Affinity labelling of the allosteric site of the L-lactate dehydrogenase of Lactobacillus casei.
Kinetic investigations employing the substrate analogues 2-oxoglutarate and phospho(enol)pyruvate indicate that the allosteric L-lactate dehydrogenase (EC 1.1.1.27) of Lactobacillus casei has a non-catalytic pyruvate-binding site to which, in addition to pyruvate, the allosteric effector fructose 1,6-bisphosphate can also be found. A modification using the 14C-labelled substrate analogue 3-bromopyruvate induces a loss of regulation by fructose 1,6-bisphosphate. The histidine residue labelled by 3-bromopyruvate is homologous to histidine-188 which is part of the anion-binding site of the non-allosteric vertebrate L-lactate dehydrogenases. Thus, the allosteric site of the allosteric L-lactate dehydrogenases corresponds to the anion-binding site of the non-allosteric vertebrate enzymes.
D000345:Affinity Labels; D000495:Allosteric Site; D000596:Amino Acids / Q000302:isolation & purification; D055598:Chemical Phenomena; D002621:Chemistry; D002851:Chromatography, High Pressure Liquid; D007770:L-Lactate Dehydrogenase / Q000302:isolation & purification*; D007780:Lacticaseibacillus casei / Q000201:enzymology*; D010446:Peptide Fragments / Q000302:isolation & purification; D013237:Stereoisomerism
D000345:Affinity Labels; D000596:Amino Acids; D010446:Peptide Fragments; D007770:L-Lactate Dehydrogenase