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1.3.1.3: DELTA4-3-oxosteroid 5beta-reductase

This is an abbreviated version!
For detailed information about DELTA4-3-oxosteroid 5beta-reductase, go to the full flat file.

Word Map on EC 1.3.1.3

Reaction

17,21-dihydroxy-5beta-pregnane-3,11,20-trione
+
NADP+
=
cortisone
+
NADPH
+
H+

Synonyms

3-oxo-DELTA4-steroid 5beta-reductase, 4,5beta-dihydrocortisone:NADP+ DELTA4-oxidoreductase, 5-beta-reductase, 5beta-POR, 5beta-red, AKR1D1, AKR1D4, aldo-keto reductase, aldo-keto reductase 1D1, aldo–keto reductase 1D1, androstenedione 5beta-reductase, CARUB_v10005016mg, cortisone 5beta-reductase, cortisone beta-reductase, DELTA 4-5beta-reductase, DELTA4-3-ketosteroid 5beta-reductase, DELTA4-3-oxosteroid 5beta-reductase, DELTA4-hydrogenase, EC 1.3.1.23, EC 1.3.1.3, h5beta-red, h5beta-reductase, More, P5betaR, progesterone 5beta-reductase, reductase, cholestenone 5beta.-, reductase, cortisone DELTA4-5beta-, SRD5beta, St5betaR1, steroid 5beta-reductase, steroid 5beta.-reductase, testosterone 5-beta-reductase, testosterone 5beta-reductase

ECTree

     1 Oxidoreductases
         1.3 Acting on the CH-CH group of donors
             1.3.1 With NAD+ or NADP+ as acceptor
                1.3.1.3 DELTA4-3-oxosteroid 5beta-reductase

Engineering

Engineering on EC 1.3.1.3 - DELTA4-3-oxosteroid 5beta-reductase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Y132G
-
10% increase in catalytic efficiency
Y132G/V309K
-
loss of activity
Y132G/V309W
-
loss of activity
R63K
mutant is able to use NADH as cofactor
R63K/R64H
increases enzymatic activity by 13.8fold with NADH as cofactor
R64G
mutant exhibits significantly improved activity with NADH
R64H
mutant exhibits significantly improved activity with NADH
R64S
mutant exhibits significantly improved activity with NADH
R64T
mutant exhibits significantly improved activity with NADH
C352G
-
site-directed mutagenesis, mutation at the substrate binding site, the mutant shows reduced activity compared to the wild-type enzyme
D181T/L182Q
-
site-directed mutagenesis, mutation at motif V, the mutant shows reduced activity compared to the wild-type enzyme
F353M
-
site-directed mutagenesis, mutation at the substrate binding site, the mutant shows similar activity as the wild-type enzyme
F353P
-
site-directed mutagenesis, mutation at the substrate binding site, the mutant shows similar activity as the wild-type enzyme
G204N
-
site-directed mutagenesis, mutation at motif IV, the mutant shows reduced activity compared to the wild-type enzyme
L182Q
-
site-directed mutagenesis, mutation at motif V, the mutant shows similar activity as the wild-type enzyme
M150L
-
site-directed mutagenesis, mutation at motif IV, the mutant shows similar activity as the wild-type enzyme
N205A
-
site-directed mutagenesis, mutation at the substrate binding site, the mutant shows increased activity compared to the wild-type enzyme
N205M
-
site-directed mutagenesis, mutation at the substrate binding site, the mutant shows increased activity compared to the wild-type enzyme
N205M/Y156V
-
site-directed mutagenesis, double mutation at the substrate binding site, the mutant shows increased activity compared to the wild-type enzyme
R146T
-
site-directed mutagenesis, mutation at motif IV, the mutant shows similar activity as the wild-type enzyme
S248M
-
site-directed mutagenesis, mutation near the substrate binding site, inactive mutant
T65P
-
site-directed mutagenesis, mutation at near motif II, the mutant shows similar activity as the wild-type enzyme
Y156V
-
site-directed mutagenesis, mutation at the substrate binding site, the mutant shows increased activity compared to the wild-type enzyme
Y179A
inactive
Y179F
inactive
Y302F
-
site-directed mutagenesis, mutation at motif IV, the mutant shows similar activity as the wild-type enzyme
E120A
-
mutant is devoid of activity
G223E
L106F
P133R
P198L
R217stop
the naturally occuring mutation of gene SRD5B1 are involved in hyper-3-oxo-DELTA4 bile aciduria from primary 3-oxo-DELTA4-steroid 5beta-reductase deficiency, phenotypes, overview
R261C
V309F
replacement of one of the residues delineating this site by a phenylalanine completely abolishes the enzyme's substrate inhibition, but the catalytic efficiency of the mutated enzyme is similar to that of the wild-type h5beta-red enzyme
Y132F
replacement of one of the residues delineating this site by a phenylalanine completely abolishes the enzyme's substrate inhibition, but the catalytic efficiency of the mutated enzyme is similar to that of the wild-type h5beta-red enzyme
Y58F
-
mutant is devoid of activity
additional information