L-乳酸脱氢酶抑制剂抑制成因的探讨

doi:10.3866/PKU.WHXB20010411

CORC > 北京大学 > 化学与分子工程学院

	L-乳酸脱氢酶抑制剂抑制成因的探讨; Theoretical studies on the inhibition of L-lactate dehydrogenase
	侯若冰 ; 义祥辉 ; 曾荣英 ; 陈志达
刊名	物理化学学报
	2001
关键词	L-乳酸脱氢酶酶促反应酶抑制剂从头计算分子片 L-lactate dehydrogenase enzymatic reaction enzymatic inhibition ab initio molecular fragment
DOI	10.3866/PKU.WHXB20010411
英文摘要	应用 HF/3 21G研究了抑制剂 H2N－ CO－ COO－对 L乳酸脱氢酶的抑制成因 .结果表明 ,酶被抑制的主要原因有 :(1)抑制剂与底物的稳定构象态在结构上极为相似 ,导致酶不能有效识别底物 ;(2)模型抑制剂各原子所带净电荷的优势使抑制剂更易与酶活性中心结合 ;(3)抑制剂通过对酶的诱导契合作用使酶活性中心的空间被缩小 ;(4)对活性中心有关结构的分析表明 ,底物的甲基分子片以及酶的氨基酸残基 Gln 102,对催化反应能否顺利进行 ,影响极大 .; 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.; http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000168268900011&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=8e1609b174ce4e31116a60747a720701 ; SCI(E); 中文核心期刊要目总览(PKU); 中国科学引文数据库(CSCD); 1; 04; 333-337; 17
语种	中文
内容类型	期刊论文
源URL	[http://ir.pku.edu.cn/handle/20.500.11897/397021]
专题	化学与分子工程学院
推荐引用方式 GB/T 7714	侯若冰,义祥辉,曾荣英,等. L-乳酸脱氢酶抑制剂抑制成因的探讨, Theoretical studies on the inhibition of L-lactate dehydrogenase[J]. 物理化学学报,2001.
APA	侯若冰,义祥辉,曾荣英,&陈志达.(2001).L-乳酸脱氢酶抑制剂抑制成因的探讨.物理化学学报.
MLA	侯若冰,et al."L-乳酸脱氢酶抑制剂抑制成因的探讨".物理化学学报 (2001).