1.1.1.30: 3-hydroxybutyrate dehydrogenase
This is an abbreviated version!
For detailed information about 3-hydroxybutyrate dehydrogenase, go to the full flat file.
Word Map on EC 1.1.1.30
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1.1.1.30
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ketone
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succinate
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acetoacetate
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lipid-requiring
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lecithin
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coa-transferase
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acetoacetyl-coa
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alpha-glycerophosphate
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thiolase
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3-oxoacid
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submitochondrial
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ketogenesis
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enzyme-phospholipid
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analysis
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diagnostics
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synthesis
- 1.1.1.30
- ketone
- succinate
- acetoacetate
-
lipid-requiring
- lecithin
-
coa-transferase
- acetoacetyl-coa
- alpha-glycerophosphate
-
thiolase
-
3-oxoacid
-
submitochondrial
-
ketogenesis
-
enzyme-phospholipid
- analysis
- diagnostics
- synthesis
Reaction
Synonyms
3-D-hydroxybutyrate dehydrogenase, 3-HBDH, 3-hydroxybutyrate dehydrogenase, 3-hydroxybutyrate dehydrogenase 2, 3-hydroxybutyrate dehydrogenase-2, 3HBDH, acetoacetyl-CoA reductase, BDH, BDH1, BDH2, BDH3, BdhA, beta-hydroxybutyrate dehydrogenase, beta-hydroxybutyric acid dehydrogenase, beta-hydroxybutyric dehydrogenase, D(-)-3-hydroxybutyrate dehydrogenase, D-(-)-3-hydroxybutyrate dehydrogenase, D-3-hydroxybutyrate dehydrogenase, D-beta-hydroxybutyrate dehydrogenase, DHRS6, HBD, HBDH, hydroxybutyrate oxidoreductase, More, NAD-beta-hydroxybutyrate dehydrogenase, Psyc_1428
ECTree
Advanced search results
Engineering
Engineering on EC 1.1.1.30 - 3-hydroxybutyrate dehydrogenase
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H144A
the mutant shows reduced catalytic efficiency with levulinic acid compared to the wild type enzyme
H144F
the mutant shows increased catalytic efficiency with levulinic acid compared to the wild type enzyme
H144I
the mutant shows increased catalytic efficiency with levulinic acid compared to the wild type enzyme
H144L
H144L/W187A
the mutant shows reduced catalytic efficiency with levulinic acid compared to the wild type enzyme
H144L/W187F
H144L/W187I
the mutant shows reduced catalytic efficiency with levulinic acid compared to the wild type enzyme
H144L/W187L
the mutant shows strongly increased catalytic efficiency with levulinic acid compared to the wild type enzyme
H144L/W187V
the mutant shows reduced catalytic efficiency with levulinic acid compared to the wild type enzyme
H144V
the mutant shows wild type catalytic efficiency with levulinic acid
W187A
the mutant shows reduced catalytic efficiency with levulinic acid compared to the wild type enzyme
W187F
W187I
the mutant shows reduced catalytic efficiency with levulinic acid compared to the wild type enzyme
W187L
the mutant shows reduced catalytic efficiency with levulinic acid compared to the wild type enzyme
W187V
the mutant shows reduced catalytic efficiency with levulinic acid compared to the wild type enzyme
H144A
catalytic efficiency (kcat/Km) is 0.2% of the activity of wild-type HBDH
L215A
both Km and kcat values are largely affected and the catalytic efficiency (kcat/Km) is less than 3% that of the wild-type enzyme
L215V
Km values increase 3.5- and 4.3fold and the kcat values are 73-118% those of the wild-type toward D-3-hydroxybutyrate and acetoacetate, respectively. Mutation does not significantly change Km and kcat toward NAD+ and NADH
Q94A
catalytic efficiency (kcat/Km) is 1.4% of the activity of wild-type HBDH
W187F
shows significant activity levels, 65% that of the wild-type enzyme
W187Y
shows significant activity levels, 41% that of the wild-type enzyme
H141A
K149R
kcat/KM for (R)-3-hydroxybutanoate is 184.2fold lower than wild-type value, kcat/Km for NAD+ is 7.2fold lower than wild-type enzyme
Q193A
kcat/KM for (R)-3-hydroxybutanoate is 307fold lower than wild-type value, kcat/Km for NAD+ is 6.2fold lower than wild-type enzyme
Q91A
additional information
H144L
the mutant shows increased catalytic efficiency with levulinic acid compared to the wild type enzyme
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site-directed mutagenesis, the mutant shows activity with levulinnic acid, in contrast to the wild-type enzyme, and is engineered for production of 4-hydroxyvaleric acid, molecular docking simulation, overview
H144L/W187F
the mutant shows strongly increased catalytic efficiency with levulinic acid compared to the wild type enzyme
W187F
the mutant shows increased catalytic efficiency with levulinic acid compared to the wild type enzyme
H141A
kcat/KM for (R)-3-hydroxybutanoate is 184.2fold lower than wild-type value, kcat/Km for NAD+ is 12.9fold lower than wild-type enzyme
Q91A
kcat/KM for (R)-3-hydroxybutanoate is 83.7fold lower than wild-type value, kcat/Km for NAD+ is 2.8fold lower than wild-type enzyme
the bdh1 mutant lags behind the wild-type in growth rates when the cells are cultured with 3-hydroxybutyrate, citrate, succinate, or nutrient broth. A test of sensitivity to diamide as an oxidative stress reveals that the lack of BDH1 causes a decline in the capacity to neutralize the stress
additional information
the bdh1 mutant lags behind the wild-type in growth rates when the cells are cultured with 3-hydroxybutyrate, citrate, succinate, or nutrient broth. A test of sensitivity to diamide as an oxidative stress reveals that the lack of BDH1 causes a decline in the capacity to neutralize the stress
additional information
the bdh1 mutant lags behind the wild-type in growth rates when the cells are cultured with 3-hydroxybutyrate, citrate, succinate, or nutrient broth. A test of sensitivity to diamide as an oxidative stress reveals that the lack of BDH1 causes a decline in the capacity to neutralize the stress
additional information
the bdh2 mutant lags behind the wild-type in growth rates when the cells are cultured with 3-hydroxybutyrate, citrate, succinate, or nutrient broth. A test of sensitivity to diamide as an oxidative stress reveals that the lack of BDH2 causes a decline in the capacity to neutralize the stress
additional information
the bdh2 mutant lags behind the wild-type in growth rates when the cells are cultured with 3-hydroxybutyrate, citrate, succinate, or nutrient broth. A test of sensitivity to diamide as an oxidative stress reveals that the lack of BDH2 causes a decline in the capacity to neutralize the stress
additional information
the bdh2 mutant lags behind the wild-type in growth rates when the cells are cultured with 3-hydroxybutyrate, citrate, succinate, or nutrient broth. A test of sensitivity to diamide as an oxidative stress reveals that the lack of BDH2 causes a decline in the capacity to neutralize the stress
additional information
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the bdh2 mutant lags behind the wild-type in growth rates when the cells are cultured with 3-hydroxybutyrate, citrate, succinate, or nutrient broth. A test of sensitivity to diamide as an oxidative stress reveals that the lack of BDH2 causes a decline in the capacity to neutralize the stress
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additional information
-
the bdh1 mutant lags behind the wild-type in growth rates when the cells are cultured with 3-hydroxybutyrate, citrate, succinate, or nutrient broth. A test of sensitivity to diamide as an oxidative stress reveals that the lack of BDH1 causes a decline in the capacity to neutralize the stress
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