregnan-3,20-dione + NADH + H+
Substrates: -
Products: -
Products: -
?
beta-ionol + NAD+
(3E)-4-(2,6,6-trimethylcyclohex-1-en-1-yl)but-3-en-2-one + NADH + H+
Substrates: -
Products: -
Products: -
?
beta-ionol + NAD+
(3E)-4-(2,6,6-trimethylcyclohex-1-en-1-yl)but-3-en-2-one + NADH + H+
Substrates: -
Products: -
Products: -
?
daunorubicin + NADPH + H+
daunorubicinol + NADP+
Substrates: inactivation of the anticancer drug
Products: -
Products: -
r
daunorubicin + NADPH + H+
daunorubicinol + NADP+
Substrates: the enzyme reduces daunorubicin to its corresponding alcohol daunorubicinol using NADPH as the coenzyme
Products: -
Products: -
r
estradiol + NAD+
estrone + NADH
-
Substrates: 72% velocity compared to testosterone oxidation
Products: -
Products: -
r
estradiol + NAD+
estrone + NADH
-
Substrates: 46% of testosterone oxidation rate
Products: -
Products: -
r
estradiol + NAD+
estrone + NADH
-
Substrates: 15% velocity compared to testosterone oxidation
Products: -
Products: -
r
testosterone + NAD+
4-androstenedione + NADH + H+
Substrates: -
Products: -
Products: -
?
testosterone + NAD+
4-androstenedione + NADH + H+
Substrates: -
Products: -
Products: -
?
testosterone + NAD+
androst-4-ene-3,17-dione + NADH + H+
-
Substrates: -
Products: -
Products: -
?
testosterone + NAD+
androst-4-ene-3,17-dione + NADH + H+
-
Substrates: -
Products: -
Products: -
?
testosterone + NAD+
androst-4-ene-3,17-dione + NADH + H+
-
Substrates: -
Products: -
Products: -
?
testosterone + NAD+
androst-4-ene-3,17-dione + NADH + H+
-
Substrates: -
Products: -
Products: -
?
testosterone + NAD+
androst-4-ene-3,17-dione + NADH + H+
-
Substrates: -
Products: -
Products: -
r
testosterone + NAD+
androst-4-ene-3,17-dione + NADH + H+
-
Substrates: -
Products: -
Products: -
?
testosterone + NAD+
androst-4-ene-3,17-dione + NADH + H+
-
Substrates: -
Products: -
Products: -
?
testosterone + NAD+
androst-4-ene-3,17-dione + NADH + H+
-
Substrates: -
Products: -
Products: -
?
testosterone + NAD+
androst-4-ene-3,17-dione + NADH + H+
-
Substrates: -
Products: -
Products: -
?
testosterone + NAD+
androst-4-ene-3,17-dione + NADH + H+
-
Substrates: -
Products: -
Products: -
?
testosterone + NAD+
androst-4-ene-3,17-dione + NADH + H+
-
Substrates: -
Products: -
Products: -
?
testosterone + NAD+
androstenedione + NADH + H+
Substrates: the enzyme shows LNCaP-AKR1C3 mediates formation of testosterone, conversion of 4-androstene-3,17-dione to testosterone
Products: -
Products: -
r
testosterone + NAD+
androstenedione + NADH + H+
Substrates: -
Products: -
Products: -
r
testosterone + NAD+
androstenedione + NADH + H+
Substrates: -
Products: -
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r
additional information
?
-
Substrates: the enzyme AKR1C34 shows 3alpha/17beta/20alpha-hydroxysteroid dehydrogenase activities, substrate specificity, detailed overview. Ala54 plays a critical role in non-/recognition of the steroidal substrates. Reaction products identification by thin-layer chromatography (TLC) and liquid chromatography/mass spectrometry (LC/MS). AKR1C34 also has morphine dehydrogenase activity, EC 1.1.1.218. No activity with cyclohexanol
Products: -
Products: -
?
additional information
?
-
J7M9D0
Substrates: residues Tyr118 and Phe310 play key roles in ligand binding in AKR1C27 and AKR1C28, Glu276 that is a critical residue for the NAD+ specificity is conserved in the enzymes. In the reverse reaction, the enzymes reduces several a-dicarbonyl compounds including scamphorquinone using NADH as the coenzyme. The enzyme oxidizes 3alpha- and 17beta-hydroxysteroids and also shows S-tetralol dehydrogenase activity, cf. EC 1.1.1.121 and (S)-specific secondary alcohol dehydrogenase. In the NADH-linked reverse reaction, AKR1C27 highly reduces non-steroidal alpha-dicarbonyl compounds, and also exhibits moderate activities towards TBE, alpha-tetralone and pyridine-3-aldehyde. Substrate specificity, detailed overview
Products: -
Products: -
?
additional information
?
-
Substrates: residues Tyr118 and Phe310 play key roles in ligand binding in AKR1C27 and AKR1C28, Glu276 that is a critical residue for the NAD+ specificity is conserved in the enzymes. In the reverse reaction, the enzymes reduces several a-dicarbonyl compounds including scamphorquinone using NADH as the coenzyme. The enzyme oxidizes 3alpha- and 17beta-hydroxysteroids and also shows S-tetralol dehydrogenase activity, cf. EC 1.1.1.121 and (S)-specific secondary alcohol dehydrogenase. In the NADH-linked reverse reaction, AKR1C27 highly reduces non-steroidal alpha-dicarbonyl compounds, and also exhibits moderate activities towards TBE, alpha-tetralone and pyridine-3-aldehyde. Substrate specificity, detailed overview
Products: -
Products: -
?
additional information
?
-
Substrates: residues Tyr118 and Phe310 play key roles in ligand binding in AKR1C27 and AKR1C28, Glu276 that is a critical residue for the NAD+ specificity is conserved in the enzymes. In the reverse reaction, the enzymes reduces several a-dicarbonyl compounds including scamphorquinone using NADH as the coenzyme. The enzyme oxidizes 3alpha- and 17beta-hydroxysteroids and also shows S-tetralol dehydrogenase activity, cf. EC 1.1.1.121 and (S)-specific secondary alcohol dehydrogenase. In the NADH-linked reverse reaction, AKR1C27 highly reduces non-steroidal alpha-dicarbonyl compounds, and also exhibits moderate activities towards TBE, alpha-tetralone and pyridine-3-aldehyde. Substrate specificity, detailed overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: residues Tyr118 and Phe310 play key roles in ligand binding in AKR1C27 and AKR1C28, Glu276 that is a critical residue for the NAD+ specificity is conserved in the enzymes. In the reverse reaction, the enzymes reduces several a-dicarbonyl compounds including scamphorquinone using NADH as the coenzyme. The enzyme oxidizes 3alpha- and 17beta-hydroxysteroids and also shows S-tetralol dehydrogenase activity, cf. EC 1.1.1.121 and (S)-specific secondary alcohol dehydrogenase. In the NADH-linked reverse reaction, AKR1C27 highly reduces non-steroidal alpha-dicarbonyl compounds, and also exhibits moderate activities towards TBE, alpha-tetralone and pyridine-3-aldehyde. Substrate specificity, detailed overview
Products: -
Products: -
?
additional information
?
-
J7M9D0
Substrates: residues Tyr118 and Phe310 play key roles in ligand binding in AKR1C27 and AKR1C28, Glu276 that is a critical residue for the NAD+ specificity is conserved in the enzymes. In the reverse reaction, the enzymes reduces several a-dicarbonyl compounds including scamphorquinone using NADH as the coenzyme. The enzyme oxidizes 3alpha- and 17beta-hydroxysteroids and also shows S-tetralol dehydrogenase activity, cf. EC 1.1.1.121 and (S)-specific secondary alcohol dehydrogenase. AKR1C28 exhibits low dehydrogenase activity for 20alpha-hydroxysteroids, but does not oxidize 3beta-hydroxysteroids (5alpha/beta-androstan-3beta-ol-17-ones and 5alpha/beta-pregnan-3beta-ol-20-ones), 17alpha-hydroxysteroids (4-androsten-17alpha-ol-3-one and 17alpha-estradiol) and 20beta-hydroxysteroids (4-pregnene-17alpha/20beta-diol-3-one and 5alpha-pregnan-20beta-ol-3-one). In the NADH-linked reverse reaction, AKR1C28 highly reduces non-steroidal alpha-dicarbonyl compounds, and also exhibits moderate activities towards TBE, alpha-tetralone and pyridine-3-aldehyde. AKR1C28 shows higher kcat/Km values for 17beta-hydroxy-C19-steroids than those for 3alpha-hydroxysteroids, and most efficiently oxidized 17beta-estradiol. Substrate specificity, overview
Products: -
Products: -
?
additional information
?
-
Substrates: residues Tyr118 and Phe310 play key roles in ligand binding in AKR1C27 and AKR1C28, Glu276 that is a critical residue for the NAD+ specificity is conserved in the enzymes. In the reverse reaction, the enzymes reduces several a-dicarbonyl compounds including scamphorquinone using NADH as the coenzyme. The enzyme oxidizes 3alpha- and 17beta-hydroxysteroids and also shows S-tetralol dehydrogenase activity, cf. EC 1.1.1.121 and (S)-specific secondary alcohol dehydrogenase. AKR1C28 exhibits low dehydrogenase activity for 20alpha-hydroxysteroids, but does not oxidize 3beta-hydroxysteroids (5alpha/beta-androstan-3beta-ol-17-ones and 5alpha/beta-pregnan-3beta-ol-20-ones), 17alpha-hydroxysteroids (4-androsten-17alpha-ol-3-one and 17alpha-estradiol) and 20beta-hydroxysteroids (4-pregnene-17alpha/20beta-diol-3-one and 5alpha-pregnan-20beta-ol-3-one). In the NADH-linked reverse reaction, AKR1C28 highly reduces non-steroidal alpha-dicarbonyl compounds, and also exhibits moderate activities towards TBE, alpha-tetralone and pyridine-3-aldehyde. AKR1C28 shows higher kcat/Km values for 17beta-hydroxy-C19-steroids than those for 3alpha-hydroxysteroids, and most efficiently oxidized 17beta-estradiol. Substrate specificity, overview
Products: -
Products: -
?
additional information
?
