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
-
2-hydroxyacids
-
enterococcus
-
nad-dependent
- d-mandelate
-
2-oxobutyric
- d-lactate
- 2-ketoisocaproate
-
knowledgebase
- delbrueckii
-
2-keto
-
4-methylthio
- benzoylformate
-
haloferax
- glyoxylate
- bulgaricus
- faecium
-
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
ECTree
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Subunits
Subunits on EC 1.1.1.272 - D-2-hydroxyacid dehydrogenase (NADP+)
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tetramer
additional information
4 * 33336, sequence calculation, 4 * 29500, recombinant enzyme, CTAB-PAGE, 4 * 47000, SDS-PAGE
tetramer
Haloferax mediterranei R-4 / ATCC 33500
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4 * 33336, sequence calculation, 4 * 29500, recombinant enzyme, CTAB-PAGE, 4 * 47000, SDS-PAGE
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the enzyme shows a structure consisting of two-compact domains separated by a deep active cleft. This typical topology is conserved in other 2-HDH. The smaller domain is the substrate binding domain or catalytic domain, which is formed from N-terminal residues 2-102 and C-terminal residues 288-317. It is folded into a five-stranded parallel beta-sheet flanked by five alpha-helices, forming a modified Rossmann topology. The larger domain is responsible for binding the cofactor and contains a conserved [GXGXXG(X17)D] motif that is characteristic of the NAD(P)H/NAD(P)+-binding region. It consists of residues 103-287, forming a seven-stranded parallel beta-sheet flanked by seven alpha-helices. A two-stranded hinge connects the two domains showing flexibilty during catalysis
additional information
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the enzyme shows a structure consisting of two-compact domains separated by a deep active cleft. This typical topology is conserved in other 2-HDH. The smaller domain is the substrate binding domain or catalytic domain, which is formed from N-terminal residues 2-102 and C-terminal residues 288-317. It is folded into a five-stranded parallel beta-sheet flanked by five alpha-helices, forming a modified Rossmann topology. The larger domain is responsible for binding the cofactor and contains a conserved [GXGXXG(X17)D] motif that is characteristic of the NAD(P)H/NAD(P)+-binding region. It consists of residues 103-287, forming a seven-stranded parallel beta-sheet flanked by seven alpha-helices. A two-stranded hinge connects the two domains showing flexibilty during catalysis
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