Crystallization (Comment) | Organism |
---|---|
three crystal structures of DDH_HALMT are solved in complex with combinations of NAD+, NADP+, NADPH, 2-ketohexanoic acid, and 2-hydroxyhexanoic acid (PDB IDs are 5mha, 5mh5, 5mh6) | Haloferax mediterranei |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-oxoisoleucine + NADPH + H+ | Haloferax mediterranei | - |
2-D-hydroxyisoleucine + NADP+ | - |
r | |
2-oxoisoleucine + NADPH + H+ | Haloferax mediterranei ATCC 33500 | - |
2-D-hydroxyisoleucine + NADP+ | - |
r | |
2-oxoisoleucine + NADPH + H+ | Haloferax mediterranei NBRC 14739 | - |
2-D-hydroxyisoleucine + NADP+ | - |
r | |
2-oxoisoleucine + NADPH + H+ | Haloferax mediterranei JCM 8866 | - |
2-D-hydroxyisoleucine + NADP+ | - |
r | |
2-oxoisoleucine + NADPH + H+ | Haloferax mediterranei R-4 | - |
2-D-hydroxyisoleucine + NADP+ | - |
r | |
2-oxoisoleucine + NADPH + H+ | Haloferax mediterranei DSM 1411 | - |
2-D-hydroxyisoleucine + NADP+ | - |
r | |
2-oxoisoleucine + NADPH + H+ | Haloferax mediterranei NCIMB 2177 | - |
2-D-hydroxyisoleucine + NADP+ | - |
r | |
an (R)-2-hydroxycarboxylate + NADP+ | Haloferax mediterranei | - |
a 2-oxocarboxylate + NADPH + H+ | - |
r | |
an (R)-2-hydroxycarboxylate + NADP+ | Haloferax mediterranei ATCC 33500 | - |
a 2-oxocarboxylate + NADPH + H+ | - |
r | |
an (R)-2-hydroxycarboxylate + NADP+ | Haloferax mediterranei NBRC 14739 | - |
a 2-oxocarboxylate + NADPH + H+ | - |
r | |
an (R)-2-hydroxycarboxylate + NADP+ | Haloferax mediterranei JCM 8866 | - |
a 2-oxocarboxylate + NADPH + H+ | - |
r | |
an (R)-2-hydroxycarboxylate + NADP+ | Haloferax mediterranei R-4 | - |
a 2-oxocarboxylate + NADPH + H+ | - |
r | |
an (R)-2-hydroxycarboxylate + NADP+ | Haloferax mediterranei DSM 1411 | - |
a 2-oxocarboxylate + NADPH + H+ | - |
r | |
an (R)-2-hydroxycarboxylate + NADP+ | Haloferax mediterranei NCIMB 2177 | - |
a 2-oxocarboxylate + NADPH + H+ | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Haloferax mediterranei | Q2VEQ7 | - |
- |
Haloferax mediterranei ATCC 33500 | Q2VEQ7 | - |
- |
Haloferax mediterranei DSM 1411 | Q2VEQ7 | - |
- |
Haloferax mediterranei JCM 8866 | Q2VEQ7 | - |
- |
Haloferax mediterranei NBRC 14739 | Q2VEQ7 | - |
- |
Haloferax mediterranei NCIMB 2177 | Q2VEQ7 | - |
- |
Haloferax mediterranei R-4 | Q2VEQ7 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-oxo-3-methylvalerate + NADPH + H+ | - |
Haloferax mediterranei | 2-D-hydroxy-3-methylvalerate + NADP+ | - |
r | |
2-oxo-3-methylvalerate + NADPH + H+ | - |
Haloferax mediterranei ATCC 33500 | 2-D-hydroxy-3-methylvalerate + NADP+ | - |
r | |
2-oxo-3-methylvalerate + NADPH + H+ | - |
Haloferax mediterranei NBRC 14739 | 2-D-hydroxy-3-methylvalerate + NADP+ | - |
r | |
2-oxo-3-methylvalerate + NADPH + H+ | - |
Haloferax mediterranei JCM 8866 | 2-D-hydroxy-3-methylvalerate + NADP+ | - |
r | |
2-oxo-3-methylvalerate + NADPH + H+ | - |
Haloferax mediterranei R-4 | 2-D-hydroxy-3-methylvalerate + NADP+ | - |
r | |
