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(11S,12S)-11,12-dihydrobenzo[g]chrysene-11,12-diol + NADP+
? + NADPH + H+
enzyme is stereoselective for benzo[g]chrysene-11S,12S-dihydrodiol
-
-
?
17beta-hydroxy-5alpha-androstan-3-one + NAD(P)H + H+
3alpha,17beta-dihydroxy-5alpha-androstan + NAD(P)+
-
-
?
2 tibolone + 2 NADPH + 2 H+
3alpha-hydroxytibolone + 3beta-hydroxytibolone + 2 NADP+
5alpha-androstan-3,17-dione + NAD(P)H
3alpha-hydroxy-5alpha-androstan-17-one + NAD(P)+
-
-
r
benzo[c]phenanthrene-3,4-dihydrodiol + NADP+
? + NADPH + H+
enzyme metabolizes both stereoisomers of benzo[c]phenanthrene-3,4-dihydrodiol
-
-
?
(2Z)-2-(5-hydroxy-4,6-dimethyl-2-oxo-1,2-dihydro-3H-indol-3-ylidene)-N,N-di(prop-2-en-1-yl)hydrazinecarbothioamide + NADPH + H+
?
-
-
-
-
r
(5beta,20R)-20-hydroxypregnan-3-one + NADH + H+
?
-
-
-
-
r
1-(4'nitrophenyl)prop-2-en-1-ol + NAD+
1-(4'nitrophenyl)prop-2-en-1-one + NADH
-
-
-
?
1-(4'nitrophenyl)prop-2-yn-1-ol + NAD+
1-(4'nitrophenyl)prop-2-yn-1-one + NADH
-
-
-
?
1-acenaphthenol + NAD(P)+
1-acenaphthenone + NAD(P)H + H+
-
pH 9.0
-
?
1-acetophenone + NADPH
1-phenylethanol + NADP+
-
-
-
-
?
17beta-hydroxy-5alpha-androstan-3-one + NAD(P)H
5alpha-androstane-3alpha,17beta-diol + NAD(P)+
-
the rate of dihydrotestosterone reduction over back-conversion is 2.4 and 5.9 for prostate and epididymis, respectively
-
r
17beta-hydroxy-5alpha-androstan-3-one + NAD(P)H + H+
3alpha,17beta-dihydroxy-5alpha-androstan + NAD(P)+
17beta-hydroxy-5alpha-androstan-3-one + NADPH
3alpha,17beta-dihydroxy-5alpha-androstan + NADP+
-
-
-
r
2-acetylpyridine + NADPH
1-(2-pyridyl)ethanol + NADP+
-
stereoselective catalysis producing mainly the (S)-alcohols
-
-
?
2-decalone + NADH
? + NAD+
-
pH 6.0
-
?
3-acetylpyridine + NADPH
1-(3-pyridyl)ethanol + NADP+
-
low activity, stereoselective catalysis producing mainly the (S)-alcohols
-
-
?
3alpha,5alpha-allopregnenolone + NAD(P)+
5alpha-dihydroprogesterone + NAD(P)H
3alpha-androstanediol + NAD+
5alpha-dihydrotestosterone + NADH + H+
-
steroid reduction direction is preferred
-
-
r
3alpha-hydroxy-5alpha-androstan-17-one + NAD+
5alpha-androstan-3,17-dione + NADH
4'-methoxyacetophenone + NADPH + H+
1-(4-methoxyphenyl)ethanol + NADP+
-
-
R,S-enantiomeric product
-
?
4-acetylpyridine + NADPH + H+
(S)-1-(4-pyridyl)ethanol + NADP+
-
-
-
-
?
4-acetylpyridine + NADPH + H+
1-(4-pyridyl)ethanol + NADP+
-
stereoselective catalysis producing mainly the (S)-alcohols
-
-
?
4-androsten-3alpha-ol-17-one + NADH + H+
4-androsten-3alpha,17beta-diol + NAD+
-
AKR1C17
-
-
r
4-androstene-3,17-dione + NADH + H+
4-androsten-3alpha-ol-17-one + NAD+
-
low activity
-
-
r
4-bromoacetophenone + NADPH + H+
1-(4-bromophenyl)ethanol + NADP+
-
-
-
-
?
4-cyanoacetophenone + NADPH + H+
1-(4-cyanophenyl)ethanol + NADP+
-
-
-
-
?
4-methylacetophenone + NADPH + H+
1-(4-methylphenyl)ethanol + NADP+
-
-
R,S-enantiomeric product
-
?
4-nitroacetophenone + NAD(P)H
1-(4-nitrophenyl)ethanol + NAD(P)+
-
pH 6.0
-
?
4-nitroacetophenone + NADPH + H+
1-(4-nitrophenyl)ethanol + NADP+
-
-
-
-
?
4-nitrobenzaldehyde + NAD(P)H
(4-nitrophenyl)methanol + NAD(P)+
5alpha-androstan-3,17-dione + NAD(P)H
3alpha-hydroxy-5alpha-androstan-17-one + NAD(P)+
-
pH 6.0 for reduction, pH 7.0 and 9.0 for androsterone oxidation
-
r
5alpha-androstan-3alpha-ol-17-one + NADH + H+
5beta-androstan-3alpha,17beta-diol + NAD+
-
-
-
-
r
5alpha-androstane-3,17-dione + NADH
5alpha-androstan-3alpha-ol-17-one + NAD+
-
low activity
AKR1C9
-
r
5alpha-dihydrotestosterone + NADH
?
-
low activity
-
-
?
5alpha-dihydrotestosterone + NADPH
5alpha-androstane-3alpha,17beta-diol + NADP+
5alpha-dihydrotestosterone + NADPH + H+
3alpha-androstanediol + NADP+
5alpha-pregnan-3,20-dione + NAD(P)H + H+
5alpha-pregnan-3alpha-ol-20-one + NAD(P)+
-
regulation of the amount of allosteric agonists that can bind to the GABA receptor in brain
-
r
5alpha-pregnane-20alpha-ol-3-one + NADH
5alpha-pregnane-3,20alpha-diol + NAD+
-
-
-
-
?
