Amino acid sequence of a dodecapeptide from the substrate-binding region of the L-lactate dehydrogenase from Lactobacillus curvatus, Lactobacillus xylosus and Bacillus stearothermophilus.
The amino acid sequence of dodecapeptides from the substrate-binding region of 3 bacterial L-lactate dehydrogenases (Lactobacillus xylosus, Lactobacillus curvatus and Bacillus stearothermophilus) were determined. They show a very high homology to the sequences of the corresponding known animal enzymes. There is, however, an essential difference between the sequences of pro- and eucaryotic enzymes: the Asn residue in position 166, common to all eucaryotes, is replaced by serine in lactobacilli and by isoleucine in Bacillus stearothermophilus. The cysteine residue in position 165, formerly considered as essential, seems to be restricted to the vertebrates, while all so far investigated invertebrates and bacteria have threonine at this position.
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D001411:Geobacillus stearothermophilus / Q000201:enzymology*; D007770:L-Lactate Dehydrogenase / Q000378:metabolism; D007778:Lactobacillus / Q000201:enzymology*; D013045:Species Specificity
D007770:L-Lactate Dehydrogenase