1.1.1.62: 17beta-estradiol 17-dehydrogenase

This is an abbreviated version, for detailed information about 17beta-estradiol 17-dehydrogenase, go to the full flat file.

Reaction

17beta-estradiol
+
NAD(P)+
=
estrone
+
NAD(P)H
+
H+

Synonyms

(17beta-HSD) type 1, (17beta-HSD) type 2, 17-beta-HSD 2, 17-beta-hydroxysteroid dehydrogenase type 12, 17-beta-hydroxysteroid dehydrogenase type 2, 17-HOR, 17-HSD, 17beta HSD1, 17beta,20alpha-hydroxysteroid dehydrogenase, 17beta-estradiol dehydrogenase, 17beta-HSD, 17beta-HSD I, 17beta-HSD type 1, 17beta-HSD type 12, 17beta-HSD type 2, 17beta-HSD type 4, 17beta-HSD type 5, 17beta-HSD type 7, 17beta-HSD type 8, 17beta-HSD1, 17beta-HSD12, 17beta-HSD2, 17beta-HSD4, 17beta-HSD5, 17beta-HSD7 2, 17beta-HSDcl, 17beta-hydroxysteroid dehydrogenase, 17beta-hydroxysteroid dehydrogenase 4, 17beta-hydroxysteroid dehydrogenase type 1, 17beta-hydroxysteroid dehydrogenase type 12, 17beta-hydroxysteroid dehydrogenase type 2, 17beta-hydroxysteroid dehydrogenase type 4, 17beta-hydroxysteroid dehydrogenase type 5, 17beta-hydroxysteroid dehydrogenase type 6, 17beta-hydroxysteroid dehydrogenase type 7, 17beta-hydroxysteroid dehydrogenase type 8, 17beta-hydroxysteroid dehydrogenase type I, 17beta-hydroxysteroid dehydrogenase types 1, 17beta-hydroxysteroid dehydrogenases type 1, 17betaHSD, 17betaHSD1, 17betaHSD14, 17betaHSD6, 17HSD1, 20 alpha-hydroxysteroid dehydrogenase, 20-alpha-HSD, 20alpha-hydroxysteroid dehydrogenase, 3beta-HSD, 3beta-hydroxysteroid dehydrogenase, 3betaHSD, 7beta-HSD type 1, AKR1C1, AKR1C2, AKR1C3, AKR1C4, dehydrogenase, estradiol 17beta-, E2DH, EDH, estradiol 17beta-dehydrogenase, estradiol dehydrogenase, estrogen 17-oxidoreductase, estrogenic 17beta-hydroxysteroid dehydrogenase, form 2 type 7 17beta-hydroxysteroid dehydrogenase, HSD17B1, HSD17B12, HSD17B2, HSD17B4, hydroxysteroid (17-beta) dehydrogenase 1, Ke6 protein, mf17beta-HSD12, microsomal 17-beta-hydroxysteroid dehydrogenase, More, oestradiol-17beta hydroxysteroid dehydrogenase, placental 17-beta-hydroxysteroid dehydrogenase, PRAP, PRL receptor associated protein, testicular 17-beta-hydroxysteroid dehydrogenase, type 1 17beta-HSD, type 1 17beta-hydroxysteroid dehydrogenase, type 12 17beta-HSD, type 12 17beta-hydroxysteroid dehydrogenase, type 7 17beta-hydroxysteroid dehydrogenase, type 8 17beta-HSD, type 8 17beta-hydroxysteroid dehydrogenase

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.62 17beta-estradiol 17-dehydrogenase

Engineering

Engineering on EC 1.1.1.62 - 17beta-estradiol 17-dehydrogenase

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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A50R
-
site-directed mutagenesis, the mutant shows increased rates of NADPH dissociation and thus enhanced substrate oxidation with NADP+ compared to the wild-type enzyme
H111A
-
site-directed mutagenesis, the mutant is dimeric like the wild-type enzyme, inactive mutant
H111L
-
site-directed mutagenesis, the mutation renders the enzyme monomeric, inactive mutant
H164G
mutation results in a conformation of the enzyme that possesses a higher catalytic activity
H164W
mutation results in a conformation of the enzyme that possesses a higher catalytic activity
N51R
-
site-directed mutagenesis, the mutant shows increased rates of NADP+ dissociation and thus enhanced substrate reduction with NADPH compared to the wild-type enzyme
R129D
-
site-directed mutagenesis, the mutation renders the enzyme monomeric, the mutant shows reduced activity compared to the wild-type enzyme
T202I
-
site-directed mutagenesis, inactive mutant due to cofactor binding deficiency
T202V
-
site-directed mutagenesis, inactive mutant due to cofactor binding deficiency
V161G
mutation increases the initial rates for the conversion of androstenedione to testosterone
Y212A
mutation increases the initial rates for the conversion of androstenedione to testosterone
A170E/F172E
-
no detectable activity
H210A/H213A
-
decreased activity
H221A
-
catalytic efficiency is reduced 20fold for oxidative reaction and 11fold for the reductive reaction
K159A
-
almost inactive enzyme, catalytic efficiencies of the substituted enzyme are more than 200fold lower for both reduction and oxidation compared with the values measured for the wild type enzyme
L111E/V113F
-
no detectable activity
S142A
-
almost inactive enzyme, catalytic efficiencies of the substituted enzyme are more than 200fold lower for both reduction and oxidation compared with the values measured for the wild type enzyme
Y155A
-
decreased activity
additional information
-
deleting the last 36 amino acids does not have a dramatic effect on the catalytic properties