5alpha-pregnane-3,20-dione + NADH
5alpha-pregnan-3alpha-ol-20-one + NAD+
-
low activity
-
-
r
5beta-androstan-3alpha-ol-17-one + NAD(P)+
5beta-androstane-3,17-dione + NAD(P)H
-
-
-
-
r
5beta-androstan-3alpha-ol-17-one + NADH
5beta-androstane-3alpha,17beta-diol + NAD+
-
-
-
-
r
5beta-androstane-3,17-dione + NADH
5beta-androstan-3alpha-ol-17-one + NAD+
-
-
-
-
r
5beta-pregnan-3alpha-ol-20-one + NAD(P)+
5beta-pregnane-3,20-dione + NAD(P)H
-
-
-
-
r
5beta-pregnane-17alpha,20beta,21-triol-3,11-dione + NAD(P)H
5beta-pregnane-3alpha,17alpha,20beta,21-tetraol-11-one + NAD(P)+
5beta-pregnane-20alpha-ol-3-one + NADH + H+
5beta-pregnane-3,20alpha-diol + NAD+
-
-
-
-
?
5beta-pregnane-3,20-dione + NADH + H+
5beta-pregnan-3alpha-ol-20-one + NAD+
-
-
-
-
r
6-tert-butyl-2,3-epoxy-4-hydroxy-5-cyclohexen-1-one + NADH
?
-
the enzyme produces both R- and S-form products in a ratio of 2.3 : 1
-
-
?
7alpha,12alpha-dihydroxy-5beta-cholestan-3-one + NADPH + H+
5beta-cholestane-3alpha,7alpha,12alpha-triol + NADP+
-
-
-
-
?
7alpha-hydroxy-5beta-cholestan-3-one + NADPH + H+
5beta-cholestane-3alpha,7alpha-diol + NADP+
-
-
-
-
?
9,10-phenanthrenequinone + NAD(P)H
? + NAD(P)+
9,10-phenanthrenequinone + NADH
?
-
-
-
-
?
acetophenone + NADPH + H+
1-phenylethanol + NADP+
-
-
-
-
?
androstan-17beta-ol-3-one + NADH
androstan-3alpha,17beta-diol + NAD+
-
-
-
?
androstan-3,17-dione + NADH
androstan-3alpha-ol-17-one + NAD+
-
-
-
?
androsterone + NAD(P)+
5alpha-androstane-3,17-dione + NAD(P)H
-
-
-
-
r
androsterone + NADP+
5alpha-androstane-3,17-dione + NADPH
-
-
-
-
r
benzenedihydrodiol + NAD(P)+
?
-
pH 9.0
-
?
beta-muricholic acid + NADH
?
-
low activity
-
-
?
chenodeoxycholic acid + NADH
?
-
-
-
-
?
cholic acid + NADH
?
-
low activity
-
-
?
dehydrolithocholic acid + NADH + H+
?
-
-
-
-
?
deoxycholic acid + NADH
?
-
low activity
-
-
?
diacetyl + NADH
?
-
-
-
-
?
etiocholane-3,17-dione + NADH
etiocholan-3alpha-ol-17-one + NAD+
-
-
-
?
glycochenodeoxycholic acid + NADH
?
-
-
-
-
?
glycolithocholic acid + NADH
?
-
-
-
-
?
glycoursodeoxycholic acid + NADH
?
-
-
-
-
?
hyodeoxycholic acid + NADH
?
-
low activity
-
-
?
isatin + NADH
?
-
-
-
-
?
lithocholic acid + NADH
?
-
-
-
-
?
murocholic acid + NADH
?
-
low activity
-
-
?
pregnane-11beta,17alpha,21-triol-3,20-dione + NADH
pregnane-3alpha,11beta,17alpha,21-tetrol-20-one + NAD+
-
-
-
?
progesterone + NAD(P)H
3alpha-hydroxy-pregn-4-ene-20-one + NAD(P)+
-
-
-
-
r
prostaglandin + NADP+
? + NADPH
-
types A1, A2, B1, B2, D2, E1, E2, F1, F2alpha and 15-keto-prostaglandinE2 and F2alpha
-
?
prostaglandin-F2alpha + NADP+
prostaglandin F2 + prostaglandin B2 + NADPH
-
-
-
?
taurolithocholic acid + NADH
?
-
-
-
-
?
tauroursodeoxycholic acid + NADH
?
-
-
-
-
?
testosterone + NAD(P)H + H+
4-androsten-3alpha,17beta-diol + NAD(P)+
-
-
-
-
r
testosterone + NADH
?
-
low activity
-
-
?
ursodeoxycholic acid + NADH
?
-
-
-
-
?
additional information
?
-
2 tibolone + 2 NADPH + 2 H+
3alpha-hydroxytibolone + 3beta-hydroxytibolone + 2 NADP+
i.e. tibolone, a 3-ketosteroid androgen receptor, conversion to potent estrogen receptor alpha agonists, tibolone induces estrogen receptor alpha-dependent gene promoter activity through cis-acting estrogen response elements, increases the stimulatory effect of TGF-beta on Smad-dependent gene promoter activity, and enhances prostaglandin E2-induced activity of transcription factor Runx2, overview
3alpha-hydroxytibolone is the primary metabolite
-
r
2 tibolone + 2 NADPH + 2 H+
3alpha-hydroxytibolone + 3beta-hydroxytibolone + 2 NADP+
i.e. tibolone, a 3-ketosteroid androgen receptor, conversion to potent estrogen receptor alpha agonists, overview
3alpha-hydroxytibolone is the primary metabolite
-
r
17beta-hydroxy-5alpha-androstan-3-one + NAD(P)H + H+
3alpha,17beta-dihydroxy-5alpha-androstan + NAD(P)+
-
-
-
?
17beta-hydroxy-5alpha-androstan-3-one + NAD(P)H + H+
3alpha,17beta-dihydroxy-5alpha-androstan + NAD(P)+
-
termination of androgen action
-
?
17beta-hydroxy-5alpha-androstan-3-one + NAD(P)H + H+
3alpha,17beta-dihydroxy-5alpha-androstan + NAD(P)+
-
conversion in animal tissues
-
?
