PMID:1567457
| Citation |
Kochhar, S, Hunziker, PE, Leong-Morgenthaler, P and Hottinger, H (1992) Evolutionary relationship of NAD(+)-dependent D-lactate dehydrogenase: comparison of primary structure of 2-hydroxy acid dehydrogenases. Biochem. Biophys. Res. Commun. 184:60-6 |
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| Abstract |
A comparison of the primary structures of NAD(+)-dependent D-lactate dehydrogenase with L-lactate dehydrogenase and L-malate dehydrogenase failed to show any sequence similarity. However, D-2-hydroxyisocaproate dehydrogenase from Lactobacillus casei, glycerate dehydrogenase from cucumber, D-3-phosphoglycerate dehydrogenase and erythronate 4-phosphate dehydrogenase from Escherichia coli showed 38%, 24%, 24% and 22% amino acid identity, respectively. The profile analysis of the aligned sequences confirmed their relatedness. The hydropathy profiles of the aligned dehydrogenases were almost identical between residues 100-300 indicating largely preserved folding patterns of their polypeptide chains. The data suggest that L- and D-specific 2-hydroxy acid dehydrogenase genes evolved from two different ancestors and thus represent two different sets of enzyme families. |
| Links | |
| Keywords |
Alcohol Oxidoreductases/genetics; Amino Acid Sequence; Biological Evolution; Carbohydrate Dehydrogenases/genetics; Databases, Factual; Escherichia coli/genetics; Escherichia coli Proteins; L-Lactate Dehydrogenase/genetics; Lactobacillus casei/genetics; Molecular Sequence Data; NAD/metabolism; Phosphoglycerate Dehydrogenase; Plants/enzymology; Protein Conformation; Sequence Homology, Nucleic Acid; Software |
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