1.1.1.272: D-2-hydroxyacid dehydrogenase (NADP+)
This is an abbreviated version!
For detailed information about D-2-hydroxyacid dehydrogenase (NADP+), go to the full flat file.
Word Map on EC 1.1.1.272
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1.1.1.272
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dehydrogenases
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2-hydroxyacids
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enterococcus
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nad-dependent
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d-mandelate
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2-oxobutyric
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d-lactate
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2-ketoisocaproate
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knowledgebase
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delbrueckii
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2-keto
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4-methylthio
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benzoylformate
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haloferax
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glyoxylate
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bulgaricus
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faecium
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d-2-hydroxyisocaproate
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mediterranei
- 1.1.1.272
- dehydrogenases
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2-hydroxyacids
-
enterococcus
-
nad-dependent
- d-mandelate
-
2-oxobutyric
- d-lactate
- 2-ketoisocaproate
-
knowledgebase
- delbrueckii
-
2-keto
-
4-methylthio
- benzoylformate
-
haloferax
- glyoxylate
- bulgaricus
- faecium
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d-2-hydroxyisocaproate
- mediterranei
Reaction
Synonyms
(R)-2-hydroxyacid dehydrogenase, (R)-sulfolactate dehydrogenase, (R)-sulfolactate:NAD(P)+ oxidoreductase, 2-D-hydroxyacid dehydrogenase, 2-HDH, 2HADH, D-2-hydroxyacid dehydrogenase, D-isomer specific 2-hydroxyacid dehydrogenase, D2-HDH, DDH, DDH_HALMT, HDH, L-2-hydroxyacid dehydrogenase, L-sulfolactate dehydrogenase
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General Information
General Information on EC 1.1.1.272 - D-2-hydroxyacid dehydrogenase (NADP+)
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evolution
physiological function
additional information
the enzyme belongs to the family of D-isomer specific 2-hydroxyacid dehydrogenases (2HADHs) that contains a wide range of oxidoreductases with various metabolic roles as well as biotechnological applications. The family comprises 22 subfamilies, the enzyme from Haloferax mediterranei belongs to the DDH subfamily, phylogenetic analysis and tree, overview
evolution
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the enzyme belongs to the family of D-isomer specific 2-hydroxyacid dehydrogenases (2HADHs) that contains a wide range of oxidoreductases with various metabolic roles as well as biotechnological applications. The family comprises 22 subfamilies, the enzyme from Haloferax mediterranei belongs to the DDH subfamily, phylogenetic analysis and tree, overview
-
evolution
-
the enzyme belongs to the family of D-isomer specific 2-hydroxyacid dehydrogenases (2HADHs) that contains a wide range of oxidoreductases with various metabolic roles as well as biotechnological applications. The family comprises 22 subfamilies, the enzyme from Haloferax mediterranei belongs to the DDH subfamily, phylogenetic analysis and tree, overview
-
evolution
-
the enzyme belongs to the family of D-isomer specific 2-hydroxyacid dehydrogenases (2HADHs) that contains a wide range of oxidoreductases with various metabolic roles as well as biotechnological applications. The family comprises 22 subfamilies, the enzyme from Haloferax mediterranei belongs to the DDH subfamily, phylogenetic analysis and tree, overview
-
evolution
-
the enzyme belongs to the family of D-isomer specific 2-hydroxyacid dehydrogenases (2HADHs) that contains a wide range of oxidoreductases with various metabolic roles as well as biotechnological applications. The family comprises 22 subfamilies, the enzyme from Haloferax mediterranei belongs to the DDH subfamily, phylogenetic analysis and tree, overview
-
evolution
-
the enzyme belongs to the family of D-isomer specific 2-hydroxyacid dehydrogenases (2HADHs) that contains a wide range of oxidoreductases with various metabolic roles as well as biotechnological applications. The family comprises 22 subfamilies, the enzyme from Haloferax mediterranei belongs to the DDH subfamily, phylogenetic analysis and tree, overview
-
evolution
-
the enzyme belongs to the family of D-isomer specific 2-hydroxyacid dehydrogenases (2HADHs) that contains a wide range of oxidoreductases with various metabolic roles as well as biotechnological applications. The family comprises 22 subfamilies, the enzyme from Haloferax mediterranei belongs to the DDH subfamily, phylogenetic analysis and tree, overview
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the enzyme catalyzes the bioconversion of 2-dehydro-L-gulonic acid to L-idonate, which plays a negative role in the manufacture of vitamin C, cf. EC 1.1.1.215. The primary biochemical function of HDH from Ketogulonicigenium vulgare is C=O bond oxidation-reduction
physiological function
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the enzyme catalyzes the bioconversion of 2-dehydro-L-gulonic acid to L-idonate, which plays a negative role in the manufacture of vitamin C, cf. EC 1.1.1.215. The primary biochemical function of HDH from Ketogulonicigenium vulgare is C=O bond oxidation-reduction
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the amino acid residues Arg234, Glu263 and His 279 form the active site of enzyme HDH. Residues Arg234, Ala210, Thr211, and Arg212, which are located on top of the catalytic triad, act as a size filter to jointly determine the substrate specificity
additional information
sequence-structure-function relationships, overview
additional information
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sequence-structure-function relationships, overview
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additional information
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sequence-structure-function relationships, overview
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additional information
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sequence-structure-function relationships, overview
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additional information
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sequence-structure-function relationships, overview
-
additional information
-
sequence-structure-function relationships, overview
-
additional information
-
sequence-structure-function relationships, overview
-
additional information
-
the amino acid residues Arg234, Glu263 and His 279 form the active site of enzyme HDH. Residues Arg234, Ala210, Thr211, and Arg212, which are located on top of the catalytic triad, act as a size filter to jointly determine the substrate specificity
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