17beta-hydroxy-5alpha-androstan-3-one + NAD(P)H + H+
3alpha,17beta-dihydroxy-5alpha-androstan + NAD(P)+
-
regulation of the amount of androgen in prostate, high levels of substrate are required for normal and abnormal growth of prostate
-
r
3alpha,5alpha-allopregnenolone + NAD(P)+
5alpha-dihydroprogesterone + NAD(P)H
-
i.e. 3alpha,5alpha-tetrahydroprogesterone or 3alpha,5alpha-THP, the enzyme catalyzes the biosynthesis and oxidation of 3alpha,5alpha-reduced neurosteroids as allopregnanolone, which stimulates GABAA receptors, sciatic nerves-induced analgesia results in increased enzyme levels in neuropathic rats, overview
-
-
r
3alpha,5alpha-allopregnenolone + NAD(P)+
5alpha-dihydroprogesterone + NAD(P)H
-
i.e. 3alpha,5alpha-tetrahydroprogesterone or 3alpha,5alpha-THP
-
-
r
3alpha-hydroxy-5alpha-androstan-17-one + NAD+
5alpha-androstan-3,17-dione + NADH
-
-
-
r
3alpha-hydroxy-5alpha-androstan-17-one + NAD+
5alpha-androstan-3,17-dione + NADH
-
-
-
r
3alpha-hydroxy-5alpha-androstan-17-one + NAD+
5alpha-androstan-3,17-dione + NADH
-
-
-
r
3alpha-hydroxy-5alpha-androstan-17-one + NAD+
5alpha-androstan-3,17-dione + NADH
-
pH 9.0
-
?
4-nitrobenzaldehyde + NAD(P)H
(4-nitrophenyl)methanol + NAD(P)+
-
pH 6.0
-
?
4-nitrobenzaldehyde + NAD(P)H
(4-nitrophenyl)methanol + NAD(P)+
-
pH 6.0
-
?
4-nitrobenzaldehyde + NAD(P)H
(4-nitrophenyl)methanol + NAD(P)+
-
NADH as cofactor
-
?
5alpha-dihydrotestosterone + NADPH
5alpha-androstane-3alpha,17beta-diol + NADP+
-
-
-
-
?
5alpha-dihydrotestosterone + NADPH
5alpha-androstane-3alpha,17beta-diol + NADP+
-
i.e. DHT or 5alpha-androstane-17beta-ol-3-one, the reduction reaction is slightly preferred by the wild-type enzyme, which is determined by residue Arg276
i.e. 5alpha-androstane-3alpha,17beta-diol
-
?
5alpha-dihydrotestosterone + NADPH + H+
3alpha-androstanediol + NADP+
-
steroid reduction direction is preferred
-
-
r
5alpha-dihydrotestosterone + NADPH + H+
3alpha-androstanediol + NADP+
-
the chemical oxidation step is rate-limiting, W227 is very important for cataylsis, steroid reduction direction is preferred
-
-
r
5beta-pregnane-17alpha,20beta,21-triol-3,11-dione + NAD(P)H
5beta-pregnane-3alpha,17alpha,20beta,21-tetraol-11-one + NAD(P)+
-
-
-
r
5beta-pregnane-17alpha,20beta,21-triol-3,11-dione + NAD(P)H
5beta-pregnane-3alpha,17alpha,20beta,21-tetraol-11-one + NAD(P)+
-
hepatic reduction in animal tissues
-
?
9,10-phenanthrenequinone + NAD(P)H
? + NAD(P)+
-
NADPH
-
?
9,10-phenanthrenequinone + NAD(P)H
? + NAD(P)+
-
pH 6.0
-
?
9,10-phenanthrenequinone + NAD(P)H
? + NAD(P)+
-
pH 6.0
-
?
additional information
?
-
biosynthesis and inactivation of steroid hormones, physiological role is to inactivate circulating androgens, progestins and glucocorticoids
-
-
?
additional information
?
-
C/EBPdelta regulates the AKR1C9 gene promoter in osteoblasts, overview
-
-
?
additional information
?
-
-
metabolizes androgens and glucocorticoids, function as a dihydrodiol dehydrogenase as well as 9-, 11-, and 15-hydroxyprostaglandin dehydrogenase, enzyme catalyzes both oxidation and reduction reaction at physiological pH and is able to reduce aromatic ketones
-
-
?
additional information
?
-
-
the enzyme displays a distinct preference for the reduction of quinones, e.g. 9,10-phenanthrenequinone, and 3-oxo steroids, e.g. androstane, pregnane and cholane, over aromatic aldehydes and ketones, whereas 3alpha-hydroxy steroids are overwhelmingly more efficiently oxidized than are 1-acenaphthenol or benzenedihydrodiol. Ethanol and 3beta-hydroxy steroids no substrates
-
-
?
additional information
?
-
-
oxidation of 3alpha-hydroxysteroids, secondary alcohols and trans-dihydrodiol proximate carcinogens derived from polycyclic aromatic hydrocarbons, reduction of quinones, aromatic aldehydes and ketones, 9-, 11-, and 15-hydroxyprostaglandin dehydrogenase activity of enzyme
-
-
?
additional information
?
-
-
involved in biosynthesis of bile acids
-
-
?
additional information
?
-
-
inactivating circulating androgens, progestins and glucocorticoids. Regulation of hormone levels in endocrine target tissues and in carcinogen actibation
-
-
?
additional information
?
-
-
no activity with acetylpyrroles
-
-
?
additional information
?
-
-
AKR1C9 catalyzes androgen, estrogen, and prostaglandin metabolism
-
-
?
additional information
?
-
-
acetophenone derivatives are reduced enantioselectively by rat liver 3alpha-HSD to give (S)-alcohols
-
-
?
additional information
?
-
-
substrate specificty, overview, recombinant AKR1C17 efficiently oxidizes 3alpha-hydroxysteroids and diverse bile acids using NAD+ as the preferred coenzyme, no activity with progesterone, cortisone, and aldosterone. The enzyme also reduces non-steroidal alpha-dicarbonyl compounds such as 9,10-phenanethrenequinone, isatin, 6-tert-butyl-2,3-epoxy-4-hydroxy-5-cyclohexen-1-one and diacetyl, but does not show significant activities towards 4-nitrobenzaldehyde and 4-nitroacetophenone
-
-
?