2-oxo-3-methylvalerate + NADPH + H+ | - |
Haloferax mediterranei DSM 1411 | 2-D-hydroxy-3-methylvalerate + NADP+ | - |
r | |
2-oxo-3-methylvalerate + NADPH + H+ | - |
Haloferax mediterranei NCIMB 2177 | 2-D-hydroxy-3-methylvalerate + NADP+ | - |
r | |
2-oxobutyrate + NADPH + H+ | - |
Haloferax mediterranei | 2-D-hydroxybutyrate + NADP+ | - |
r | |
2-oxoisocaproate + NADPH + H+ | - |
Haloferax mediterranei | 2-hydroxyisocaproate + NADP+ | - |
r | |
2-oxoisoleucine + NADPH + H+ | - |
Haloferax mediterranei | 2-D-hydroxyisoleucine + NADP+ | - |
r | |
2-oxoisoleucine + NADPH + H+ | - |
Haloferax mediterranei ATCC 33500 | 2-D-hydroxyisoleucine + NADP+ | - |
r | |
2-oxoisoleucine + NADPH + H+ | - |
Haloferax mediterranei NBRC 14739 | 2-D-hydroxyisoleucine + NADP+ | - |
r | |
2-oxoisoleucine + NADPH + H+ | - |
Haloferax mediterranei JCM 8866 | 2-D-hydroxyisoleucine + NADP+ | - |
r | |
2-oxoisoleucine + NADPH + H+ | - |
Haloferax mediterranei R-4 | 2-D-hydroxyisoleucine + NADP+ | - |
r | |
2-oxoisoleucine + NADPH + H+ | - |
Haloferax mediterranei DSM 1411 | 2-D-hydroxyisoleucine + NADP+ | - |
r | |
2-oxoisoleucine + NADPH + H+ | - |
Haloferax mediterranei NCIMB 2177 | 2-D-hydroxyisoleucine + NADP+ | - |
r | |
an (R)-2-hydroxycarboxylate + NADP+ | - |
Haloferax mediterranei | a 2-oxocarboxylate + NADPH + H+ | - |
r | |
an (R)-2-hydroxycarboxylate + NADP+ | - |
Haloferax mediterranei ATCC 33500 | a 2-oxocarboxylate + NADPH + H+ | - |
r | |
an (R)-2-hydroxycarboxylate + NADP+ | - |
Haloferax mediterranei NBRC 14739 | a 2-oxocarboxylate + NADPH + H+ | - |
r | |
an (R)-2-hydroxycarboxylate + NADP+ | - |
Haloferax mediterranei JCM 8866 | a 2-oxocarboxylate + NADPH + H+ | - |
r | |
an (R)-2-hydroxycarboxylate + NADP+ | - |
Haloferax mediterranei R-4 | a 2-oxocarboxylate + NADPH + H+ | - |
r | |
an (R)-2-hydroxycarboxylate + NADP+ | - |
Haloferax mediterranei DSM 1411 | a 2-oxocarboxylate + NADPH + H+ | - |
r | |
an (R)-2-hydroxycarboxylate + NADP+ | - |
Haloferax mediterranei NCIMB 2177 | a 2-oxocarboxylate + NADPH + H+ | - |
r | |
additional information | the DDH enzyme is a 2-oxocarboxylic reductase with broad substrate specificity. It shows a marked preference for those having an unbranched chain of 4-5 carbon atoms, such as 2-oxoisoleucine. It exhibits dual cofactor specificity, yet shows better catalytic efficiency with NADPH | Haloferax mediterranei | ? | - |
- |
|
additional information | the DDH enzyme is a 2-oxocarboxylic reductase with broad substrate specificity. It shows a marked preference for those having an unbranched chain of 4-5 carbon atoms, such as 2-oxoisoleucine. It exhibits dual cofactor specificity, yet shows better catalytic efficiency with NADPH | Haloferax mediterranei ATCC 33500 | ? | - |
- |
|
additional information | the DDH enzyme is a 2-oxocarboxylic reductase with broad substrate specificity. It shows a marked preference for those having an unbranched chain of 4-5 carbon atoms, such as 2-oxoisoleucine. It exhibits dual cofactor specificity, yet shows better catalytic efficiency with NADPH | Haloferax mediterranei NBRC 14739 | ? | - |
