EC Number   |
General Information |
Reference |
|---|
    1.1.1.345 | 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 |
-, 743180 |
| 1.1.1.345 | 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 |
-, 712292 |
| 1.1.1.345 | 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 |
-, 712292 |
| 1.1.1.345 | 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 |
-, 748018 |
| 1.1.1.345 | metabolism |
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 |
-, 712292 |
| 1.1.1.345 | more |
enzyme three-dimensional structure analysis, active site and cofactor binding site structures, overview |
-, 743180 |
| 1.1.1.345 | 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 |
-, 743180 |
