The complete primary structure of the allosteric L-lactate dehydrogenase from Lactobacillus casei.
The polypeptide chain of the allosteric L-lactate dehydrogenase (EC 1.1.1.27) of Lactobacillus casei consists of 325 amino acid residues. Despite the strikingly different enzymatic characteristics of the allosteric L-lactate dehydrogenase of L. casei and of the non-allosteric vertebrate enzymes, the sequence of the allosteric enzyme shows a distinct homology with that of the non-allosteric vertebrate enzymes (average identity: 37%). An especially high sequence homology can be identified within the active center (average identity: 70%). A clear deviation of the L. casei enzyme from the vertebrate enzyme is the lack of the first 12 amino acid residues at the N terminus and an additional 7 amino acid residues at the C terminus. The localization of the binding site of the allosteric effector D-fructose 1,6-bisphosphate and pH and effector-induced changes of the spectroscopic properties are discussed on the basis of the primary structure.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001665:Binding Sites; D055598:Chemical Phenomena; D002621:Chemistry; D002851:Chromatography, High Pressure Liquid; D006863:Hydrogen-Ion Concentration; D007770:L-Lactate Dehydrogenase / Q000302:isolation & purification*; D007780:Lacticaseibacillus casei / Q000201:enzymology*; D010446:Peptide Fragments / Q000302:isolation & purification; D013237:Stereoisomerism
D000596:Amino Acids; D010446:Peptide Fragments; D007770:L-Lactate Dehydrogenase