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.
Word Map on EC 1.1.1.36
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1.1.1.36
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polyhydroxyalkanoate
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beta-ketothiolase
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eutropha
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ralstonia
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poly3-hydroxybutyrate
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cupriavidus
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necator
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medium-chain-length
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2-enoyl-coa
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3-hydroxyhexanoate
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enoyl
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poly3-hydroxybutyrate-co-3-hydroxyhexanoate
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short-chain-length
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ramigera
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3-hydroxyalkanoate
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3r-hydroxyacyl-coas
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trans-2-enoyl-coa
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phbhhx
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pha-negative
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zoogloea
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r-3-hydroxybutyrate
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copolyesters
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3-hydroxyvalerate
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poly3-hydroxybutyrate-co-3-hydroxyvalerate
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3-ketothiolase
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scp-2
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synthesis
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biotechnology
- 1.1.1.36
- polyhydroxyalkanoate
- beta-ketothiolase
- eutropha
-
ralstonia
-
poly3-hydroxybutyrate
- cupriavidus
- necator
-
medium-chain-length
-
2-enoyl-coa
- 3-hydroxyhexanoate
-
enoyl
-
poly3-hydroxybutyrate-co-3-hydroxyhexanoate
-
short-chain-length
- ramigera
- 3-hydroxyalkanoate
-
3r-hydroxyacyl-coas
- trans-2-enoyl-coa
-
phbhhx
-
pha-negative
-
zoogloea
-
r-3-hydroxybutyrate
-
copolyesters
- 3-hydroxyvalerate
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poly3-hydroxybutyrate-co-3-hydroxyvalerate
- 3-ketothiolase
- scp-2
- synthesis
- biotechnology
Reaction
Synonyms
(3R)-hydroxyacyl-CoA dehydrogenase, (R)-3-hydroxyacyl-CoA dehydrogenase, AAR, AcAc-CoA reductase, 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, ketoacyl reductase, MFE-2, More, MSMEG_6753, NADH-preferring acetoacetyl-CoA reductase, NADP-linked acetoacetyl CoA reductase, NADPH-dependent acetoacetyl coenzyme A reductase, NADPH-dependent acetoacetyl-CoA reductase, NADPH-dependent acetoacetyl-coenzyme A 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
1.1.1.36 acetoacetyl-CoA reductaseAdvanced search results
results (
results (Engineering
Engineering on EC 1.1.1.36 - acetoacetyl-CoA reductase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Q47L
T173S
Q47L
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the mutant shows with increased enzymatic efficiency compared to the wild type enzyme
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T173S
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the mutant shows with increased enzymatic efficiency compared to the wild type enzyme
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Q47L
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
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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
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T173S
E366A
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site-directed mutagenesis, kcat/Km 100times lower than that of the wild type
truncated version
additional information
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
the mutant shows with increased enzymatic efficiency compared to the wild type enzyme
T173S
by random mutagenesis and high-throughput screening, enzyme mutant engineering for increased production of poly(3-hydroxybutyrate) in a Corynebacterium glutamicum expression system
T173S
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
T173S
the mutant shows with increased enzymatic efficiency compared to the wild type enzyme
T173S
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
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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
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T173S
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
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by random mutagenesis and high-throughput screening, enzyme mutant engineering for increased production of poly(3-hydroxybutyrate) in a Corynebacterium glutamicum expression system
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truncated version
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truncated version (lacking the carboxyl-terminal 271 amino acids). The truncated form contains only the D-3-hydroxyacyl-CoA dehydrogenase activity
truncated version
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truncated version (lacking the carboxyl-terminal 271 amino acids). The truncated form contains only the D-3-hydroxyacyl-CoA dehydrogenase activity
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additional information
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loss of AtKCR1 function results in embryo lethality, which cannot be rescued by AtKCR2 expression using the AtKCR1 promoter. Disruption of the AtKCR2 gene has no obvious phenotypic effect. Suppressed KCR activity results in a reduction of cuticular wax load and affects VLCFA composition of sphingolipids, seed triacylglycerols, and root glycerolipids, phenotypes, detailed overview
additional information
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site-directed mutagenesis, while the wild-type enzyme, comprising amino acid residues 1-906, is unstable and not crystallizable, as is the recombinant truncated version comprising amino acid residues 1-591, the mutants 1-604 and 1-612, with or without further modifications, are stable with different crystallizability, overview
additional information
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the Candida tropicalis MFE-2 with a deleted hydratase 2 domain (Ct MFE-2(h2delta)) and mutational variants of the A and B domains (Ct MFE-2(h2deltaadelta), Ct MFE-2(h2deltabdelta), and Ct MFE-2(h2deltaadeltabdelta)) are overexpressed and characterized
additional information
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construction of transgenic Zea mays plants, by microprojectile bombardment, expression of the enzyme from Alcaligenes eutrophus using the small subunit 24 amino acid transit peptide of Pisum sativum ribulose bisphosphate carboxylase to target the plasmid into the chloroplasts of maize
additional information
directed evolution and structural analysis of NADPH-dependent acetoacetyl-CoA reductase reveals two mutations responsible for enhanced kinetics, enzyme mutant is engineered by means of directed evolution consisting of an error-prone PCR-mediated mutagenesis and a P(3HB) accumulation-based in vivo screening system using Escherichia coli. Comparative three-dimensional structural analysis of wild-type PhaB and highly active PhaB mutants reveals that the beneficial mutations affect the flexibility around the active site, which in turn play an important role in substrate recognition. Both the kinetic analysis and crystal structure data support the conclusion that PhaB forms a ternary complex with NADPH and acetoacetyl-CoA
additional information
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
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directed evolution and structural analysis of NADPH-dependent acetoacetyl-CoA reductase reveals two mutations responsible for enhanced kinetics, enzyme mutant is engineered by means of directed evolution consisting of an error-prone PCR-mediated mutagenesis and a P(3HB) accumulation-based in vivo screening system using Escherichia coli. Comparative three-dimensional structural analysis of wild-type PhaB and highly active PhaB mutants reveals that the beneficial mutations affect the flexibility around the active site, which in turn play an important role in substrate recognition. Both the kinetic analysis and crystal structure data support the conclusion that PhaB forms a ternary complex with NADPH and acetoacetyl-CoA
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additional information
disruption or knockout of fabG1 abolishes HA synthesis, and complementation of the DELTAfabG1 mutant with the fabG1 gene restores both PHA synthesis capability and the NADPH-dependent acetoacetyl-CoA reductase activity. Heterologous coexpression of the PHA synthase genes, phaEC together with fabG1, but not its five paralogs, reconstructs the PHA biosynthetic pathway in Haloferax volcanii, a PHA-defective haloarchaeon
additional information
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disruption or knockout of fabG1 abolishes HA synthesis, and complementation of the DELTAfabG1 mutant with the fabG1 gene restores both PHA synthesis capability and the NADPH-dependent acetoacetyl-CoA reductase activity. Heterologous coexpression of the PHA synthase genes, phaEC together with fabG1, but not its five paralogs, reconstructs the PHA biosynthetic pathway in Haloferax volcanii, a PHA-defective haloarchaeon
additional information
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disruption or knockout of fabG1 abolishes HA synthesis, and complementation of the DELTAfabG1 mutant with the fabG1 gene restores both PHA synthesis capability and the NADPH-dependent acetoacetyl-CoA reductase activity. Heterologous coexpression of the PHA synthase genes, phaEC together with fabG1, but not its five paralogs, reconstructs the PHA biosynthetic pathway in Haloferax volcanii, a PHA-defective haloarchaeon
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additional information
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constructs are tested for complementation in Saccharomyces cerevisiae