-
Substrates: residues Tyr118 and Phe310 play key roles in ligand binding in AKR1C27 and AKR1C28, Glu276 that is a critical residue for the NAD+ specificity is conserved in the enzymes. In the reverse reaction, the enzymes reduces several a-dicarbonyl compounds including scamphorquinone using NADH as the coenzyme. The enzyme oxidizes 3alpha- and 17beta-hydroxysteroids and also shows S-tetralol dehydrogenase activity, cf. EC 1.1.1.121 and (S)-specific secondary alcohol dehydrogenase. AKR1C28 exhibits low dehydrogenase activity for 20alpha-hydroxysteroids, but does not oxidize 3beta-hydroxysteroids (5alpha/beta-androstan-3beta-ol-17-ones and 5alpha/beta-pregnan-3beta-ol-20-ones), 17alpha-hydroxysteroids (4-androsten-17alpha-ol-3-one and 17alpha-estradiol) and 20beta-hydroxysteroids (4-pregnene-17alpha/20beta-diol-3-one and 5alpha-pregnan-20beta-ol-3-one). In the NADH-linked reverse reaction, AKR1C28 highly reduces non-steroidal alpha-dicarbonyl compounds, and also exhibits moderate activities towards TBE, alpha-tetralone and pyridine-3-aldehyde. AKR1C28 shows higher kcat/Km values for 17beta-hydroxy-C19-steroids than those for 3alpha-hydroxysteroids, and most efficiently oxidized 17beta-estradiol. Substrate specificity, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: residues Tyr118 and Phe310 play key roles in ligand binding in AKR1C27 and AKR1C28, Glu276 that is a critical residue for the NAD+ specificity is conserved in the enzymes. In the reverse reaction, the enzymes reduces several a-dicarbonyl compounds including scamphorquinone using NADH as the coenzyme. The enzyme oxidizes 3alpha- and 17beta-hydroxysteroids and also shows S-tetralol dehydrogenase activity, cf. EC 1.1.1.121 and (S)-specific secondary alcohol dehydrogenase. AKR1C28 exhibits low dehydrogenase activity for 20alpha-hydroxysteroids, but does not oxidize 3beta-hydroxysteroids (5alpha/beta-androstan-3beta-ol-17-ones and 5alpha/beta-pregnan-3beta-ol-20-ones), 17alpha-hydroxysteroids (4-androsten-17alpha-ol-3-one and 17alpha-estradiol) and 20beta-hydroxysteroids (4-pregnene-17alpha/20beta-diol-3-one and 5alpha-pregnan-20beta-ol-3-one). In the NADH-linked reverse reaction, AKR1C28 highly reduces non-steroidal alpha-dicarbonyl compounds, and also exhibits moderate activities towards TBE, alpha-tetralone and pyridine-3-aldehyde. AKR1C28 shows higher kcat/Km values for 17beta-hydroxy-C19-steroids than those for 3alpha-hydroxysteroids, and most efficiently oxidized 17beta-estradiol. Substrate specificity, overview
Products: -
Products: -
?
additional information
?
-
J7M9D0
Substrates: the enzyme shows NAD+-dependent dehydrogenase activity towards other nonsteroidal alicyclic alcohols and 3alpha/17beta-hydroxy-C18/C19/C21-steroids
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme shows NAD+-dependent dehydrogenase activity towards other nonsteroidal alicyclic alcohols and 3alpha/17beta-hydroxy-C18/C19/C21-steroids
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme shows NAD+-dependent dehydrogenase activity towards other nonsteroidal alicyclic alcohols and 3alpha/17beta-hydroxy-C18/C19/C21-steroids
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme shows NAD+-dependent dehydrogenase activity towards other nonsteroidal alicyclic alcohols and 3alpha/17beta-hydroxy-C18/C19/C21-steroids
Products: -
Products: -
?
additional information
?
-
J7M9D0
Substrates: the enzyme show NAD+-dependent dehydrogenase activity towards other nonsteroidal alicyclic alcohols and 3alpha/17beta-hydroxy-C18/C19/C21-steroids. No or poor activity with naphthalene dihydrodiol, morphine, beta-ionol, geraniogeraniol, farnesol, 5alpha-androstane-3alpha,17beta-diol, 5alpha-pregnan-20alpha-ol-3-one, and 4-pregnen-20alpha-3-one
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme show NAD+-dependent dehydrogenase activity towards other nonsteroidal alicyclic alcohols and 3alpha/17beta-hydroxy-C18/C19/C21-steroids. No or poor activity with naphthalene dihydrodiol, morphine, beta-ionol, geraniogeraniol, farnesol, 5alpha-androstane-3alpha,17beta-diol, 5alpha-pregnan-20alpha-ol-3-one, and 4-pregnen-20alpha-3-one
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme show NAD+-dependent dehydrogenase activity towards other nonsteroidal alicyclic alcohols and 3alpha/17beta-hydroxy-C18/C19/C21-steroids. No or poor activity with naphthalene dihydrodiol, morphine, beta-ionol, geraniogeraniol, farnesol, 5alpha-androstane-3alpha,17beta-diol, 5alpha-pregnan-20alpha-ol-3-one, and 4-pregnen-20alpha-3-one
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme show NAD+-dependent dehydrogenase activity towards other nonsteroidal alicyclic alcohols and 3alpha/17beta-hydroxy-C18/C19/C21-steroids. No or poor activity with naphthalene dihydrodiol, morphine, beta-ionol, geraniogeraniol, farnesol, 5alpha-androstane-3alpha,17beta-diol, 5alpha-pregnan-20alpha-ol-3-one, and 4-pregnen-20alpha-3-one
Products: -
Products: -
?
additional information
?
-
J7M9D0
Substrates: the enzyme show NAD+-dependent dehydrogenase activity towards other nonsteroidal alicyclic alcohols and 3alpha/17beta-hydroxy-C18/C19/C21-steroids. No or poor activity with naphthalene dihydrodiol, morphine, and 5alpha-pregnan-20alpha-ol-3-one
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme show NAD+-dependent dehydrogenase activity towards other nonsteroidal alicyclic alcohols and 3alpha/17beta-hydroxy-C18/C19/C21-steroids. No or poor activity with naphthalene dihydrodiol, morphine, and 5alpha-pregnan-20alpha-ol-3-one
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme show NAD+-dependent dehydrogenase activity towards other nonsteroidal alicyclic alcohols and 3alpha/17beta-hydroxy-C18/C19/C21-steroids. No or poor activity with naphthalene dihydrodiol, morphine, and 5alpha-pregnan-20alpha-ol-3-one
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme show NAD+-dependent dehydrogenase activity towards other nonsteroidal alicyclic alcohols and 3alpha/17beta-hydroxy-C18/C19/C21-steroids. No or poor activity with naphthalene dihydrodiol, morphine, and 5alpha-pregnan-20alpha-ol-3-one
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5alpha-dihydrotestosterone + NAD+
androstandione + NADH + H+
-
Substrates: -
Products: -
Products: -
r
androst-4-ene-3beta,17beta-diol + NAD+
androst-4-ene-3beta-ol-17-one + NADH + H+
-
Substrates: -
Products: -
Products: -
?
daunorubicin + NADPH + H+
daunorubicinol + NADP+
Substrates: inactivation of the anticancer drug
Products: -
Products: -
r
testosterone + NAD+
androst-4-ene-3,17-dione + NADH + H+
-
Substrates: -
Products: -
Products: -
?
testosterone + NAD+
androst-4-ene-3,17-dione + NADH + H+
-
Substrates: -
Products: -
Products: -
?
testosterone + NAD+
androst-4-ene-3,17-dione + NADH + H+
-
Substrates: -
Products: -
Products: -
?
testosterone + NAD+
androst-4-ene-3,17-dione + NADH + H+
-
Substrates: -
Products: -
Products: -
?
testosterone + NAD+
androst-4-ene-3,17-dione + NADH + H+
-
Substrates: -
Products: -
Products: -
r
testosterone + NAD+
androst-4-ene-3,17-dione + NADH + H+
-
Substrates: -
Products: -
Products: -
?
testosterone + NAD+
androst-4-ene-3,17-dione + NADH + H+
-
Substrates: -
Products: -
Products: -
?
testosterone + NAD+
androst-4-ene-3,17-dione + NADH + H+
-
Substrates: -
Products: -
Products: -
?
testosterone + NAD+
androst-4-ene-3,17-dione + NADH + H+
-
Substrates: -
Products: -
Products: -
?
testosterone + NAD+
androst-4-ene-3,17-dione + NADH + H+
-
Substrates: -
Products: -
Products: -
?