- |
|
additional information | the DDH enzyme is a 2-oxocarboxylic reductase with broad substrate specificity. It shows a marked preference for those having an unbranched chain of 4-5 carbon atoms, such as 2-oxoisoleucine. It exhibits dual cofactor specificity, yet shows better catalytic efficiency with NADPH | Haloferax mediterranei JCM 8866 | ? | - |
- |
|
additional information | the DDH enzyme is a 2-oxocarboxylic reductase with broad substrate specificity. It shows a marked preference for those having an unbranched chain of 4-5 carbon atoms, such as 2-oxoisoleucine. It exhibits dual cofactor specificity, yet shows better catalytic efficiency with NADPH | Haloferax mediterranei R-4 | ? | - |
- |
|
additional information | the DDH enzyme is a 2-oxocarboxylic reductase with broad substrate specificity. It shows a marked preference for those having an unbranched chain of 4-5 carbon atoms, such as 2-oxoisoleucine. It exhibits dual cofactor specificity, yet shows better catalytic efficiency with NADPH | Haloferax mediterranei DSM 1411 | ? | - |
- |
|
additional information | the DDH enzyme is a 2-oxocarboxylic reductase with broad substrate specificity. It shows a marked preference for those having an unbranched chain of 4-5 carbon atoms, such as 2-oxoisoleucine. It exhibits dual cofactor specificity, yet shows better catalytic efficiency with NADPH | Haloferax mediterranei NCIMB 2177 | ? | - |
- |
|
pyruvate + NADPH + H+ | - |
Haloferax mediterranei | D-lactate + NADP+ | - |
r | |
pyruvate + NADPH + H+ | - |
Haloferax mediterranei ATCC 33500 | D-lactate + NADP+ | - |
r | |
pyruvate + NADPH + H+ | - |
Haloferax mediterranei NBRC 14739 | D-lactate + NADP+ | - |
r | |
pyruvate + NADPH + H+ | - |
Haloferax mediterranei JCM 8866 | D-lactate + NADP+ | - |
r | |
pyruvate + NADPH + H+ | - |
Haloferax mediterranei R-4 | D-lactate + NADP+ | - |
r | |
pyruvate + NADPH + H+ | - |
Haloferax mediterranei DSM 1411 | D-lactate + NADP+ | - |
r | |
pyruvate + NADPH + H+ | - |
Haloferax mediterranei NCIMB 2177 | D-lactate + NADP+ | - |
r |
Synonyms | Comment | Organism |
---|---|---|
2HADH | - |
Haloferax mediterranei |
D-2-hydroxyacid dehydrogenase | - |
Haloferax mediterranei |
D-isomer specific 2-hydroxyacid dehydrogenase | - |
Haloferax mediterranei |
DDH | - |
Haloferax mediterranei |
DDH_HALMT | - |
Haloferax mediterranei |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
additional information | the enzyme prefers NADPH over NADH | Haloferax mediterranei | |
NADP+ | - |
Haloferax mediterranei | |
NADPH | - |
Haloferax mediterranei |
General Information | Comment | Organism |
---|---|---|
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 | Haloferax mediterranei |
additional information | sequence-structure-function relationships, overview | Haloferax mediterranei |