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17beta-hydroxy-5alpha-androstan-3-one + NAD(P)H + H+
3alpha,17beta-dihydroxy-5alpha-androstan + NAD(P)+
-
-
?
2 tibolone + 2 NADPH + 2 H+
3alpha-hydroxytibolone + 3beta-hydroxytibolone + 2 NADP+
i.e. tibolone, a 3-ketosteroid androgen receptor, conversion to potent estrogen receptor alpha agonists, tibolone induces estrogen receptor alpha-dependent gene promoter activity through cis-acting estrogen response elements, increases the stimulatory effect of TGF-beta on Smad-dependent gene promoter activity, and enhances prostaglandin E2-induced activity of transcription factor Runx2, overview
3alpha-hydroxytibolone is the primary metabolite
-
r
17beta-hydroxy-5alpha-androstan-3-one + NAD(P)H + H+
3alpha,17beta-dihydroxy-5alpha-androstan + NAD(P)+
3alpha,5alpha-allopregnenolone + NAD(P)+
5alpha-dihydroprogesterone + NAD(P)H
-
i.e. 3alpha,5alpha-tetrahydroprogesterone or 3alpha,5alpha-THP, the enzyme catalyzes the biosynthesis and oxidation of 3alpha,5alpha-reduced neurosteroids as allopregnanolone, which stimulates GABAA receptors, sciatic nerves-induced analgesia results in increased enzyme levels in neuropathic rats, overview
-
-
r
3alpha-androstanediol + NAD+
5alpha-dihydrotestosterone + NADH + H+
-
steroid reduction direction is preferred
-
-
r
4-acetylpyridine + NADPH + H+
(S)-1-(4-pyridyl)ethanol + NADP+
-
-
-
-
?
5alpha-dihydrotestosterone + NADPH
5alpha-androstane-3alpha,17beta-diol + NADP+
-
-
-
-
?
5alpha-dihydrotestosterone + NADPH + H+
3alpha-androstanediol + NADP+
-
steroid reduction direction is preferred
-
-
r
5alpha-pregnan-3,20-dione + NAD(P)H + H+
5alpha-pregnan-3alpha-ol-20-one + NAD(P)+
-
regulation of the amount of allosteric agonists that can bind to the GABA receptor in brain
-
r
5beta-pregnane-17alpha,20beta,21-triol-3,11-dione + NAD(P)H
5beta-pregnane-3alpha,17alpha,20beta,21-tetraol-11-one + NAD(P)+
-
hepatic reduction in animal tissues
-
?
acetophenone + NADPH + H+
1-phenylethanol + NADP+
-
-
-
-
?
androsterone + NADP+
5alpha-androstane-3,17-dione + NADPH
-
-
-
-
r
additional information
?
-
17beta-hydroxy-5alpha-androstan-3-one + NAD(P)H + H+
3alpha,17beta-dihydroxy-5alpha-androstan + NAD(P)+
-
-
-
?
17beta-hydroxy-5alpha-androstan-3-one + NAD(P)H + H+
3alpha,17beta-dihydroxy-5alpha-androstan + NAD(P)+
-
termination of androgen action
-
?
17beta-hydroxy-5alpha-androstan-3-one + NAD(P)H + H+
3alpha,17beta-dihydroxy-5alpha-androstan + NAD(P)+
-
conversion in animal tissues
-
?
17beta-hydroxy-5alpha-androstan-3-one + NAD(P)H + H+
3alpha,17beta-dihydroxy-5alpha-androstan + NAD(P)+
-
regulation of the amount of androgen in prostate, high levels of substrate are required for normal and abnormal growth of prostate
-
r
additional information
?
-
biosynthesis and inactivation of steroid hormones, physiological role is to inactivate circulating androgens, progestins and glucocorticoids
-
-
?
additional information
?
-
C/EBPdelta regulates the AKR1C9 gene promoter in osteoblasts, overview
-
-
?
additional information
?
-
-
involved in biosynthesis of bile acids
-
-
?
additional information
?
-
-
inactivating circulating androgens, progestins and glucocorticoids. Regulation of hormone levels in endocrine target tissues and in carcinogen actibation
-
-
?
additional information
?
-
-
AKR1C9 catalyzes androgen, estrogen, and prostaglandin metabolism
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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naphthalene-1,2-dione
naphthalene-1,2-dione leads to the time and concentration dependent irreversible inactivation of AKR1C9 via alkylation
(E/Z)-sulfindac
-
wild-type, W86Y and W227Y
1,10-phenanthroline
-
wild-type, W86Y and W227Y
1,7-phenanthroline
-
wild-type, W86Y and W227Y
1-(4'nitrophenyl)prop-2-en-1-ol
-
inactivation dependent on NAD+ concentration, optimal at 0.5-1.0 mM NAD+, 2-mercaptoethanol prvides a concentration-dependent protection
1-(4'nitrophenyl)prop-2-en-1-one
-
inactivation can be retarded markedly in a concentration-dependent manner by both NADH and NADPH. Competitive inhibitor of NAD+ binding, measured for androsterone oxidation
1-(4'nitrophenyl)prop-2-yn-1-one
-
competitive inhibitor of NAD+ binding, measured for androsterone oxidation
17beta-bromoacetoxy-5alpha-dihydrotestosterone
-
inactivation by modification of steroid-binding site
4-androstene-3,17-dione
-
versus substrate, the products, 4-androstene-3,17-dione and NADH, inhibit the activity uncompetitively and competitively, respectively, with respect to NAD+ in the presence of a saturated concentration of 0.004 mM of the substrate
6alpha-Methylprednisolone
-
-
acetaminophen
-
non-competitive, only androsterone oxidation, pH 7.0
acetylenic ketones
-
inactivation by forming Michael adducts with enzyme nucleophiles
-
aspirin
-
salicylate, non-competitive, only androsterone oxidation, pH 7.0
Betamethasone
-
non-competitive
Cu2+
-
100% inhibition at 0.1 mM
D-glucose 6-phosphate
-
-
dexamethasone
-
non-competitive
Flufenamic acid
-
wild-type, W86Y and W227Y
iodoacetate
-
50% inhibition at 0.1 mM
Ketamine
-
specific inhibitor for AKR1C17, but no inhibition of AKR1C9
Mefenamic acid
-
wild-type, W86Y and W227Y
