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
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General Information
General Information on EC 1.1.1.30 - 3-hydroxybutyrate dehydrogenase
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malfunction
metabolism
additional information
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Gln94, His144, Lys152, and Gln196 form hydrogen bonds with carboxyl and/or ketone group of acetoacetate, Trp187, Trp257 form hydrophobic interactions with the carbon atoms of acetoacetate, and Ser142 and Tyr155 are directly related to the catalytic mechanism
enzyme inactivation in developing zebrafish embryo results in heme deficiency and delays erythrocyte maturation
malfunction
inhibiting expression of the 3-hydroxybutyrate dehydrogenase-2 gene results in abnormal accumulation of intracellular iron, increased oxidative stress, and mitochondrial iron deficiency
steady-state ordered kinetic mechanism for acetoacetate reduction, where hydride transfer is not rate limiting. Hydride transfer becomes more rate limiting with non-native substrate 3-oxovalerate. Hydride and proton transfers occur in the same transition state. Transition states show concerted, albeit not synchronous, proton and hydride transfers to 3-oxovalerate
metabolism
steady-state ordered kinetic mechanism for acetoacetate reduction, where hydride transfer is not rate limiting. Hydride transfer becomes more rate limiting with non-native substrate 3-oxovalerate. Hydride and proton transfers occur in the same transition state. Transition states showconcerted, albeit not synchronous, proton and hydride transfers to 3-oxovalerate
metabolism
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steady-state ordered kinetic mechanism for acetoacetate reduction, where hydride transfer is not rate limiting. Hydride transfer becomes more rate limiting with non-native substrate 3-oxovalerate. Hydride and proton transfers occur in the same transition state. Transition states show concerted, albeit not synchronous, proton and hydride transfers to 3-oxovalerate
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