testosterone + NAD+
androstenedione + NADH + H+
Substrates: the enzyme shows LNCaP-AKR1C3 mediates formation of testosterone, conversion of 4-androstene-3,17-dione to testosterone
Products: -
Products: -
r
testosterone + NAD+
androstenedione + NADH + H+
Substrates: -
Products: -
Products: -
r
testosterone + NAD+
androstenedione + NADH + H+
Substrates: -
Products: -
Products: -
r
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
conserved residues Gln270 and Glu276 are critical residues for the NAD+ specificity
NADH
-
A-specific, i.e. transfer of pro-R-hydrogen from NADH to substrate
additional information
J7M9D0
high preference for NAD+ compared to NADP+
-
additional information
high preference for NAD+ compared to NADP+
-
additional information
high preference for NAD+ compared to NADP+
-
additional information
J7M9D0
the rabbit enzyme shows high coenzyme preference for NAD+ over NADP+. Also in the reverse reaction, the enzymes reduces several alpha-dicarbonyl compounds including (S)-camphorquinone using NADH as the coenzyme, exhibiting low Km values of 0.004-0.006 mM. The reductase activity of the enzyme determined with NADPH as the coenzyme is less than 40% of their NADH-linked activity
-
additional information
the rabbit enzyme shows high coenzyme preference for NAD+ over NADP+. Also in the reverse reaction, the enzymes reduces several alpha-dicarbonyl compounds including (S)-camphorquinone using NADH as the coenzyme, exhibiting low Km values of 0.004-0.006 mM. The reductase activity of the enzyme determined with NADPH as the coenzyme is less than 40% of their NADH-linked activity
-
additional information
the rabbit enzyme shows high coenzyme preference for NAD+ over NADP+. Also in the reverse reaction, the enzymes reduces several alpha-dicarbonyl compounds including (S)-camphorquinone using NADH as the coenzyme, exhibiting low Km values of 0.004-0.006 mM. The reductase activity of the enzyme determined with NADPH as the coenzyme is less than 40% of their NADH-linked activity
-
additional information
-
the rabbit enzyme shows high coenzyme preference for NAD+ over NADP+. Also in the reverse reaction, the enzymes reduces several alpha-dicarbonyl compounds including (S)-camphorquinone using NADH as the coenzyme, exhibiting low Km values of 0.004-0.006 mM. The reductase activity of the enzyme determined with NADPH as the coenzyme is less than 40% of their NADH-linked activity
-
additional information
J7M9D0
the rabbit enzymes show high coenzyme preference for NAD+ over NADP+. Also in the reverse reaction, the enzymes reduces several alpha-dicarbonyl compounds including S-camphorquinone using NADH as the coenzyme, exhibiting low Km values of 0.004-0.006 mM. The reductase activity of the enzyme determined with NADPH as the coenzyme is less than 40% of their NADH-linked activity
-
additional information
the rabbit enzymes show high coenzyme preference for NAD+ over NADP+. Also in the reverse reaction, the enzymes reduces several alpha-dicarbonyl compounds including S-camphorquinone using NADH as the coenzyme, exhibiting low Km values of 0.004-0.006 mM. The reductase activity of the enzyme determined with NADPH as the coenzyme is less than 40% of their NADH-linked activity
-
additional information
the rabbit enzymes show high coenzyme preference for NAD+ over NADP+. Also in the reverse reaction, the enzymes reduces several alpha-dicarbonyl compounds including S-camphorquinone using NADH as the coenzyme, exhibiting low Km values of 0.004-0.006 mM. The reductase activity of the enzyme determined with NADPH as the coenzyme is less than 40% of their NADH-linked activity
-
additional information
-
the rabbit enzymes show high coenzyme preference for NAD+ over NADP+. Also in the reverse reaction, the enzymes reduces several alpha-dicarbonyl compounds including S-camphorquinone using NADH as the coenzyme, exhibiting low Km values of 0.004-0.006 mM. The reductase activity of the enzyme determined with NADPH as the coenzyme is less than 40% of their NADH-linked activity
-
additional information
the enzyme shows high preference for NAD+ compared with NADP+
-
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2E)-3-(4-bromophenyl)-2-[4-(methylsulfonyl)phenyl]prop-2-enoic acid
93.3% inhibition at 0.1 mM
(2E)-3-(4-ethylphenyl)-2-[4-(methylsulfonyl)phenyl]prop-2-enoic acid
89.1% inhibition at 0.1 mM
(2E)-3-(4-methylphenyl)-2-[4-(methylsulfonyl)phenyl]prop-2-enoic acid
92.7% inhibition at 0.1 mM
(2E)-3-[3-(3-methylbut-2-en-1-yl)-4-[(3-phenylpropanoyl)oxy]phenyl]prop-2-enoate
-
(2E)-3-[3-(3-methylbut-2-en-1-yl)-4-[(3-phenylpropanoyl)oxy]phenyl]prop-2-enoic acid
i.e. baccharin, a component of Brazilian propolis, exhibits a high inhibitory potency and selectivity for AKR1C3 over other AKR1C isoforms. When the cinnamic acid group of baccharin is esterified, there is a dramatic decrease in potency and selectivity for AKR1C3 in comparison to baccharin. Low or submicromolar inhibition is observed when the 3-prenyl group of baccharin is removed, and the selectivity over AKR1C2 is low. Inhibition of NAD+ dependent oxidation of S-tetralol
(2E)-3-[4-(acetyloxy)-3-(3-methylbut-2-en-1-yl)phenyl]prop-2-enoic acid
-
(2E)-3-[4-(methylsulfanyl)phenyl]-2-[4-(methylsulfonyl)phenyl]prop-2-enoic acid
93.5% inhibition at 0.1 mM
(2E)-3-[4-hydroxy-3-(3-methylbut-2-en-1-yl)phenyl]prop-2-enoate
37% inhibition at 0.010 mM
1-(4-[[(2R)-2-methylpiperidin-1-yl]sulfonyl]phenyl)-1,3-dihydro-2H-pyrrol-2-one
IC50 value in HCT-116 cells engineered to over-express AKR1C3 is 11 nM
1-(4-[[(2R,6S)-2,6-dimethylpiperidin-1-yl]sulfonyl]phenyl)pyrrolidin-2-one
IC50 value in HCT-116 cells engineered to over-express AKR1C3 is 22 nM
1-[4-(3,4-dihydroisoquinolin-2(1H)-ylsulfonyl)phenyl]pyrrolidin-2-one
IC50 value in HCT-116 cells engineered to over-express AKR1C3 is 24 nM
17beta-estradiol
-
0.175 mM, 25-40% inhibition of testosterone oxidation
2'-des-methyl-indomethacin
the cofactor binding cavity of AKR1C3 is not perturbed upon binding of the inhibitor
2-(2,4-dioxo-1,3-thiazolidin-5-yl)-N-(2-hydroxyphenyl)acetamide
inhibitor is about 1000times more selective for isoform AKR1C3 over AKR1C2, and selectivity is even higher when compared with AKR1C1 and AKR1C4
2-[1-(4-chlorobenzoyl)-5-methoxy-1H-indol-3-yl]-N-(2-methylbenzene-1-sulfonyl)acetamide
-
2-[1-(4-chlorobenzoyl)-5-methoxy-1H-indol-3-yl]-N-(4-cyanobenzene-1-sulfonyl)acetamide
-
2-[1-(4-chlorobenzoyl)-5-methoxy-1H-indol-3-yl]-N-(4-fluorobenzene-1-sulfonyl)acetamide
-
2-[1-(4-chlorobenzoyl)-5-methoxy-1H-indol-3-yl]-N-(4-methoxybenzene-1-sulfonyl)acetamide
-
2-[1-(4-chlorobenzoyl)-5-methoxy-1H-indol-3-yl]-N-(4-methylbenzene-1-sulfonyl)acetamide
-
2-[1-(4-chlorobenzoyl)-5-methoxy-1H-indol-3-yl]-N-(4-phenoxybenzene-1-sulfonyl)acetamide
-
2-[1-(4-chlorobenzoyl)-5-methoxy-1H-indol-3-yl]-N-(5-chlorothiophene-2-sulfonyl)acetamide
-
2-[1-(4-chlorobenzoyl)-5-methoxy-1H-indol-3-yl]-N-(methanesulfonyl)acetamide
-
2-[1-(4-chlorobenzoyl)-5-methoxy-1H-indol-3-yl]-N-(naphthalene-2-sulfonyl)acetamide
-
2-[1-(4-chlorobenzoyl)-5-methoxy-1H-indol-3-yl]-N-(trifluoromethanesulfonyl)acetamide
-
2-[1-(4-chlorobenzoyl)-5-methoxy-1H-indol-3-yl]-N-[3-(trifluoromethyl)benzene-1-sulfonyl]acetamide
-
2-[1-(4-chlorobenzoyl)-5-methoxy-1H-indol-3-yl]-N-[4-(propan-2-yl)benzene-1-sulfonyl]acetamide
-
2-[1-(4-chlorobenzoyl)-5-methoxy-1H-indol-3-yl]-N-[4-(trifluoromethyl)benzene-1-sulfonyl]acetamide
-
2-[1-(4-chlorobenzoyl)-5-methoxy-2-methyl-1H-indol-3-yl]-N-(trifluoromethanesulfonyl)acetamide
-
3-((4-nitronaphthalen-1-yl)amino)benzoic acid
inhibitor nanomolar potency and selective inhibition of isoform AKR1C3 but also acts as an androgen receptor antagonist. It inhibits 5alpha-dihydrotestosterone stimulated androgen receptor reporter gene activity with an IC50 value of 4.7 microM and produces a concentration dependent reduction in androgen receptor levels in prostate cancer cells
3-phenoxybenzoic acid
inhibitor carboxylic acid binds to the oxyanion site, in which the carboxylate group very closely overlays the acetate molecule found in other AKR1C3 structures and forms hydrogen bonds to the enzyme catalytic residues His117 and Tyr55, as well as to a conserved water network located in and near the SP3 subpocket. The 3-phenoxy ring extends into the SP1 subpocket and makes van der Waals contacts with the aromatic residues Phe306, Phe311 and Tyr319 that line the pocket
3-[(4-nitrophenyl)amino]benzoic acid
94fold selectivity for the inhibition of isoform AKR1C3 over AKR1C2
3-[1-(4-chlorobenzoyl)-5-methoxy-3-methyl-1H-indol-2-yl]-2,2-dimethylpropanoic acid
-
3-[1-(4-chlorobenzoyl)-5-methoxy-3-methyl-1H-indol-2-yl]-2-methylpropanoic acid
-
3-[1-(4-chlorobenzoyl)-5-methoxy-3-methyl-1H-indol-2-yl]-N-(2-methylbenzene-1-sulfonyl)propanamide
-
3-[1-(4-chlorobenzoyl)-5-methoxy-3-methyl-1H-indol-2-yl]-N-(4-methylbenzene-1-sulfonyl)propanamide
-
3-[1-(4-chlorobenzoyl)-5-methoxy-3-methyl-1H-indol-2-yl]-N-(5-chlorothiophene-2-sulfonyl)propanamide
-
3-[1-(4-chlorobenzoyl)-5-methoxy-3-methyl-1H-indol-2-yl]-N-(methanesulfonyl)-2-methylpropanamide
-
3-[1-(4-chlorobenzoyl)-5-methoxy-3-methyl-1H-indol-2-yl]-N-(methanesulfonyl)propanamide
-
3-[1-(4-chlorobenzoyl)-5-methoxy-3-methyl-1H-indol-2-yl]-N-(naphthalene-2-sulfonyl)propanamide
-
3-[1-(4-chlorobenzoyl)-5-methoxy-3-methyl-1H-indol-2-yl]-N-(trifluoromethanesulfonyl)propanamide
-
