1.1.1.36: acetoacetyl-CoA reductase

This is an abbreviated version, for detailed information about acetoacetyl-CoA reductase, go to the full flat file.

Reaction

(R)-3-hydroxyacyl-CoA
+
NADP+
=
3-oxoacyl-CoA
+
NADPH
+
H+

Synonyms

(3R)-hydroxyacyl-CoA dehydrogenase, (R)-3-hydroxyacyl-CoA dehydrogenase, acetoacetyl CoA reductase, acetoacetyl coenzyme A reductase, acetoacetyl-CoA reductase, AKR1B15, aldo-keto reductase 1B15, beta-ketoacyl reductase, beta-ketoacyl-CoA reductase, beta-ketoacyl-coenzyme A reductase, D(-)-beta-hydroxybutyryl CoA-NADP oxidoreductase, D-3-hydroxyacyl-CoA dehydrogenase, D-3-hydroxyacyl-CoA reductase, D-specific 3-hydroxyacyl-CoA dehydrogenase, hydroxyacyl coenzyme-A dehydrogenase, KCR, MFE-2, More, NADP-linked acetoacetyl CoA reductase, NADPH-dependent acetoacetyl coenzyme A reductase, NADPH-dependent acetoacetyl-CoA reductase, NADPH-linked acetoacetyl-CoA reductase, NADPH:acetoacetyl-CoA reductase, PHA-specific acetoacetyl-CoA reductase, PhaB, PhbB, polyhydroxyalkanoate-specific acetoacetyl coenzyme A reductase, polyhydroxybutyrate enzyme, short chain beta-ketoacetyl(acetoacetyl)-CoA reductase

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.36 acetoacetyl-CoA reductase

Engineering

Engineering on EC 1.1.1.36 - acetoacetyl-CoA reductase

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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A+/B+CtMFE-2(h2delta)
-
recombinant enzyme
A-/B+CtMFE-2(hdelta2deltaadelta)
-
domain A deleted
A-/B-CtMFE-2(hdelta2deltabdelta)
-
domain A and B deleted
Q47L
-
random mutagenesis, the mutant exhibits a kcat value 2.4fold higher compared to the wild-type enzyme, enhanced activity, and enhanced P(3HB) accumulation when expressed in recombinant Corynebacterium glutamicum. The mutation affects the interaction with substrates, resulting in the acquirement of enhanced activity
Q47L
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
random mutagenesis, the mutant exhibits a kcat value 2.4fold higher compared to the wild-type enzyme, enhanced activity, and enhanced P(3HB) accumulation when expressed in recombinant Corynebacterium glutamicum. The mutation affects the interaction with substrates, resulting in the acquirement of enhanced activity
-
T173S
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
by random mutagenesis and high-throughput screening, enzyme mutant engineering for increased production of poly(3-hydroxybutyrate) in a Corynebacterium glutamicum expression system; random mutagenesis, the mutant exhibits a kcat value 3.5fold higher compared to the wild-type enzyme, enhanced activity, and enhanced P(3HB) accumulation when expressed in recombinant Corynebacterium glutamicum. The mutation affects the interaction with substrates, resulting in the acquirement of enhanced activity
-
D370A
-
site-directed mutagenesis
D490A
-
site-directed mutagenesis
D510A
-
site-directed mutagenesis, inactive
D517A
-
site-directed mutagenesis
E366A
-
site-directed mutagenesis, kcat/Km 100times lower than that of the wild type
E408A
-
site-directed mutagenesis
G16S
-
site-directed mutagenesis
H406A
-
site-directed mutagenesis
H515A
-
site-directed mutagenesis
H532A
-
site-directed mutagenesis
Y347A
-
site-directed mutagenesis
Y410A
-
site-directed mutagenesis
Y505A
-
site-directed mutagenesis
G16S
-
site-directed mutagenesis
G329S
-
site-directed mutagenesis
truncated version
additional information