1.1.1.345: D-2-hydroxyacid dehydrogenase (NAD+)
This is an abbreviated version!
For detailed information about D-2-hydroxyacid dehydrogenase (NAD+), go to the full flat file.
Reaction
Synonyms
D-2-HADH, D-2-hydroxyacid dehydrogenase, D-2-hydroxyisocaproate dehydrogenase, D-HicDH, D-isomer specific 2-hydroxyacid dehydrogenase, D-isomer specific NAD+-dependent 2-hydroxyacid dehydrogenase, D-isomer-specific 2-hydroxyacid dehydrogenase, D-lactate dehydrogenase, D-lactate:NAD+ oxidoreductase, D-malate dehydrogenases, D-mandelate dehydrogenase, D-ManDH1, D-ManDH2, D-MDH, D2-HDH, HdhD, Ldb1010, ldh1837, LEUM_1837, ManDH2, NAD-dependent D-2-hydroxyacid dehydrogenase, PanE, R-HicDH
ECTree
Advanced search results
General Information
General Information on EC 1.1.1.345 - D-2-hydroxyacid dehydrogenase (NAD+)
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
evolution
malfunction
metabolism
physiological function
additional information
the enzyme belongs to the the NAD-dependent dehydrogenase family. Comparison with closely related members of the NAD-dependent dehydrogenase family reveals that whilst the D2-HDH core fold is structurally conserved, the substrate-binding site has a number of non-canonical features that may influence substrate selection and thus dictate the physiological function of the enzyme. The protein, 2-hydroxyisocaproate dehydrogenase (HO-HxoDH), is virtually identical to the D2-HDH, with only three amino-acid differences between the two proteins, all at sites not known to be biologically relevant
evolution
-
the enzyme belongs to the the NAD-dependent dehydrogenase family. Comparison with closely related members of the NAD-dependent dehydrogenase family reveals that whilst the D2-HDH core fold is structurally conserved, the substrate-binding site has a number of non-canonical features that may influence substrate selection and thus dictate the physiological function of the enzyme. The protein, 2-hydroxyisocaproate dehydrogenase (HO-HxoDH), is virtually identical to the D2-HDH, with only three amino-acid differences between the two proteins, all at sites not known to be biologically relevant
-
-
the inactivation of panE does not affect the total percentage of leucine degraded but totally prevents KIC reduction to 2-hydroxyisocaproate and slightly decreases the production of isovalerate
malfunction
-
the inactivation of panE does not affect the total percentage of leucine degraded but totally prevented 4-methyl-2-oxopentanoate reduction to 2-hydroxyisocaproate and slightly decreased the production of isovalerate
malfunction
-
the inactivation of panE does not affect the total percentage of leucine degraded but totally prevents KIC reduction to 2-hydroxyisocaproate and slightly decreases the production of isovalerate
-
malfunction
Lactococcus cremoris TIL46
-
the inactivation of panE does not affect the total percentage of leucine degraded but totally prevented 4-methyl-2-oxopentanoate reduction to 2-hydroxyisocaproate and slightly decreased the production of isovalerate
-
-
its probable physiological role is to regenerate the NAD+ necessary to catabolize branched-chain amino acids, leading to the production of ATP and aroma compounds responsible for the reduction of the 2-keto acids derived from leucine, isoleucine, and valine
metabolism
in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
metabolism
-
in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
-
metabolism
-
in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
-
metabolism
-
in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
-
metabolism
-
in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
-
metabolism
-
in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
-
metabolism
-
in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
-
metabolism
-
in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
-
metabolism
-
in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
-
metabolism
-
in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
-
metabolism
-
in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
-
metabolism
Lactococcus cremoris TIL46
-
its probable physiological role is to regenerate the NAD+ necessary to catabolize branched-chain amino acids, leading to the production of ATP and aroma compounds responsible for the reduction of the 2-keto acids derived from leucine, isoleucine, and valine
-
metabolism
-
in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
-
the substrate-binding site has a number of non-canonical features that may influence substrate selection and thus dictate the physiological function of the enzyme
physiological function
-
the substrate-binding site has a number of non-canonical features that may influence substrate selection and thus dictate the physiological function of the enzyme
-
enzyme three-dimensional structure analysis, active site and cofactor binding site structures, overview
additional information
-
enzyme three-dimensional structure analysis, active site and cofactor binding site structures, overview
-