EC Number |
General Information |
Reference |
---|
1.1.1.28 | evolution |
although both types of enzymes, NAD-dependent D- and L-lactate dehydrogenases (D-LDH, EC 1.1.1.28; and L-LDH, EC 1.1.1.27) catalyze identical reactions except for the distinct chirality of the lactate product, they are evolutionarily distinct from each other. Allosteric mechanism of D-LDHs, overview |
-, 739841 |
1.1.1.28 | evolution |
the enzyme belongs to the D-isomer-specific 2-hydroxyacid dehydrogenase family |
-, 741246 |
1.1.1.28 | evolution |
two evolutionarily distinct families of LDH enzymes perform the oxidation of NADH/reduction of NAD+ to yield a product that differs only in its chirality: L-lactate or D-lactate |
710727 |
1.1.1.28 | metabolism |
amino acid residues I177 and N213 form a gate guarding the NAD adenine moiety binding cavity |
760888 |
1.1.1.28 | metabolism |
in the organism, xylose is converted into lactic and acetic acids by xylose isomerization by xylose isomerase to xylulose, which is phosphorylated to xylulose 5-phosphate by xylulokinase. Through the phosphoketolase pathway, xylulose 5-phosphate is finally converted to lactic acid and acetic acid in a process known as hetero-lactic acid fermentation |
-, 701818 |
1.1.1.28 | metabolism |
the enzyme acts at the last step of the glycolytic pathway under anaerobic conditions |
-, 739841 |
1.1.1.28 | more |
ldhD transcription levels are higher than those of ldhL, EC 1.1.1.27 |
-, 739905 |
1.1.1.28 | more |
ldhL, EC 1.1.1.27, transcription levels are higher than those of ldhD |
-, 739905 |
1.1.1.28 | more |
the side chain of residue Tyr52 locates very near the C3 substituent group of 2-ketoacid substrate and is associated with the recognition of substrate side chain |
740225 |
1.1.1.28 | physiological function |
a deletion mutant lacking all four NADH dehydrogenases retains the ability to grow on N-acetylglucosamine under fumarate-respiring conditions, while an additional deletion of LdhA or respiratory quinone-dependent D-LDH deprives the mutant of this growth ability |
760398 |