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Lactate dehydrogenase interaction with lactate analogs

, : Lactate dehydrogenase interaction with lactate analogs. Bioorganicheskaya Khimiya 3(4): 529-536

A study was performed on swine muscle lactate dehydrogenase (LDH) M4 interaction with the analogs of lactate. Carboxy, methoxy and hydroxy groups of substrates were shown to bind to the respective loci of the active site. The analogs comprising cyclic nonpolar moieties form stable complexes which are incapable of further reaction. Analysis of model of LDH 3-dimensional structure allowed to suggest that methyl group of lactate molecule interacts with a locus in the vicinity of Tyr 246 and Val 241 residues. It is only for ternary complexes formed by LDH.cntdot.NAD and lactate or its analogs that deprotonation of a functional group (presumably, that of histidine) in the active site does occur. In complexes with NADH, protonation is observed independent of substrate structure.


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