1.1.1.35: 3-hydroxyacyl-CoA dehydrogenase

This is an abbreviated version, for detailed information about 3-hydroxyacyl-CoA dehydrogenase, go to the full flat file.

Reaction

(S)-3-hydroxyacyl-CoA
+
NAD+
=
3-oxoacyl-CoA
+
NADH
+
H+

Synonyms

(S)-3-hydroxyacyl-CoA dehydrogenase/enoyl-CoA hydratase, (S)-3-hydroxybutyryl-CoA dehydrogenase, (S)-stereospecific 3-hydroxyacyl-CoA dehydrogenase/enoyl-CoA hydratase, 1-specific DPN-linked beta-hydroxybutyric dehydrogenase, 17beta-HSD10, 3-hydroxyacetyl-coenzyme A dehydrogenase, 3-hydroxyacyl coenzyme A dehydrogenase, 3-hydroxyacyl-CoA dehydrogenase, 3-hydroxyacyl-CoA dehydrogenase II, 3-hydroxyacyl-coenzyme A dehydrogenase, 3-hydroxyadipyl-CoA dehydrogenase, 3-hydroxyadipyl-CoA dehydrogenase (NAD+) (probably (S)-3-specific), 3-hydroxybutyryl-CoA dehydrogenase, 3-hydroxyisobutyryl-CoA dehydrogenase, 3-keto reductase, 3-ketoacyl-CoA reductase, 3-L-hydroxyacyl-CoA dehydrogenase, 3-L-hydroxybutyryl-CoA dehydrogenase, 3beta-hydroxyacyl coenzyme A dehydrogenase, beta hydroxyacyl dehydrogenase, beta-hydroxy acid dehydrogenase, beta-hydroxyacyl CoA dehydrogenase, beta-hydroxyacyl-coenzyme A synthetase, beta-hydroxybutyrylcoenzyme A dehydrogenase, beta-keto-reductase, beta-ketoacyl reductase, beta-ketoacyl-CoA reductase, beta-ketoacyl-coenzyme A reductase, betahydroxyacylcoenzyme A dehydrogenase, CbHBD, endoplasmic reticulum-associated amyloid beta-peptide binding protein, F54C8.1, FadB, FadB', FadB2, Ferp_1035, Fum13p, H16_A0461, HAD, HADH, HADH2, HADHSC, HCDH, KCR1, KCR2, L-3-hydroxyacyl CoA dehydrogenase, L-3-hydroxyacyl-CoA dehydrogenase, L-3-hydroxyacyl-CoA dehydrogenase, short chain, L-3-hydroxyacylcoenzyme A dehydrogenase, L-3-hydroxybutyryl CoA dehydrogenase, L-specific 3-hydroxyacyl-CoA dehydrogenase, LIC13300, medium- and short-chain-3-hydroxyacyl-CoA dehydrogenase, medium- and short-chain-3-hydroxyacyl-coenzyme A dehydrogenase, More, Msed_0399, multifunctional beta-oxidation enzyme, PaaH, PaaH1, RePaaH1, SCHAD, SCHAD I, SCHAD II, SCHSD, Scully protein, short chain L-3-hydroxyacyl-CoA dehydrogenase, short-chain 3-hydroxyacyl-CoA dehydrogenase, short-chain 3-hydroxyacyl-coenzyme A dehydrogenase, short-chain hydroxyacyl CoA dehydrogenase, short-chain L-3-hydroxyacyl-CoA dehydrogenase, TFP, type 10 17beta-hydroxysteroid dehydrogenase, type II HADH

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.35 3-hydroxyacyl-CoA dehydrogenase

Engineering

Engineering on EC 1.1.1.35 - 3-hydroxyacyl-CoA dehydrogenase

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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R204A
-
site-directed mutagenesis, the mutant with attenuated interactions on the dimerization interface still maintains a dimerization form, but the enzymatic activity is significantly decreased compared the wild-type
R204A/Y209A
-
site-directed mutagenesis, the mutant with attenuated interactions on the dimerization interface still maintains a dimerization form, but the enzymatic activity is significantly decreased compared the wild-type
Y209A
-
site-directed mutagenesis, the mutant with attenuated interactions on the dimerization interface still maintains a dimerization form, but the enzymatic activity is significantly decreased compared the wild-type
K50A
-
site-directed mutagenesis, the mutant shows about 2fold increased activity compared to the wild-type enzyme
K50A//L232Y
-
site-directed mutagenesis, the mutant shows about 3fold increased activity compared to the wild-type enzyme
K50A/K54
-
site-directed mutagenesis, the mutant shows about 3fold increased activity compared to the wild-type enzyme
K50A/K54A/L232Y
-
site-directed mutagenesis, the mutant shows about 5fold increased activity compared to the wild-type enzyme
K54A
-
site-directed mutagenesis, the mutant shows about 2fold increased activity compared to the wild-type enzyme
K54A/L232Y
-
site-directed mutagenesis, the mutant shows about 4fold increased activity compared to the wild-type enzyme
L232Z
-
site-directed mutagenesis, the mutant shows about 2.5fold increased activity compared to the wild-type enzyme
K56A
-
site-directed mutagenesis, the mutant shows about twofold increased activity compared to the wild-type enzyme
N190A
-
site-directed mutagenesis, the mutant shows highly decreased activity compared to the wild-type enzyme
R52A
-
site-directed mutagenesis, the mutant shows highly decreased activity compared to the wild-type enzyme
S119A
-
site-directed mutagenesis, almost inactive mutant
K56A
-
site-directed mutagenesis, the mutant shows about twofold increased activity compared to the wild-type enzyme
-
N190A
-
site-directed mutagenesis, the mutant shows highly decreased activity compared to the wild-type enzyme
-
R52A
-
site-directed mutagenesis, the mutant shows highly decreased activity compared to the wild-type enzyme
-
S119A
-
site-directed mutagenesis, almost inactive mutant
-
D279E
-
naturally occuring polymorphism probably involved in development of type 2 diabetes
D45G/Y214H
-
a naturally occuring enzyme mutation causing human disease
H152Q
-
naturally occuring polymorphism probably involved in development of type 2 diabetes
M176V
-
a naturally occuring enzyme mutation causing human disease
M188V
-
naturally occuring enzyme mutation, clinical data, overview
P246L
-
a naturally occuring enzyme mutation causing human disease
P258L
-
naturally occuring enzyme mutation, clinical data, overview
P86L
-
naturally occuring polymorphism probably involved in development of type 2 diabetes
R224X
-
a naturally occuring enzyme mutation causing human disease
R236X
-
naturally occuring enzyme mutation, clinical data, overview
N208A
-
site-directed mutagenesis, the substrate binding of the mutant enzyme is affected
S137C
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
S137T
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
additional information