University of Messina, Dept. of Chemical, Biological, Pharmaceutical and Environmental Sciences, Viale F. Stagno d'Alcontres 31, Messina, Italy.
Curr Med Chem. 2019;26(18):3242-3252. doi: 10.2174/0929867324666170209103444.
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.
乳酸脱氢酶（LHD）是几乎所有生物中无氧代谢的关键酶，也是糖异生和单链 DNA 代谢过程中葡萄糖恢复的功能检查点。这种酶在进化过程中具有良好的保守结构，在物种之间，其氨基酸序列只有很小但有时非常有用的变化，这使其成为设计和构建能够调节其催化潜能和表达的功能分子的有吸引力的目标。研究主要集中在调节剂的选择上，特别是针对 LDH 同工酶（特别是 LDH-5）和恶性疟原虫乳酸脱氢酶（pfLDH）。本文综述了抑制剂的设计和开发的最新进展，指出了它们的特异性和治疗潜力。