NADH
-
the products, 4-androstene-3,17-dione and NADH, inhibit the activity uncompetitively and competitively, respectively, with respect to NAD+ in the presence of a saturated concentration of 0.004 mM of the substrate
non-steroidal anti-inflamatory drug
-
Oxyphenybutazone
-
competitive
p-chloromercuribenzoate
-
non-competitive with respect to dihydrocortisone 46-100% inhibition at 0.01 mM, preincubation with NADH lowers the inhibitory effect
ponalrestat
-
wild-type, W86Y and W227Y, weak inhibitor
Prednisolone
-
competitive
progesterone
-
competitive to testosterone
prostaglandin A2alpha
-
-
prostaglandin F1alpha
-
-
salicylate
-
non-competitive
Tolmetin
-
competitive, only androsterone oxidation, pH 7.0
Zomepirac
-
competitive, only androsterone oxidation, pH 7.0
additional information
-
not inhibited by dicoumarol, disulfiram and barbiturates. Inhibitory potency of non-steroidal anti-inflamatory drugs and salicylates falls sharply as the pH is increased from 6 to 9
-
indomethacin
-
-
indomethacin
-
non-steroidal anti-inflamatory drug, uncompetitive against NAD+, competitive against androsterone
indomethacin
-
competitive, IC50 for reduction of 9,10-phenanthrenequinone is 0.000735 mM and of androsterone 0.00333 mM
indomethacin
-
wild-type, W86Y and W227Y
Meclofenamic acid
-
competitive
Meclofenamic acid
-
wild-type, W86Y and W227Y
non-steroidal anti-inflamatory drug
-
-
-
non-steroidal anti-inflamatory drug
-
competitive
-
Prostaglandin
-
A2alpha
Prostaglandin
-
A1, B1, E1, F1, F1alpha, A2, B2, E2 and F2alpha, inhibit 9,10-phenanthrenequinone reduction and androsterone oxidation, the order of inhibitory potency is related to their lipophilicity
testosterone
-
competitive inhibitor of androsterone binding
testosterone
-
competitive to progesterone
zopolrestat
-
-
zopolrestat
-
wild-type, W86Y and W227Y, weak inhibitor
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0.0013 - 0.0441
3alpha-hydroxy-5alpha-androstan-17-one
0.0011 - 0.0304
5alpha-androstan-3,17-dione
0.0027
(5beta,20R)-20-hydroxypregnan-3-one
-
pH 7.4, 25°C, recombinant wild-type AKR1C17
0.0012 - 0.726
17beta-hydroxy-5alpha-androstan-3-one
3.54 - 33.7
2-decalone
-
-
0.029 - 0.408
3alpha-hydroxy-5alpha-androstan-17-one
0.163 - 0.211
4-nitrobenzaldehyde
-
-
0.0017 - 0.0042
5alpha-androstan-3,17-dione
0.00065
5alpha-androstane-3,17-dione
-
pH 7.0, 25, reduction reaction
0.781 - 7.331
5alpha-androstane-3alpha,17beta-diol
0.0021
5beta-androstane-3,17-dione
-
pH 7.4, 25°C, recombinant wild-type AKR1C17
0.01
5beta-pregnane-17alpha,20beta,21-triol-3,11-dione
-
-
0.0024
5beta-pregnane-3,20-dione
-
pH 7.4, 25°C, recombinant wild-type AKR1C17
0.023
6-tert-butyl-2,3-epoxy-4-hydroxy-5-cyclohexen-1-one
-
pH 7.4, 25°C, recombinant wild-type AKR1C17
0.00122 - 0.038
9,10-phenanthrenequinone
0.0041
androsterone
-
pH 7.0, 25, oxidation reaction
0.004
Dehydrolithocholic acid
-
pH 7.4, 25°C, recombinant wild-type AKR1C17
0.42
diacetyl
-
pH 7.4, 25°C, recombinant wild-type AKR1C17
0.022
isatin
-
pH 7.4, 25°C, recombinant wild-type AKR1C17
additional information
(11S,12S)-11,12-dihydrobenzo[g]chrysene-11,12-diol
0.0013 - 0.0441
3alpha-hydroxy-5alpha-androstan-17-one
NAD+
0.0041 - 0.024
3alpha-hydroxy-5alpha-androstan-17-one
NADP+
0.0011 - 0.0039
5alpha-androstan-3,17-dione
NADPH
0.0039 - 0.0304
5alpha-androstan-3,17-dione
NADH
0.0012
17beta-hydroxy-5alpha-androstan-3-one
-
cloned human liver enzyme type I
0.0192
17beta-hydroxy-5alpha-androstan-3-one
-
cloned human liver enzyme type II
0.505
17beta-hydroxy-5alpha-androstan-3-one
-
NAD(H), prostate
0.614
17beta-hydroxy-5alpha-androstan-3-one
-
NADP(H), prostate
0.645
17beta-hydroxy-5alpha-androstan-3-one
-
NADP(H), epididymis
0.726
17beta-hydroxy-5alpha-androstan-3-one
-
NAD(H), epididymis
0.029
3alpha-hydroxy-5alpha-androstan-17-one
-
Y205F
0.042 - 0.408
3alpha-hydroxy-5alpha-androstan-17-one
-
-
0.046
3alpha-hydroxy-5alpha-androstan-17-one
-
recombinant wild type enzyme
0.047
3alpha-hydroxy-5alpha-androstan-17-one
-
-
0.0017
5alpha-androstan-3,17-dione
-
-
0.0041
5alpha-androstan-3,17-dione
-
recombinant wild type enzyme
0.0042
5alpha-androstan-3,17-dione
-
Y205F
0.781
5alpha-androstane-3alpha,17beta-diol
-
NAD(H), prostate
1.09
5alpha-androstane-3alpha,17beta-diol
-
NADP(H), prostate
3.042
5alpha-androstane-3alpha,17beta-diol
-
NAD(H), epididymis
7.331
5alpha-androstane-3alpha,17beta-diol
-
NADP(H), epididymis
0.00122 - 0.0051
9,10-phenanthrenequinone
-
-
0.038
9,10-phenanthrenequinone
-
pH 7.4, 25°C, recombinant wild-type AKR1C17
0.04
NAD+
-
-
0.94
NAD+
-
recombinant wild type enzyme
0.015
NADH
-
-
0.027
NADH
-
recombinant wild type enzyme
additional information
(11S,12S)-11,12-dihydrobenzo[g]chrysene-11,12-diol
racemic benzo[g]chrysene-11,12-dihydrodiol derived from the fjord-region parent hydrocarbon benzo[g]chrysene is oxidized with a kcat/Km of 1520 min/mM, which is more than 100 times greater than that observed with benzo[a]pyrene-7,8-dihydrodiol
additional information
benzo[a]pyrene-7,8-dihydrodiol
kcat/Km of 39 min/mM
additional information
additional information
-
kinetics
-
additional information
additional information
-
transient-state and steady-state kinetics
-
additional information