3-[1-(4-chlorobenzoyl)-5-methoxy-3-methyl-1H-indol-2-yl]-N-[4-(propan-2-yl)benzene-1-sulfonyl]propanamide
-
3-[1-(4-chlorobenzoyl)-5-methoxy-3-methyl-1H-indol-2-yl]-N-[4-(trifluoromethoxy)benzene-1-sulfonyl]propanamide
-
3-[1-(4-chlorobenzoyl)-5-methoxy-3-methyl-1H-indol-2-yl]-N-[4-(trifluoromethyl)benzene-1-sulfonyl]propanamide
-
3-[[4-(methoxymethyl)phenyl]amino]benzoic acid
360fold selectivity for the inhibition of isoform AKR1C3 over AKR1C2
3a-phenyl-2,3,3a,4-tetrahydro-1H-pyrrolo[1,2-a]benzimidazol-1-one
inhibitor shows 17fold and 30fold selectivity against isoforms AKR1C2 and AKR1C1, respectively, and much higher selectivity against AKR1C4
6-methoxy-9-[3-(trifluoromethyl)benzoyl]-2,3,4,9-tetrahydro-1H-carbazole-3-carboxylic acid
-
9-(4-chlorobenzoyl)-6-methoxy-2,3,4,9-tetrahydro-1H-carbazole-2-carboxylic acid
-
9-(4-chlorobenzoyl)-6-methoxy-2,3,4,9-tetrahydro-1H-carbazole-3-carboxylic acid
-
9-(4-chlorobenzoyl)-N-(methanesulfonyl)-6-methoxy-2,3,4,9-tetrahydro-1H-carbazole-3-carboxamide
-
biochain A
-
0.014 mM, 50% inhibition, reduction of androst-4-ene-3,17-dione, 0.008 mM, oxidation of androstanediol
coumestrol
-
0.005 mM, 50% inhibition, reduction of androst-4-ene-3,17-dione, 0.011 mM, 50% inhibition, oxidation of androstanediol
N-(4-acetylbenzene-1-sulfonyl)-2-[1-(4-chlorobenzoyl)-5-methoxy-1H-indol-3-yl]acetamide
-
N-(4-acetylbenzene-1-sulfonyl)-3-[1-(4-chlorobenzoyl)-5-methoxy-3-methyl-1H-indol-2-yl]propanamide
-
N-(4-bromobenzene-1-sulfonyl)-2-[1-(4-chlorobenzoyl)-5-methoxy-1H-indol-3-yl]acetamide
-
N-[2,5-bis(trifluoromethyl)benzene-1-sulfonyl]-2-[1-(4-chlorobenzoyl)-5-methoxy-1H-indol-3-yl]acetamide
-
tert-butyl(2E)-3-[3-(3-methylbut-2-en-1-yl)-4-[(3-phenylpropanoyl)oxy]phenyl]prop-2-enoate
-
Triton X-100
-
immediate loss of 60-70% activity, remaining activity is stable for 4 days, competitive vs. testosterone, non-competitive vs. NAD+
[1-[4-(chloromethyl)benzoyl]-5-methoxy-2-methyl-1H-indol-3-yl]acetic acid
-
[5-fluoro-2-methyl-1-[3-(trifluoromethyl)benzoyl]-1H-indol-3-yl]acetic acid
-
[5-methoxy-2-methyl-1-[3-(trifluoromethyl)benzoyl]-1H-indol-3-yl]acetic acid
-
[5-methoxy-2-methyl-1-[4-(trifluoromethyl)benzoyl]-1H-indol-3-yl]acetic acid
-
3-[[4-(trifluoromethyl)phenyl]amino]benzoic acid
250fold selectivity for the inhibition of isoform AKR1C3 over AKR1C2
3-[[4-(trifluoromethyl)phenyl]amino]benzoic acid
in complex with AKR1C3. Compound adopts a similar binding orientation as flufenamic acid, however, its phenylamino ring projects deeper into a subpocket and confers selectivity over the other AKR1C isoforms
quercetin
-
0.009 mM, 50% inhibition, reduction of androst-4-ene-3,17-dione, 0.005 mM, oxidation of androstanediol
zearalenone
-
0.004 mM, 50% inhibition, reduction of androst-4-ene-3,17-dione, 0.002 mM, oxidation of androstanediol
additional information
development of potent and selective indomethacin analogues for the inhibition of AKR1C3 in castrate-resistant prostate cancer, overview. Increasing the length of the aliphatic side chain of indomethacin from -ethyl to -propyl leads to a 2fold reduction in AKR1C3 potency, but the compound retained 257fold selectivity for AKR1C3 over AKR1C2
-
additional information
screening of baccharin analogues as selective inhibitors against type 5 17beta-hydroxysteroid dehydrogenase (AKR1C3), selectivity versus AKR1C2
-
additional information
no or poor inhibition by 7-hydroxyflavone, chrysin, quercetin, genistein, galangin, lithocholic acid, and zearalenone
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.095
(R)-1,2,3,4-tetrahydro-1-naphthol
pH 7.4, 25°C, recombinant enzyme
0.03
alpha-3-hydroxyhexobarbital
pH 7.4, 25°C, recombinant enzyme
0.013
beta-3-hydroxyhexobarbital
pH 7.4, 25°C, recombinant enzyme
0.63
cis-benzene dihydrodiol
pH 7.4, 25°C, recombinant enzyme
0.004
(S)-1,2,3,4-tetrahydro-1-naphthol
pH 7.4, 25°C
0.022
(S)-1,2,3,4-tetrahydro-1-naphthol
pH 7.4, 25°C
0.061
(S)-1,2,3,4-tetrahydro-1-naphthol
pH 7.4, 25°C, recombinant enzyme
0.25
(S)-1,2,3,4-tetrahydro-1-naphthol
pH 7.4, 25°C
0.00067
5alpha-androstan-17beta-ol-3-one
pH 7.4, 25°C
0.0078
5alpha-androstan-17beta-ol-3-one
pH 7.4, 25°C
0.13
5alpha-androstan-17beta-ol-3-one
pH 7.4, 25°C
0.0022
5alpha-Androstan-3alpha-ol-17-one
pH 7.4, 25°C
0.0092
5alpha-Androstan-3alpha-ol-17-one
pH 7.4, 25°C
0.0005
5alpha-androstane-3alpha,17beta-diol
pH 7.4, 25°C
0.0078
5alpha-androstane-3alpha,17beta-diol
pH 7.4, 25°C
0.00067
5alpha-pregnan-3alpha-ol-20-one
pH 7.4, 25°C
0.0035
5alpha-pregnan-3alpha-ol-20-one
pH 7.4, 25°C
0.00067
5beta-androstan-17beta-ol-3-one
pH 7.4, 25°C
0.0076
5beta-androstan-17beta-ol-3-one
pH 7.4, 25°C
0.03
5beta-androstan-17beta-ol-3-one
pH 7.4, 25°C
0.0015
5beta-Androstan-3alpha-ol-17-one
pH 7.4, 25°C
0.0023
5beta-Androstan-3alpha-ol-17-one
pH 7.4, 25°C
0.0022
5beta-androstane-3alpha,17beta-diol
pH 7.4, 25°C
0.02
5beta-androstane-3alpha,17beta-diol
pH 7.4, 25°C
0.0036
5beta-Pregnan-3alpha-ol-20-one
pH 7.4, 25°C
0.0037
5beta-Pregnan-3alpha-ol-20-one
pH 7.4, 25°C
0.0021
6-tert-butyl-2,3-epoxy-4-hydroxy-5-cyclohexen-1-one
pH 7.4, 25°C
0.0042
6-tert-butyl-2,3-epoxy-4-hydroxy-5-cyclohexen-1-one
pH 7.4, 25°C
0.101
6-tert-butyl-2,3-epoxy-4-hydroxy-5-cyclohexen-1-one
pH 7.4, 25°C
0.0185
NAD+
-
enzyme avtivity in hepatic microsomes, one individual animal
0.0174
testosterone
-
enzyme avtivity in hepatic microsomes, one individual animal
additional information
additional information
J7M9D0
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
J7M9D0
Michaelis-Menten kinetics of wild-type and mutant enzymes, overview
-
additional information
additional information
Michaelis-Menten kinetics of wild-type and mutant enzymes, overview
-
additional information
additional information
Michaelis-Menten kinetics of wild-type and mutant enzymes, overview
-
additional information
additional information
-
Michaelis-Menten kinetics of wild-type and mutant enzymes, overview
-
additional information
additional information
Michaelis-Menten kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0075
(R)-1,2,3,4-tetrahydro-1-naphthol
pH 7.4, 25°C, recombinant enzyme
0.04
alpha-3-hydroxyhexobarbital
pH 7.4, 25°C, recombinant enzyme
0.0967
beta-3-hydroxyhexobarbital
pH 7.4, 25°C, recombinant enzyme
0.032
cis-benzene dihydrodiol
pH 7.4, 25°C, recombinant enzyme
0.045
trans-benzene dihydrodiol
pH 7.4, 25°C, recombinant enzyme
0.042
(S)-1,2,3,4-tetrahydro-1-naphthol
pH 7.4, 25°C
0.1
(S)-1,2,3,4-tetrahydro-1-naphthol
pH 7.4, 25°C
0.105
(S)-1,2,3,4-tetrahydro-1-naphthol
pH 7.4, 25°C, recombinant enzyme
0.367
(S)-1,2,3,4-tetrahydro-1-naphthol
pH 7.4, 25°C
0.0052
5alpha-androstan-17beta-ol-3-one
pH 7.4, 25°C
0.0103
5alpha-androstan-17beta-ol-3-one
pH 7.4, 25°C
0.065
5alpha-androstan-17beta-ol-3-one
pH 7.4, 25°C
0.0033
5alpha-Androstan-3alpha-ol-17-one
pH 7.4, 25°C
0.058
5alpha-Androstan-3alpha-ol-17-one
pH 7.4, 25°C
0.0027
5alpha-androstane-3alpha,17beta-diol
pH 7.4, 25°C
0.055
5alpha-androstane-3alpha,17beta-diol
pH 7.4, 25°C
0.0012
5alpha-pregnan-3alpha-ol-20-one
pH 7.4, 25°C
0.0072
5alpha-pregnan-3alpha-ol-20-one
pH 7.4, 25°C
0.002
5beta-androstan-17beta-ol-3-one
pH 7.4, 25°C
0.0032
5beta-androstan-17beta-ol-3-one
pH 7.4, 25°C
0.0167
5beta-androstan-17beta-ol-3-one
pH 7.4, 25°C
0.0023
5beta-Androstan-3alpha-ol-17-one
pH 7.4, 25°C
0.052
5beta-Androstan-3alpha-ol-17-one
pH 7.4, 25°C
0.004
5beta-androstane-3alpha,17beta-diol
pH 7.4, 25°C
0.0122
5beta-androstane-3alpha,17beta-diol
pH 7.4, 25°C
0.005
5beta-Pregnan-3alpha-ol-20-one
pH 7.4, 25°C
0.0074
5beta-Pregnan-3alpha-ol-20-one
pH 7.4, 25°C
0.023
5beta-Pregnan-3alpha-ol-20-one
pH 7.4, 25°C
0.052
6-tert-butyl-2,3-epoxy-4-hydroxy-5-cyclohexen-1-one
pH 7.4, 25°C
0.108
6-tert-butyl-2,3-epoxy-4-hydroxy-5-cyclohexen-1-one
pH 7.4, 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.083
(R)-1,2,3,4-tetrahydro-1-naphthol
pH 7.4, 25°C, recombinant enzyme
1.67
(S)-1,2,3,4-tetrahydro-1-naphthol
pH 7.4, 25°C, recombinant enzyme
2.17
alpha-3-hydroxyhexobarbital
pH 7.4, 25°C, recombinant enzyme
7.5
beta-3-hydroxyhexobarbital
pH 7.4, 25°C, recombinant enzyme
0.05
cis-benzene dihydrodiol
pH 7.4, 25°C, recombinant enzyme
0.05
trans-benzene dihydrodiol
pH 7.4, 25°C, recombinant enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000107
2-(2,4-dioxo-1,3-thiazolidin-5-yl)-N-(2-hydroxyphenyl)acetamide
pH 7.0, temperature not specified in the publication
0.00273
3a-phenyl-2,3,3a,4-tetrahydro-1H-pyrrolo[1,2-a]benzimidazol-1-one
pH 7.0, temperature not specified in the publication
0.0029
Hexestrol
pH 7.4, 25°C, recombinant enzyme
0.00056
hinokitiol
pH 7.4, 25°C, recombinant enzyme
0.000024
ikarisoside A
pH 7.4, 25°C, recombinant enzyme
0.0007
noranhydroicaritin
pH 7.4, 25°C, recombinant enzyme
0.00038
quercitrin
pH 7.4, 25°C, recombinant enzyme
0.003
zearalenone
pH 7.4, 25°C, recombinant enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.021
(2E)-3-(3,3-dimethyl-3,4-dihydro-2H-1-benzopyran-6-yl)prop-2-enoate
Homo sapiens
pH 7.0, 37°C
0.0136
(2E)-3-(4-bromophenyl)-2-[4-(methylsulfonyl)phenyl]prop-2-enoic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.0136
(2E)-3-(4-ethylphenyl)-2-[4-(methylsulfonyl)phenyl]prop-2-enoic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.0134
(2E)-3-(4-methylphenyl)-2-[4-(methylsulfonyl)phenyl]prop-2-enoic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.0001
(2E)-3-[3-(3-methylbut-2-en-1-yl)-4-[(3-phenylpropanoyl)oxy]phenyl]prop-2-enoic acid
