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Curr Med Chem. 2017 Feb 8. doi: 10.2174/0929867324666170209103444. [Epub ahead of print]

Lactate dehydrogenase inhibition: biochemical relevance and therapeutical potential.

Author information

1
University of Messina, Dept. of Chemical, Biological, Pharmaceutical and Environmental Sciences, Viale F. Stagno d'Alcontres 31, 98166,Italy.

Abstract

Lactate dehydrogenase (LHD) is a key enzyme of anaerobic metabolism in almost all living organisms and it is also a functional checkpoint for glucose restoration during gluconeogenesis and single-stranded DNA metabolism. This enzyme has a well preserved structure during evolution and among the species, with little, but sometimes very useful, changes in the amino acid sequence, which makes it an attractive target for the design and construction of functional molecules able to modulate its catalytic potential and expression. Research has focused mainly on the selection of modulator especially as far as LDH isozymes (especially LDH-5) and lactate dehydrogenases of Plasmodium falciparum (pfLDH) are concerned. This review summarizes the recent advances in the design and development of inhibitors, pointing out their specificity and therapeutic potentials.

KEYWORDS:

Lactate dehydrogenase; bifunctional inhibitor; enzyme inhibitor; galloflavin; miRNA and shRNAs.; oxamate and derivatives; quinoline derivatives

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