Acta Phys. -Chim. Sin. ›› 2001, Vol. 17 ›› Issue (04): 333-337.doi: 10.3866/PKU.WHXB20010411

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Theoretical Studies on the Inhibition of L-lactate Dehydrogenase

Hou Ruo-Bing;Yi Xiang-Hui;Zeng Rong-Ying;Chen Zhi-Da   

  1. College of Chemistry and Life Sciences,Guangxi Normal University,Guilin 541004;State Key Laboratory of Rare Earth Material Chemistry and Application,Peking University,Beijing 100871
  • Received:2000-10-31 Revised:2000-12-11 Published:2001-04-15
  • Contact: Yi Xiang-Hui

Abstract: The model enzymatic inhibition mechanism by inhibitor oxamate has been studied at the HF/321G level. All the conclusions can be summarrized as follows:(a)the conformations of the optimized model inhibitor oxamate and substrate are much more similar with each other,which leads to an unidentified action of the substrate and inhibitor by Llactate dehydrogenase(LDH); (b)the electronic distribution of the inhibitor is favorable for the combination of oxamate to LDH active site; (3)the space of LDH active site is contracted by the inducedfit interaction between the LDH and the inhibitor;(4) the molecular fragment methyl of substrate and the residue Gln102 of LDH probably play an important role in the enzymatic reaction.

Key words: L-lactate dehydrogenase, Enzymatic reaction, Enzymatic inhibition, Ab initio, Molecular fragment