Homo sapiens
pH 7.0, 37°C
0.0086
(2E)-3-[4-(acetyloxy)-3-(3-methylbut-2-en-1-yl)phenyl]prop-2-enoate
Homo sapiens
pH 7.0, 37°C
0.00044
(2E)-3-[4-(acetyloxy)-3-(3-methylbut-2-en-1-yl)phenyl]prop-2-enoic acid
Homo sapiens
pH 7.0, 37°C
0.0058
(2E)-3-[4-(methylsulfanyl)phenyl]-2-[4-(methylsulfonyl)phenyl]prop-2-enoic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.068
(2E)-3-[4-(pyridine-4-carbonyloxy)phenyl]prop-2-enoic acid
Homo sapiens
pH 7.0, 37°C
0.0097
(2E)-3-[4-hydroxy-3-(3-methylbut-2-en-1-yl)phenyl]prop-2-enoate
Homo sapiens
pH 7.0, 37°C
0.00356
(4-chlorophenyl)(5-methoxy-2-methyl-1H-indol-1-yl)methanone
Homo sapiens
100 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.00096
(E)-3-(3-((3-phenylpropanoyl)oxy)phenyl)acrylic acid
Homo sapiens
pH 7.0, 37°C
0.0023
(Z/E)-3-(4-((3-phenylpropanoyl)oxy)phenyl)acrylic acid
Homo sapiens
pH 7.0, 37°C
0.632
(Z/E)-tert-butyl 3-(4-(3-phenylpropanoyloxy)phenyl)acrylate
Homo sapiens
pH 7.0, 37°C
0.000094
1-(4-[[(2R)-2-methylpiperidin-1-yl]sulfonyl]phenyl)-1,3-dihydro-2H-pyrrol-2-one
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.000056
1-(4-[[(2R,6S)-2,6-dimethylpiperidin-1-yl]sulfonyl]phenyl)pyrrolidin-2-one
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.000052
1-[4-(3,4-dihydroisoquinolin-2(1H)-ylsulfonyl)phenyl]pyrrolidin-2-one
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.000213
2-(2,4-dioxo-1,3-thiazolidin-5-yl)-N-(2-hydroxyphenyl)acetamide
Homo sapiens
pH 7.0, temperature not specified in the publication
0.00882
2-[1-(4-chlorobenzoyl)-5-methoxy-1H-indol-3-yl]-N-(2-methylbenzene-1-sulfonyl)acetamide
Homo sapiens
100 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.00111
2-[1-(4-chlorobenzoyl)-5-methoxy-1H-indol-3-yl]-N-(4-cyanobenzene-1-sulfonyl)acetamide
Homo sapiens
100 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.00786
2-[1-(4-chlorobenzoyl)-5-methoxy-1H-indol-3-yl]-N-(4-fluorobenzene-1-sulfonyl)acetamide
Homo sapiens
100 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.0058
2-[1-(4-chlorobenzoyl)-5-methoxy-1H-indol-3-yl]-N-(4-methoxybenzene-1-sulfonyl)acetamide
Homo sapiens
111 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.0124
2-[1-(4-chlorobenzoyl)-5-methoxy-1H-indol-3-yl]-N-(4-methylbenzene-1-sulfonyl)acetamide
Homo sapiens
100 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.00252
2-[1-(4-chlorobenzoyl)-5-methoxy-1H-indol-3-yl]-N-(4-phenoxybenzene-1-sulfonyl)acetamide
Homo sapiens
100 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.00373
2-[1-(4-chlorobenzoyl)-5-methoxy-1H-indol-3-yl]-N-(5-chlorothiophene-2-sulfonyl)acetamide
Homo sapiens
100 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.012
2-[1-(4-chlorobenzoyl)-5-methoxy-1H-indol-3-yl]-N-(methanesulfonyl)acetamide
Homo sapiens
100 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.00119
2-[1-(4-chlorobenzoyl)-5-methoxy-1H-indol-3-yl]-N-(naphthalene-2-sulfonyl)acetamide
Homo sapiens
100 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.00021
2-[1-(4-chlorobenzoyl)-5-methoxy-1H-indol-3-yl]-N-(trifluoromethanesulfonyl)acetamide
Homo sapiens
100 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.00265
2-[1-(4-chlorobenzoyl)-5-methoxy-1H-indol-3-yl]-N-[3-(trifluoromethyl)benzene-1-sulfonyl]acetamide
Homo sapiens
100 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.00634
2-[1-(4-chlorobenzoyl)-5-methoxy-1H-indol-3-yl]-N-[4-(propan-2-yl)benzene-1-sulfonyl]acetamide
Homo sapiens
110 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.00207
2-[1-(4-chlorobenzoyl)-5-methoxy-1H-indol-3-yl]-N-[4-(trifluoromethyl)benzene-1-sulfonyl]acetamide
Homo sapiens
100 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.00074
2-[1-(4-chlorobenzoyl)-5-methoxy-2-methyl-1H-indol-3-yl]-N-(trifluoromethanesulfonyl)acetamide
Homo sapiens
100 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.0052
2-[[(3-hydroxyphenyl)carbonyl]amino]-4,5-dimethoxybenzoic acid
Homo sapiens
pH 7.0, temperature not specified in the publication
0.00084
2-[[(3-hydroxyphenyl)carbonyl]amino]-5-nitrobenzoic acid
Homo sapiens
pH 7.0, temperature not specified in the publication
0.08
3-((4-nitronaphthalen-1-yl)amino)benzoic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.1
3-(5-methoxy-2-methyl-1H-indol-3-yl)propanoic acid
Homo sapiens
above, 100 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.000036
3-[(4-nitrophenyl)amino]benzoic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.00015
3-[1-(4-chlorobenzoyl)-2-ethyl-5-methoxy-1H-indol-3-yl]propanoic acid
Homo sapiens
100 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.00029
3-[1-(4-chlorobenzoyl)-5-fluoro-2-methyl-1H-indol-3-yl]propanoic acid
Homo sapiens
100 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.00022
3-[1-(4-chlorobenzoyl)-5-methoxy-2-methyl-1H-indol-3-yl]propanoic acid
Homo sapiens
100 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.00012
3-[1-(4-chlorobenzoyl)-5-methoxy-3-methyl-1H-indol-2-yl]-2,2-dimethylpropanoic acid
Homo sapiens
100 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.00029
3-[1-(4-chlorobenzoyl)-5-methoxy-3-methyl-1H-indol-2-yl]-2-methylpropanoic acid
Homo sapiens
100 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.00325
3-[1-(4-chlorobenzoyl)-5-methoxy-3-methyl-1H-indol-2-yl]-N-(2-methylbenzene-1-sulfonyl)propanamide
Homo sapiens
100 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.00311
3-[1-(4-chlorobenzoyl)-5-methoxy-3-methyl-1H-indol-2-yl]-N-(4-methylbenzene-1-sulfonyl)propanamide
Homo sapiens
100 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.00553
3-[1-(4-chlorobenzoyl)-5-methoxy-3-methyl-1H-indol-2-yl]-N-(methanesulfonyl)-2-methylpropanamide
Homo sapiens
100 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.00034
3-[1-(4-chlorobenzoyl)-5-methoxy-3-methyl-1H-indol-2-yl]-N-(methanesulfonyl)propanamide
Homo sapiens
100 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.00254
3-[1-(4-chlorobenzoyl)-5-methoxy-3-methyl-1H-indol-2-yl]-N-(naphthalene-2-sulfonyl)propanamide
Homo sapiens
100 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.00144
3-[1-(4-chlorobenzoyl)-5-methoxy-3-methyl-1H-indol-2-yl]-N-(trifluoromethanesulfonyl)propanamide
Homo sapiens
100 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.00469
3-[1-(4-chlorobenzoyl)-5-methoxy-3-methyl-1H-indol-2-yl]-N-[4-(propan-2-yl)benzene-1-sulfonyl]propanamide
Homo sapiens
100 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.0025
3-[1-(4-chlorobenzoyl)-5-methoxy-3-methyl-1H-indol-2-yl]-N-[4-(trifluoromethoxy)benzene-1-sulfonyl]propanamide
Homo sapiens
110 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.00111
3-[1-(4-chlorobenzoyl)-5-methoxy-3-methyl-1H-indol-2-yl]-N-[4-(trifluoromethyl)benzene-1-sulfonyl]propanamide
Homo sapiens
100 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.00013
3-[1-(4-chlorobenzoyl)-5-methoxy-3-methyl-1H-indol-2-yl]propanoic acid
Homo sapiens
100 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.000054
3-[[4-(methoxymethyl)phenyl]amino]benzoic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.000062
3-[[4-(trifluoromethyl)phenyl]amino]benzoic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.00546
3a-phenyl-2,3,3a,4-tetrahydro-1H-pyrrolo[1,2-a]benzimidazol-1-one
Homo sapiens
pH 7.0, temperature not specified in the publication
0.00015
4-[1-(4-chlorobenzoyl)-5-methoxy-3-methyl-1H-indol-2-yl]butanoic acid
Homo sapiens
100 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.0019
5-bromo-2-[[(3-hydroxyphenyl)carbonyl]amino]benzoic acid
Homo sapiens
pH 7.0, temperature not specified in the publication
0.0022
5-chloro-2-[[(3-hydroxyphenyl)carbonyl]amino]benzoic acid
Homo sapiens
pH 7.0, temperature not specified in the publication
0.0024
5-methoxy-3-(2-oxobutyl)-1H-indole-1-carboxylic acid
Homo sapiens
100 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.000279
6-methoxy-9-[3-(trifluoromethyl)benzoyl]-2,3,4,9-tetrahydro-1H-carbazole-3-carboxylic acid
Homo sapiens
100 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.00034
9-(4-chlorobenzoyl)-6-methoxy-2,3,4,9-tetrahydro-1H-carbazole-2-carboxylic acid
Homo sapiens
100 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.00016
9-(4-chlorobenzoyl)-6-methoxy-2,3,4,9-tetrahydro-1H-carbazole-3-carboxylic acid
Homo sapiens
100 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.00507
9-(4-chlorobenzoyl)-N-(methanesulfonyl)-6-methoxy-2,3,4,9-tetrahydro-1H-carbazole-3-carboxamide
Homo sapiens
100 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.0001
indomethacin
Homo sapiens
100 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.02278
methyl 5-methoxy-3-(2-oxobutyl)-1H-indole-1-carboxylate
Homo sapiens
100 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.01134
methyl [1-(4-chlorobenzoyl)-5-methoxy-1H-indol-3-yl]acetate
Homo sapiens
100 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.00564
methyl [1-(4-chlorobenzoyl)-5-methoxy-2-methyl-1H-indol-3-yl]acetate
Homo sapiens
100 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.00209
N-(4-acetylbenzene-1-sulfonyl)-2-[1-(4-chlorobenzoyl)-5-methoxy-1H-indol-3-yl]acetamide
Homo sapiens
100 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.00265
N-(4-acetylbenzene-1-sulfonyl)-3-[1-(4-chlorobenzoyl)-5-methoxy-3-methyl-1H-indol-2-yl]propanamide
Homo sapiens
100 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.00397
N-(4-bromobenzene-1-sulfonyl)-2-[1-(4-chlorobenzoyl)-5-methoxy-1H-indol-3-yl]acetamide