additional information
-
equilibrium kinetics of wild-type and mutant enzymes
-
additional information
additional information
-
stereoselectivity, kinetics
-
additional information
additional information
-
cofactor kinetics of wild-type and mutant enzymes, overview
-
additional information
additional information
-
steady-state, transient state kinetics, and kinetic isotope effects, kinetic analysis and mechanism, ordered bi-bi mechanism, detailed overview
-
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0.00063 - 0.85
(2Z)-2-(5-hydroxy-4,6-dimethyl-2-oxo-1,2-dihydro-3H-indol-3-ylidene)-N,N-di(prop-2-en-1-yl)hydrazinecarbothioamide
0.115
(5beta,20R)-20-hydroxypregnan-3-one
-
pH 7.4, 25°C, recombinant wild-type AKR1C17
1.13 - 1.25
3alpha-hydroxy-5alpha-androstan-17-one
0.267 - 0.283
5alpha-androstan-3,17-dione
0.42
5alpha-androstane-3,17-dione
-
pH 7.0, 25, reduction reaction
0.037 - 0.43
5alpha-dihydroprogesterone
0.047
5beta-androstane-3,17-dione
-
pH 7.4, 25°C, recombinant wild-type AKR1C17
0.105
5beta-pregnane-3,20-dione
-
pH 7.4, 25°C, recombinant wild-type AKR1C17
0.1
6-tert-butyl-2,3-epoxy-4-hydroxy-5-cyclohexen-1-one
-
pH 7.4, 25°C, recombinant wild-type AKR1C17
0.183 - 3.93
9,10-phenanthrenequinone
0.0053 - 0.83
androsterone
0.022
Dehydrolithocholic acid
-
pH 7.4, 25°C, recombinant wild-type AKR1C17
0.167
diacetyl
-
pH 7.4, 25°C, recombinant wild-type AKR1C17
0.283
isatin
-
pH 7.4, 25°C, recombinant wild-type AKR1C17
additional information
additional information
-
0.00063
(2Z)-2-(5-hydroxy-4,6-dimethyl-2-oxo-1,2-dihydro-3H-indol-3-ylidene)-N,N-di(prop-2-en-1-yl)hydrazinecarbothioamide
-
cofactor NADP+, pH 7.0, 25°C, steroid oxidation, recombinant mutant W227A
0.37
(2Z)-2-(5-hydroxy-4,6-dimethyl-2-oxo-1,2-dihydro-3H-indol-3-ylidene)-N,N-di(prop-2-en-1-yl)hydrazinecarbothioamide
-
cofactor NADP+, pH 7.0, 25°C, steroid oxidation, recombinant wild-type enzyme
0.8
(2Z)-2-(5-hydroxy-4,6-dimethyl-2-oxo-1,2-dihydro-3H-indol-3-ylidene)-N,N-di(prop-2-en-1-yl)hydrazinecarbothioamide
-
cofactor NADP+, pH 7.0, 25°C, steroid oxidation, recombinant mutant R276M
0.85
(2Z)-2-(5-hydroxy-4,6-dimethyl-2-oxo-1,2-dihydro-3H-indol-3-ylidene)-N,N-di(prop-2-en-1-yl)hydrazinecarbothioamide
-
cofactor NAD+, pH 7.0, 25°C, steroid oxidation, recombinant wild-type enzyme
1.13
3alpha-hydroxy-5alpha-androstan-17-one
-
Y205F
1.25
3alpha-hydroxy-5alpha-androstan-17-one
-
recombinant wild type enzyme
0.267
5alpha-androstan-3,17-dione
-
Y205F
0.283
5alpha-androstan-3,17-dione
-
recombinant wild type enzyme
0.037
5alpha-dihydroprogesterone
-
cofactor NADPH, pH 7.0, 25°C, steroid reduction, recombinant mutant W227A
0.3
5alpha-dihydroprogesterone
-
cofactor NADPH, pH 7.0, 25°C, steroid reduction, recombinant wild-type enzyme
0.4
5alpha-dihydroprogesterone
-
cofactor NADPH, pH 7.0, 25°C, steroid reduction, recombinant mutant R276M
0.43
5alpha-dihydroprogesterone
-
cofactor NADH, pH 7.0, 25°C, steroid reduction, recombinant wild-type enzyme
0.183
9,10-phenanthrenequinone
-
pH 7.4, 25°C, recombinant wild-type AKR1C17
1.17 - 3.93
9,10-phenanthrenequinone
-
-
0.0053
androsterone
-
steady-state, pH 8.0, 25°C, recombinant mutant W227A
0.0083
androsterone
-
steady-state, pH 8.0, 25°C, recombinant mutant F118A
0.57
androsterone
-
steady-state, pH 8.0, 25°C, recombinant mutant T226A
0.82
androsterone
-
pH 7.0, 25, oxidation reaction
0.83
androsterone
-
steady-state, pH 8.0, 25°C, recombinant wild-type enzyme
1.13
NAD+
-
recombinant wild type enzyme
0.283
NADH
-
recombinant wild type enzyme
additional information
additional information
-
kcat in steady-state, single turnover, burst in multiple turnover, steady-state in multiple turnover
-
additional information
additional information
-
single turnover, and multiple burst and steady-state in turnover, kinetic isotope effects with 4-pro-R-[2H]-NADPH on recombinant wild-type and mutant enzymes
-
additional information
additional information
-
cofactor kinetics of wild-type and mutant enzymes, overview
-
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F118A
largest changes in kcat/Km
F129A
largest changes in kcat/Km, F129A alters the stereochemical preference from oxidizing predominantly the S,S-stereoisomer to oxidizing predominantly the R,R-stereoisomer of benzo[g]chrysene-11,12-dihydrodiol
L54A
mutant shows intermediate changes in kcat/Km versus wild type
N167A
site-directed mutagenesis, most impaired enzyme
N306A
mutant shows intermediate changes in kcat/Km versus wild type
Q190A
site-directed mutagenesis, decreased binding affinity to NADP(H), only binding of cofactor is affected, residue is located at the catalytic cente
R276M
elimination of salt bridge between Arg276 and the 2'-phosphate of AMP results in 100fold decrease of the affinity to NADP(H)
S166A
site-directed mutagenesis, decreased binding affinity to NADP(H), only binding of cofactor is affected, residue is located at the catalytic center
T226A
smallest change in kcat/Km is observed when alanine is used to substitute hydrophilic residues
T24A
smallest change in kcat/Km is observed when alanine is used to substitute hydrophilic residues
W227A
largest changes in kcat/Km
Y216S
