SUBSTRATE-SPECIFICITY AND INHIBITORS OF ASPARTIC PROTEINASES

被引:41
作者
KAY, J [1 ]
DUNN, BM [1 ]
机构
[1] UNIV FLORIDA,J HILLIS MILLER HLTH CTR,DEPT BIOCHEM & MOLEC BIOL,GAINESVILLE,FL 32610
关键词
ASPARTIC PROTEINASES; NATURALLY-OCCURRING AND RECOMBINANT; PEPSIN; RENIN; CHYMOSIN; CATHEPSIN-D; CATHEPSIN-E; HIV PROTEINASE; ACTIVE SITE MAPPING; INDIVIDUAL SUB-SITES; CHROMOGENIC SUBSTRATES; SPECIFIC INHIBITORS;
D O I
10.3109/00365519209104651
中图分类号
R-3 [医学研究方法]; R3 [基础医学];
学科分类号
1001 ;
摘要
Aspartic proteinases of vertebrate, fungal and retroviral origin have been characterised by utilisation of chromogenic peptide substrates and synthetic inhibitors as probes. By this means, the molecular topography of sub-sites within the active site cleft of individual enzymes has been elucidated. With suitable selection of residues to occupy each sub-site, the design of effective inhibitors specifically targetted against individual aspartic proteinases has become feasible.
引用
收藏
页码:23 / 30
页数:8
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