Homo sapiens
100 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.00194
N-[2,5-bis(trifluoromethyl)benzene-1-sulfonyl]-2-[1-(4-chlorobenzoyl)-5-methoxy-1H-indol-3-yl]acetamide
Homo sapiens
100 mM Tris-HCl buffer, 37°C, pH not specified in the publication
607
tert-butyl(2E)-3-[3-(3-methylbut-2-en-1-yl)-4-[(3-phenylpropanoyl)oxy]phenyl]prop-2-enoate
Homo sapiens
pH 7.0, 37°C
0.0005
[1-(4-chlorobenzoyl)-5-fluoro-1H-indol-3-yl]acetic acid
Homo sapiens
100 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.00025
[1-(4-chlorobenzoyl)-5-fluoro-2-methyl-1H-indol-3-yl]acetic acid
Homo sapiens
100 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.00096
[1-(4-chlorobenzoyl)-5-methoxy-1H-indol-3-yl]acetic acid
Homo sapiens
100 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.00007
[1-(4-chlorobenzoyl)-5-methoxy-2-propyl-1H-indol-3-yl]acetic acid
Homo sapiens
111 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.00496
[1-(4-fluorobenzoyl)-5-methoxy-1H-indol-3-yl]acetic acid
Homo sapiens
100 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.00071
[1-(4-fluorobenzoyl)-5-methoxy-2-methyl-1H-indol-3-yl]acetic acid
Homo sapiens
100 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.00012
[1-[4-(chloromethyl)benzoyl]-5-methoxy-2-methyl-1H-indol-3-yl]acetic acid
Homo sapiens
100 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.00223
[5-fluoro-2-methyl-1-[3-(trifluoromethyl)benzoyl]-1H-indol-3-yl]acetic acid
Homo sapiens
100 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.00014
[5-methoxy-1-(4-methoxybenzoyl)-2-methyl-1H-indol-3-yl]acetic acid
Homo sapiens
100 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.00521
[5-methoxy-1-[3-(trifluoromethyl)benzoyl]-1H-indol-3-yl]acetic acid
Homo sapiens
111 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.00108
[5-methoxy-1-[4-(trifluoromethyl)benzoyl]-1H-indol-3-yl]acetic acid
Homo sapiens
110 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.00016
[5-methoxy-2-methyl-1-(4-methylbenzoyl)-1H-indol-3-yl]acetic acid
Homo sapiens
100 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.00244
[5-methoxy-2-methyl-1-[3-(trifluoromethyl)benzoyl]-1H-indol-3-yl]acetic acid
Homo sapiens
100 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.00027
[5-methoxy-2-methyl-1-[4-(trifluoromethyl)benzoyl]-1H-indol-3-yl]acetic acid
Homo sapiens
100 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.00007
3-[1-(4-chlorobenzoyl)-3-ethyl-5-methoxy-1H-indol-2-yl]propanoic acid
Homo sapiens
110 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.00009
3-[1-(4-chlorobenzoyl)-3-ethyl-5-methoxy-1H-indol-2-yl]propanoic acid
Homo sapiens
100 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.05
Hexestrol
Oryctolagus cuniculus
above, pH 7.4, 25°C, recombinant wild-type and mutant enzymes
0.002
hinokitiol
Oryctolagus cuniculus
pH 7.4, 25°C, recombinant enzyme
0.0026
hinokitiol
Oryctolagus cuniculus
pH 7.4, 25°C, recombinant mutant Y118F/F310I enzyme
0.01
hinokitiol
Oryctolagus cuniculus
pH 7.4, 25°C, recombinant mutant Y118F enzyme
0.013
hinokitiol
Oryctolagus cuniculus
pH 7.4, 25°C, recombinant mutant F310I enzyme
0.037
hinokitiol
Oryctolagus cuniculus
pH 7.4, 25°C, recombinant enzyme
0.042
hinokitiol
Oryctolagus cuniculus
pH 7.4, 25°C, recombinant enzyme
0.017
icarisid II
Oryctolagus cuniculus
pH 7.4, 25°C, recombinant enzyme
0.021
icarisid II
Oryctolagus cuniculus
pH 7.4, 25°C, recombinant enzyme
0.05
icarisid II
Oryctolagus cuniculus
above, pH 7.4, 25°C, recombinant enzyme
0.00013
ikarisoside A
Oryctolagus cuniculus
pH 7.4, 25°C, recombinant enzyme
0.0004
ikarisoside A
Oryctolagus cuniculus
pH 7.4, 25°C, recombinant mutant Y118F/F310I enzyme
0.00049
ikarisoside A
Oryctolagus cuniculus
pH 7.4, 25°C, recombinant mutant Y118F enzyme
0.009
ikarisoside A
Oryctolagus cuniculus
pH 7.4, 25°C, recombinant enzyme
0.009
ikarisoside A
Oryctolagus cuniculus
pH 7.4, 25°C, recombinant wild-type enzyme
0.013
ikarisoside A
Oryctolagus cuniculus
pH 7.4, 25°C, recombinant enzyme
0.02
ikarisoside A
Oryctolagus cuniculus
pH 7.4, 25°C, recombinant mutant F310I enzyme
0.015
kaempferol
Oryctolagus cuniculus
pH 7.4, 25°C, recombinant enzyme
0.02
kaempferol
Oryctolagus cuniculus
above, pH 7.4, 25°C, recombinant enzyme
0.00224
methyl [5-methoxy-1-(4-methoxybenzoyl)-2-methyl-1H-indol-3-yl]acetate
Homo sapiens
100 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.00759
methyl [5-methoxy-1-(4-methoxybenzoyl)-2-methyl-1H-indol-3-yl]acetate
Homo sapiens
100 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.00754
methyl [5-methoxy-2-methyl-1-(4-methylbenzoyl)-1H-indol-3-yl]acetate
Homo sapiens
110 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.01571
methyl [5-methoxy-2-methyl-1-(4-methylbenzoyl)-1H-indol-3-yl]acetate
Homo sapiens
111 mM Tris-HCl buffer, 37°C, pH not specified in the publication
0.0022
noranhydroicaritin
Oryctolagus cuniculus
pH 7.4, 25°C, recombinant enzyme
0.0064
noranhydroicaritin
Oryctolagus cuniculus
pH 7.4, 25°C, recombinant enzyme
0.015
noranhydroicaritin
Oryctolagus cuniculus
pH 7.4, 25°C, recombinant enzyme
0.007
Phenolphthalein
Oryctolagus cuniculus
pH 7.4, 25°C, recombinant enzyme
0.017
Phenolphthalein
Oryctolagus cuniculus
pH 7.4, 25°C, recombinant enzyme
0.02
Phenolphthalein
Oryctolagus cuniculus
pH 7.4, 25°C, recombinant enzyme
0.0024
quercitrin
Oryctolagus cuniculus
pH 7.4, 25°C, recombinant enzyme
0.0025
quercitrin
Oryctolagus cuniculus
pH 7.4, 25°C, recombinant enzyme
0.0091
zearalenone
Oryctolagus cuniculus
pH 7.4, 25°C, recombinant enzyme
0.05
zearalenone
Oryctolagus cuniculus
pH 7.4, 25°C, recombinant enzyme
0.05
zearalenone
Oryctolagus cuniculus
above, pH 7.4, 25°C, recombinant enzyme
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
0.186 micromol min/g liver, microsomes, substrate testosterone, coenzyme NAD+
additional information
-
0.086 micromol min/g liver, microsomes, substrate testosterone, coenzyme NADP+
additional information
-
0.1556 micromol min/g liver, microsomes, substrate 5alpha-dihydrotestosterone, coenzyme NAD+
additional information
-
0.046 micromol min/g liver, microsomes, substrate 5alpha-dihydrotestosterone, coenzyme NADP+
additional information
-
0.388 micromol min/g liver, microsomes, substrate 5beta-dihydrotestosterone, coenzyme NAD+
additional information
-
0.144 micromol min/g liver, microsomes, substrate 5beta-dihydrotestosterone, coenzyme NADP+
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10
7.4
9 - 10
-
oxidation of testosterone, equal velocity of oxidation and reduction at pH 8.0
9.5 - 10
NAD+-linked (S)-tetralol dehydrogenase activity
6
NADH-linked (S)-camphorquinone reduction activity
7
-
oxidation of testosterone, equal velocity of oxidation and reduction at pH 6.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
45
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
uniform, diffuse, and strong expression of isoform AKR1C3 in normal endometrial epithelium but not in endometrial stromal cells. The expression of AKR1C3 is reduced in both hyperplastic and carcinomatous endometrial epithelium
brenda
uniform, diffuse, and strong expression of isoform AKR1C3 in normal endometrial epithelium but not in endometrial stromal cells. The expression of AKR1C3 is reduced in both hyperplastic and carcinomatous endometrial epithelium
brenda
-
positive AKR1C3 immunoreactivity is extensively present in both adenocarcinoma and squamous cell carcinoma arising from the lung and the gastroesophageal junction
brenda
-
positive AKR1C3 immunoreactivity is extensively present in both adenocarcinoma and squamous cell carcinoma arising from the lung and the gastroesophageal junction
brenda
-
strong isoform AKR1C3 immunoreactivity in columnar epithelium but only weak immunoreactivity in squamous epithelium of the gastrointestinal junction
brenda
-
pre- and peri-pubertal changes promote expression of the enzyme in Leydig cells
brenda
-
strong isoform AKR1C3 immunoreactivity in bronchial epithelium but not in bronchial glands or alveolar pneumocytes
brenda
-
positive AKR1C3 immunoreactivity is extensively present in both adenocarcinoma and squamous cell carcinoma arising from the lung and the gastroesophageal junction
brenda
-
positive AKR1C3 immunoreactivity is extensively present in both adenocarcinoma and squamous cell carcinoma arising from the lung and the gastroesophageal junction
brenda
-
in contrast to the normal adult testis, the pediatric cryptorchid testis shows AKR1C3 expression in 18%-26% of Sertoli cells in patients at Tanner stages 2 and beyond
brenda
-
positive AKR1C3 immunoreactivity is extensively present in both adenocarcinoma and squamous cell carcinoma arising from the lung and the gastroesophageal junction
brenda
additional information
high expression level of AKR1C26
brenda
high expression level of AKR1C28
brenda
-
cryptorchid testis. AKR1C3 expression is identified at all ages in fibromyocytes surrounding the testicular tubules
brenda
additional information
-
strong immunoreactivity for AKR1C3 not only in classically hormone-associated tissues but also in nonhormone-associated tissues
brenda
additional information
-
in patients with cryptorchid testis, no AKR1C3 expression is seen in germ cells at any stage
brenda
additional information
-