site-directed mutagenesis, decreased binding affinity to NADP(H), only binding of cofactor is affected, residue is located at the catalytic cente
Y310A
mutant shows intermediate changes in kcat/Km versus wild type
C217A
-
resistant to inactivation by secosteroids, therefore Cys217 is the point of covalent attachment of acetylenic ketones
D50E
-
1/30th catalytic efficiency of wild type, unlikely to be the general amino acid for catalysis
D50N
-
1/30th catalytic efficiency of wild type, unlikely to be the general amino acid for catalysis
E276R
-
site-directed mutagenesis, the mutation alters the cofactor specificity of AKR1C17 from NAD+ to NADP+, the switch is analogy th the residues of AKRc9 and its cofactor specificity, overview
F118A
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme, effects of mutation on binding constants and kinetics, overview
F129A
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme, effects of mutation on binding constants and kinetics, overview
H117A
-
1/500th catalytic efficiency of wild type, unlikely to be the general amino acid for catalysis
K84M
-
inactive, unable to bind steroids
K84R
-
inactive, unable to bind steroids
L54A
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme, effects of mutation on binding constants and kinetics, overview
N306A
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme, effects of mutation on binding constants and kinetics, overview
Q270K
-
site-directed mutagenesis, the mutation alters the cofactor specificity of AKR1C17 from NAD+ to NADP+, the switch is analogy th the residues of AKRc9 and its cofactor specificity, overview
Q270K/E276R
-
site-directed mutagenesis, the mutation alters the cofactor specificity of AKR1C17 from NAD+ to NADP+, the switch is analogy th the residues of AKRc9 and its cofactor specificity, overview
R276E
-
site-directed mutagenesis, the mutant shows increased preference for the oxidation reaction compared to the wild-type enzyme
R276G
-
site-directed mutagenesis, the mutant shows slightly increased preference for the reduction reaction compared to the wild-type enzyme
T226A
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme, effects of mutation on binding constants and kinetics, overview
T24A
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme, effects of mutation on binding constants and kinetics, overview
Y205F
-
kinetically indistinguishable from the wild type, no general amino acid for catalysis in 3alpha-hydroxysteroid dehydrogenase
Y310A
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme, effects of mutation on binding constants and kinetics, overview
Y55F
-
inactive, unable to perform steroid oxidoreduction, strongest candidate for the general amino acid
Y55S
-
inactive, strongest candidate for the general amino acid
additional information
-
positions of Tyr/Lys pair are conserved across the aldo-keto reductase and short-chain dehydrogenase/reductase family. Tyr retains ability to form ternary complex and acts as general acid
R276M
-
site-directed mutagenesis, mutant does no longer form a salt-linkage to the phosphate of 2'-AMP, and does no longer bind tightly to NAD(P)H, the burst phase kinetics for the NADP+-dependent oxidation of 3alpha-diol is eliminated
R276M
-
site-directed mutagenesis, the mutant shows slightly increased preference for the reduction reaction compared to the wild-type enzyme
W148Y
-
site-directed mutagenesis, kinetically similar to wild type enzyme, no function in ligand binding
W148Y
-
can catalyse steroid oxidoreduction similar to wild type, plays no role in steroid binding or catalysis
W227A
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme, 23fold decreased affinity for progesterone, effects of mutation on binding constants and kinetics, overview
W227A
-
site-directed mutagenesis, highly reduced activity compared to the wild-type, very slow chemical transformation
W227Y
-
site-directed mutagenesis, important role in binding steroid hormones, but not small substrates or inhibitors, interacts with the C and/or D-rings of steroid ligand
W227Y
-
mainly influenced in steroid binding
W86Y
-
site-directed mutagenesis, important in binding steroids and non-steroidal anti-inflamatory drugs, region in which it resides is part of the substrate/inhibitor binding pocket, near the A-, and B-rings of bound steroid
W86Y
-
plays role in cofactor and steroid binding
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Askonas, L.J.; Ricigliano, J.W.; Penning, T.M.
The kinetic mechanism catalysed by homogeneous rat liver 3alpha-hydroxysteroid dehydrogenase. Evidence for binary and ternary dead-end complexes containing non-steroidal anti-inflammatory drugs
Biochem. J.
278
835-841
1991
Rattus norvegicus
brenda
Penning, T.M.; Sharp, R.B
Prostaglandin dehydrogenase activity of purified rat liver 3alpha-hydroxysteroid dehydrogenase
Biochem. Biophys. Res. Commun.
148
646-652
1987
Rattus norvegicus
brenda
Pawlowski, J.E.; Huizinga, M.; Penning, T.M.
Cloning and sequencing of the cDNA for rat liver 3alpha-hydroxysteroid/dihydrodiol dehydrogenase
J. Biol. Chem.
266
8820-8825
1991
Rattus norvegicus, Rattus norvegicus Sprangue-Dawley
brenda
Penning, T.M.; Mukharji, I.; Barrows, S.; Talalay, P.