no isoform AKR1C3 immunoreactivity in bronchial glands or alveolar pneumocytes and small cell carcinoma of the lung, only weak immunoreactivity in squamous epithelium of the gastrointestinal junction
brenda
additional information
AKR1C3 is upregulated in leukemia, lung cancers, and carcinomas of hormone-sensitive tissues such as the prostate and mammary gland
brenda
additional information
mRNA for AKR1C34 is expressed liver-specific in female hamsters and ubiquitously in male hamsters
brenda
additional information
J7M9D0
ubiquitous expression in rabbit tissues
brenda
additional information
ubiquitous expression in rabbit tissues
brenda
additional information
ubiquitous expression in rabbit tissues
brenda
additional information
-
ubiquitous expression in rabbit tissues
brenda
additional information
-
strong immunoreactivity for AKR1C3 not only in classically hormone-associated tissues but also in non-hormone-associated tissues
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
mutation of Tyr118 and Phe310 in AKR1C27 to the corresponding residues (Phe and Ile, respectively) in AKR1C28 produces an enzyme that is similar to AKR1C28
physiological function
additional information
evolution
the enzyme is a member of the aldo-keto reductase (AKR) superfamily that metabolizes endogenous substrates, such as carbohydrates, prostaglandins and steroids, and xenobiotics in a NAD(P)(H)-dependent manner
evolution
the enzyme is a member of the aldoketo reductase (AKR) 1C subfamily in the AKR superfamily
evolution
enzyme AKR1C34 is a member of the aldoketo reductase (AKR) 1C subfamily in the AKR superfamily
physiological function
in LNCaP and LNCaP-AKR1C3 cells overexpressing isoform AKR1C3, metabolism proceeds via 5alpha-reduction to form 5alpha-androstane-3,17-dione and then (epi)androsterone-3-glucuronide. LNCaP-AKR1C3 cells make significantly higher amounts of testosterone-17beta-glucuronide. When 5alpha-reductase is inhibited by finasteride, the production of testosterone-17beta-glucuronide is further elevated in LNCaP-AKR1C3 cells. When AKR1C3 activity is inhibited with indomethacin the production of testosterone-17beta-glucuronide is significantly decreased. 4-Androstene-3,17-dione treatment stimulates cell proliferation in both cell lines. LNCaP-AKR1C3 cells are resistant to the growth inhibitory properties of finasteride, consistent with the diversion of 4-androstene-3,17-dione metabolism from 5alpha-reduced androgens to increased formation of testosterone
physiological function
exposure of HCT-15 cells to cisplatin results in aquisition of cisplatin resistance and concomitant induction of isoform AKR1C3 and aldo-keto reductase AKR1C1 expression. The resistance lowers the sensitivity toward cellular damages evoked by oxidative stress-derived aldehydes, 4-hydroxy-2-nonenal and 4-oxo-2-nonenal that are detoxified by AKR1C1 and AKR1C3. Overexpression of AKR1C1 or AKR1C3 in the parental HCT15 cells mitigates the cytotoxicity of the aldehydes and cisplatin. Knockdown of both AKR1C1 and AKR1C3 in the resistant cells or treatment of the cells with specific inhibitors of the aldo-keto reductases increases the sensitivity to ciplatin toxicity
physiological function
crucial role of AKR1C3 in the acquisition of daunorubicin resistance of leukemic cells by metabolizing both daunorubicin and cytotoxic aldehydes derived from ROS-linked lipid peroxidation. Daunorubicin, at its sublethal doses, induces the expression of AKR1C1, EC 1.1.1.149, and AKR1C3, both of which reduce the daunorubicin sensitivity of the cells, AKR1C3 is more inducible than AKR1C1 by the daunorubicin treatment
physiological function
AKR1C3 catalyzes the conversion of the weak androgen precursors 4-androstene-3,17-dione and 5alpha-androstane-3,17-dione to the potent androgens testosterone and 5alpha-dihydrotestosterone (DHT), respectively, and is one of the most highly upregulated genes in castrate-resistant prostate cancer, CRPC
physiological function
aldo-keto reductase 1C3 (AKR1C3), also known as type 5 17beta-hydroxysteroid dehydrogenase, is a downstream steroidogenic enzyme and converts androgen precursors to the potent androgen receptor ligands testosterone and 5alpha-dihydrotestosterone. AKR1C3 is involved in the development of castration resistant prostate cancer (CRPC)
physiological function
enzyme AKR1C34 oxidizes various xenobiotic alicyclic alcohols using NAD+
physiological function
-
key enzyme involved in the degradation of steroid compounds
physiological function
-
key enzyme involved in the degradation of steroid compounds
-
additional information
the structure of the AKR1C3-NADP+ complex is solved by molecular replacement, overview
additional information
J7M9D0
structure analysis by homology modelling, overview
additional information
structure analysis by homology modelling, overview
additional information
structure analysis by homology modelling, overview
additional information
-
structure analysis by homology modelling, overview
additional information
J7M9D0
Tyr118 and Phe310 play key roles in ligand binding. Homology structure modeling of AKR1C27 on the basis of sequence alignment and crystal structure analysis of the AKR1C5 ternary complex, PDB ID 1Q13, overview
additional information
Tyr118 and Phe310 play key roles in ligand binding. Homology structure modeling of AKR1C27 on the basis of sequence alignment and crystal structure analysis of the AKR1C5 ternary complex, PDB ID 1Q13, overview
additional information
Tyr118 and Phe310 play key roles in ligand binding. Homology structure modeling of AKR1C27 on the basis of sequence alignment and crystal structure analysis of the AKR1C5 ternary complex, PDB ID 1Q13, overview
additional information
-
Tyr118 and Phe310 play key roles in ligand binding. Homology structure modeling of AKR1C27 on the basis of sequence alignment and crystal structure analysis of the AKR1C5 ternary complex, PDB ID 1Q13, overview
additional information
J7M9D0
Homology structure modeling of AKR1C28 on the basis of sequence alignment and crystal structure analysis of the AKR1C5 ternary complex, PDB ID 1Q13, overview
additional information
Homology structure modeling of AKR1C28 on the basis of sequence alignment and crystal structure analysis of the AKR1C5 ternary complex, PDB ID 1Q13, overview
additional information
Homology structure modeling of AKR1C28 on the basis of sequence alignment and crystal structure analysis of the AKR1C5 ternary complex, PDB ID 1Q13, overview
additional information
-
Homology structure modeling of AKR1C28 on the basis of sequence alignment and crystal structure analysis of the AKR1C5 ternary complex, PDB ID 1Q13, overview
Show AA Sequence and Transmembrane Helices (1759 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
176000
-
agarose gel chromatography and density gradient centrifugation of Triton X-100 solubilized microsomes
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
10 ns molecular dynamics simulations of inhibitor bound to isofrom AKR1C3. Binding could induce conformational changes to both inhibitor and enzyme. The compound presumably assumes a stable, energetically favored, planar conformation, with an estimated free energy of binding of ?5 kcal/mol
docking of inhibitors (2E)-3-(4-methylphenyl)-2-[4-(methylsulfonyl)phenyl]prop-2-enoic acid, (2E)-3-(4-ethylphenyl)-2-[4-(methylsulfonyl)phenyl]prop-2-enoic acid, (2E)-3-(4-bromophenyl)-2-[4-(methylsulfonyl)phenyl]prop-2-enoic acid and (2E)-3-[4-(methylsulfanyl)phenyl]-2-[4-(methylsulfonyl)phenyl]prop-2-enoic acid to crystal structure. Compounds occupy a similar position of the active site as the co-crystallized indomethacin, with the Aryl1 overlapping with the p-chlorobenzoyl moiety of the indomethacin and the Aryl2 overlapping with an indole part of the indomethacin
in complex with 3-phenoxybenzoic acid, to 1.68 A resolution, space group P212121
in complex with inhibitor 1-(4-[[(2R)-2-methylpiperidin-1-yl]sulfonyl]phenyl)-1,3-dihydro-2H-pyrrol-2-one. The 2-pyrrolidinone does not interact directly with residues in the oxyanion hole
in complex with inhibitor 3-[[4-(trifluoromethyl)phenyl]amino]benzoic acid. Compound adopts a similar binding orientation as flufenamic acid, however, its phenylamino ring projects deeper into a subpocket and confers selectivity over the other AKR1C isoforms
NADP+ and 2'-des-methyl-indomethacin is determined at a resolution of 1.8 A by molecular replacement. The cofactor binding cavity of AKR1C3 is not perturbed upon binding of the inhibitor
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F310I
Y118F
Y118F/F310I
additional information
F310I
site-directed mutagenesis, the mutant shows altered kinetic and substrate specificity compared to the wild-type enzyme
Y118F
site-directed mutagenesis, the mutant shows altered kinetic and substrate specificity compared to the wild-type enzyme
Y118F/F310I
site-directed mutagenesis, the mutant shows altered kinetic and substrate specificity compared to the wild-type enzyme. The double mutation converts AKR1C27 to an enzyme with almost the same substrate specificity and inhibitor sensitivity as those of AKR1C28
Y118F/F310I
site-directed mutagenesis of Tyr118 and Phe310 in AKR1C27 to the corresponding residues (Phe and Ile, respectively) in AKR1C28 produces an enzyme that is similar to AKR1C28, suggesting their key roles in ligand binding
additional information
J7M9D0