Purification and properties of a 3alpha-hydroxysteroid dehydrogenase of rat liver cytosol and its inhibition by anti-inflammatory drugs
Biochem. J.
222
601-611
1984
Rattus norvegicus, Rattus norvegicus Sprangue-Dawley
brenda
Tomkins, G.M.
A mammalian 3alpha-hydroxysteroid dehydrogenase
J. Biol. Chem.
218
437-447
1956
Rattus norvegicus
brenda
Ricigliano, J.W.; Penning, T.M.
Evidence that enzyme-generated aromatic Michael acceptors covalently modify the nucleotide-binding site of 3alpha-hydroxysteroid dehydrogenase
Biochem. J.
269
749-755
1990
Rattus norvegicus, Rattus norvegicus Sprangue-Dawley
brenda
Span, P.N.; Sweep, C.G.J.; Benraad, T.J.; Smals, A.G.H.
3alpha-Hydroxysteroid oxidoreductase activities in dihydrotestosterone degradation and back-formation in rat prostate and epididymis
J. Steroid Biochem. Mol. Biol.
58
319-324
1996
Rattus norvegicus
brenda
Jez, J.M.; Schlegel, B.P.; Penning, T.M.
Characterization of the substrate binding site in rat liver 3alpha-hydroxysteroid/dihydrodiol dehydrogenase. The roles of tryptophans in ligand binding and protein fluorescence
J. Biol. Chem.
271
30190-30198
1996
Rattus norvegicus
brenda
Penning, T.M.; Bennett, M.J.; Smith-Hoog, S.; Schlegel, B.P.; Jez, J.M.; Lewis, M.
Structure and function of 3alpha-hydroxysteroid dehydrogenase
Steroids
62
101-111
1997
Rattus norvegicus
brenda
Ma, H.; Ratnam, K.; Penning, T.M.
Mutation of nicotinamide pocket residues in rat liver 3alpha-hydroxysteroid dehydrogenase reveals different modes of cofactor binding
Biochemistry
39
102-109
2000
Rattus norvegicus (P23457)
brenda
Heredia, V.V.; Penning, T.M.
Dissection of the physiological interconversion of 5alpha-DHT and 3alpha-diol by rat 3alpha-HSD via transient kinetics shows that the chemical step is rate-determining: effect of mutating cofactor and substrate-binding pocket residues on catalysis
Biochemistry
43
12028-12037
2004
Rattus norvegicus
brenda
Heredia, V.V.; Cooper, W.C.; Kruger, R.G.; Jin, Y.; Penning, T.M.
Alanine scanning mutagenesis of the testosterone binding site of rat 3alpha-hydroxysteroid dehydrogenase demonstrates contact residues influence the rate-determining step
Biochemistry
43
5832-5841
2004
Rattus norvegicus
brenda
Uwai, K.; Konno, N.; Kitamura, S.; Ohta, S.; Takeshita, M.
Purification and characterization of rat liver enzyme catalyzing stereoselective reduction of acetylpyridines
Chirality
17
494-500
2005
Rattus norvegicus
brenda
Papari-Zareei, M.; Brandmaier, A.; Auchus, R.J.
Arginine 276 controls the directional preference of AKR1C9 (rat liver 3alpha-hydroxysteroid dehydrogenase) in human embryonic kidney 293 cells
Endocrinology
147
1591-1597
2006
Rattus norvegicus
brenda
Sanai, M.; Endo, S.; Matsunaga, T.; Ishikura, S.; Tajima, K.; El-Kabbani, O.; Hara, A.
Rat NAD+-dependent 3alpha-hydroxysteroid dehydrogenase (AKR1C17): a member of the aldo-keto reductase family highly expressed in kidney cytosol
Arch. Biochem. Biophys.
464
122-129
2007
Rattus norvegicus
brenda
Uwai, K.; Konno, N.; Yasuta, Y.; Takeshita, M.
Electronic effects of para-substitution on acetophenones in the reaction of rat liver 3alpha-hydroxysteroid dehydrogenase
Bioorg. Med. Chem.
16
1084-1089
2008
Rattus norvegicus
brenda
Cooper, W.C.; Jin, Y.; Penning, T.M.
Elucidation of a complete kinetic mechanism for a mammalian hydroxysteroid dehydrogenase (HSD) and identification of all enzyme forms on the reaction coordinate: the example of rat liver 3alpha-HSD (AKR1C9)
J. Biol. Chem.
282
33484-33493
2007
Rattus norvegicus
brenda
McCarthy, T.L.; Hochberg, R.B.; Labaree, D.C.; Centrella, M.
3-ketosteroid reductase activity and expression by fetal rat osteoblasts
J. Biol. Chem.
282
34003-34012
2007
Rattus norvegicus (P23457)
brenda
Azzarello, J.; Fung, K.M.; Lin, H.K.
Tissue distribution of human AKR1C3 and rat homolog in adult genitourinary system
J. Histochem. Cytochem.
56
853-861
2008
Homo sapiens, Rattus norvegicus
brenda
Meyer, L.; Venard, C.; Schaeffer, V.; Patte-Mensah, C.; Mensah-Nyagan, A.G.
The biological activity of 3alpha-hydroxysteroid oxido-reductase in the spinal cord regulates thermal and mechanical pain thresholds after sciatic nerve injury
Neurobiol. Dis.
30
30-41
2008
Rattus norvegicus
brenda
Shultz, C.A.; Palackal, N.T.; Mangal, D.; Harvey, R.G.; Blair, I.A.; Penning, T.M.
Fjord-region benzo[g]chrysene-11,12-dihydrodiol and benzo[c]phenanthrene-3,4-dihydrodiol as substrates for rat liver dihydrodiol dehydrogenase (AKR1C9): structural basis for stereochemical preference
Chem. Res. Toxicol.
21
668-677
2008
Rattus norvegicus (P23457)
brenda
Bjrkhem, I.; Danielsson, H.
Stereochemistry of hydrogen transfer from pyridine nucleotides catalyzed by delta-4-3-oxosteroid 5-beta-reductase and 3-alpha-hydroxysteroid dehydrogenase from rat liver
Eur. J. Biochem.
12
80-4
1970
Rattus norvegicus
brenda