a double mutation Y118F/F310I in AKR1C27 converts AKR1C27 to an enzyme with almost the same substrate specificity and inhibitor sensitivity as those of AKR1C28, overview
additional information
a double mutation Y118F/F310I in AKR1C27 converts AKR1C27 to an enzyme with almost the same substrate specificity and inhibitor sensitivity as those of AKR1C28, overview
additional information
a double mutation Y118F/F310I in AKR1C27 converts AKR1C27 to an enzyme with almost the same substrate specificity and inhibitor sensitivity as those of AKR1C28, overview
additional information
-
a double mutation Y118F/F310I in AKR1C27 converts AKR1C27 to an enzyme with almost the same substrate specificity and inhibitor sensitivity as those of AKR1C28, overview
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
43
-
half life of 10 min at pH 10.0, no decrease in activity in the presence of 0.2 mM testosterone, 10% activity lost after 30 min at pH 7.0
45
50
-
20% activity lost after 1 h in the presence of 52.5% glycerol, half-time for heat inactivation 120 min, activity is rapidly lost above 50°C
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stable at 4°C for at least 10-12 days in the presence of 10 mM 2-mercaptoethanol, activity increases 2fold in the first 2-3 days
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 20 mM potassium phosphate, 50% glycerol, 1 mM dithiotreitol, 1 mM EDTA, pH 7.5, 1 year, no loss in activity
-
-80°C, 30 mM Tris-HCl, pH 8.4, 1 mM EDTA, 1 mM dithiothreitol, several months, no loss of activity
-
4°C, 10 mM Tris/HCl buffer, pH 8.0, 5 mM 2-mercaptoethanol, 0.5 mM EDTA
-
4°C, 50 mM Tris-HCl, pH 9.0, 20% glycerol, 100 mM KCl, 5 mg/ml N-octyl glucoside, 24 h, 20% loss of activity, -20°C, 1 week, no loss of activity
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21 (DE3) pLysS by nickel affinity chromatography, ultrafiltration, and dialysis
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography, ultrafiltration, and dialysis
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3) pLysS by nickel affinity chromatography, ultrafiltration, and dialysis
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in HeLa human cervical carcinoma cells and COS-1 monkey kidney tumor cells
-
gene AKR1C26, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)pLysS
gene AKR1C27, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)pLysS
gene AKR1C28, DNA and amino acid sequence determination and analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21 (DE3) pLysS
gene AKR1C28, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) pLysS
gene AKR1C35, cloned from liver, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)pLysS
gene PGER6, DNA and amino acid sequence determination and analysis, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3) pLysS
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
exposure of HCT-15 cells to cisplatin results in aquisition of cisplatin resistance and concomitant induction of isoform AKR1C3 and aldo-keto reductase AKR1C1 expression
LuxR is a negative regulator in the expression of the 3,17beta-HSD gene
marked upregulation of AKR1C3 is found in a subset including hepatocellular, bladder, renal, gastric, and non-small cell lung carcinoma
-
the expression of isoform AKR1C3 is reduced in both hyperplastic and carcinomatous endometrial epithelium
LuxR is a negative regulator in the expression of the 3,17beta-HSD gene
-
LuxR is a negative regulator in the expression of the 3,17beta-HSD gene
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
distribution of human and rat AKR1C3 is comparable but not identical between the two species. These features warrant future studies of AKR1C3 in both hormone- and non-hormone-associated tissues and identification of the rodent homolog for establishing animal models
medicine
-
distribution of human and rat AKR1C3 is comparable but not identical between the two species. These features warrant future studies of AKR1C3 in both hormone- and non-hormone-associated tissues and identification of the rodent homolog for establishing animal models
medicine
-
in patients with cryptorchid testis, AKR1C3 expression occurs in a Tanner stage dependent-fashion. Pre- and peri-pubertal changes appear to promote expression of the enzyme in Leydig cells. In contrast to the normal adult testis, the pediatric cryptorchid testis reveals AKR1C3 expression in Sertoli cells
medicine
-
enzyme is involved in activation of prodrug PR-104A designed to exploit tumor hypoxia. AKR1C3 protein is detected by Western blot in 7 of 23 cell lines and correlates with oxic PR-104A metabolism. AKR1C3 is unable to sensitize cells to 10 other bioreductive prodrugs and is associated with single-agent PR-104 activity across a panel of 9 human tumor xenograft models. Overexpression in two AKR1C3-negative tumor xenograft models strongly enhances PR-104 antitumor activity. Marked upregulation of AKR1C3 is found in a subset including hepatocellular, bladder, renal, gastric, and non-small cell lung carcinoma
medicine
-
establishment of MCF-7 cells that stably express AKR1C3 to model its over-expression in breast cancer. AKR1C3 expression increases steroid conversion by MCF-7 cells, leading to a pro-estrogenic state. Estrone is reduced fastest by MCF-7 cells expressing AKR1C3 when compared to other substrates at 0.1M. MCF-7 cells expressing AKR1C3 cells proliferate three times faster than parental cells in response to estrone and 17-estradiol. MCF-7 cells expressing AKR1C3 cells also reduce PGD2, limiting its dehydration to form PGJ2 products
medicine
uniform, diffuse, and strong expression of isoform AKR1C3 in normal endometrial epithelium but not in endometrial stromal cells. The expression of AKR1C3 is reduced in both hyperplastic and carcinomatous endometrial epithelium
medicine
exposure of HCT-15 cells to cisplatin results in aquisition of cisplatin resistance and concomitant induction of isoform AKR1C3 and aldo-keto reductase AKR1C1 expression. The resistance lowers the sensitivity toward cellular damages evoked by oxidative stress-derived aldehydes, 4-hydroxy-2-nonenal and 4-oxo-2-nonenal that are detoxified by AKR1C1 and AKR1C3. Overexpression of AKR1C1 or AKR1C3 in the parental HCT15 cells mitigates the cytotoxicity of the aldehydes and cisplatin. Knockdown of both AKR1C1 and AKR1C3 in the resistant cells or treatment of the cells with specific inhibitors of the aldo-keto reductases increases the sensitivity to ciplatin toxicity. Pretreatment of the resistant cells with proteasome inhibitor Z-Leu-Leu-Leu-al augments the cisplatin sensitization elicited by aldo-keto reductase inhibitors
medicine
-
positive isoform AKR1C3 immunoreactivity is extensively present in both adenocarcinoma and squamous cell carcinoma arising from the lung and the gastroesophageal junction. Isoform AKR1C3 immunoreactivity is absent in small cell carcinoma of the lung
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REF.
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TITLE
JOURNAL
VOL.
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YEAR
ORGANISM (UNIPROT)
PUBMED ID
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Cavia porcellus
brenda
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-
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Rattus norvegicus
brenda
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Cavia porcellus
-
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235
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Cavia porcellus
brenda
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185
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Bos taurus
brenda
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brenda
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brenda
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Homo sapiens
brenda
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Homo sapiens
brenda
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Homo sapiens
brenda
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Homo sapiens
brenda
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Homo sapiens (P42330), Homo sapiens
brenda
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Homo sapiens (P42330)
brenda
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5
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Homo sapiens (P42330)
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Oryctolagus cuniculus (J7M9D0), Oryctolagus cuniculus (G1T465), Oryctolagus cuniculus (J7MBS9), Oryctolagus cuniculus
brenda
Zang, T.; Verma, K.; Chen, M.; Jin, Y.; Trippier, P.C.; Penning, T.M.
Screening baccharin analogs as selective inhibitors against type 5 17beta-hydroxysteroid dehydrogenase (AKR1C3)
Chem. Biol. Interact.
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Homo sapiens (P42330)
brenda
Endo, S.; Noda, M.; Ikari, A.; Tatematsu, K.; El-Kabbani, O.; Hara, A.; Kitade, Y.; Matsunaga, T.
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158
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Mesocricetus auratus (A0A097ZMY7)
brenda
Ji, Y.; Yang, J.; Gao, L.; Xiong, G.; Yu, Y.; Zhang, Y.
Characterization of a LuxR repressor for 3,17beta-HSD in Comamonas testosteroni ATCC11996
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336
109271
2021
Comamonas testosteroni, Comamonas testosteroni ATCC 11996
brenda
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