Penicillin and beyond: Evolution, protein fold, multimodular polypeptides, and multiprotein complexes

被引:32
作者
Ghuysen, JM
Charlier, P
Coyette, J
Duez, C
Fonze, E
Fraipont, C
Goffin, C
Joris, B
NguyenDisteche, M
机构
[1] Centre d'Ingénierie des Protéines, Université de Liège, Institut de Chimie
关键词
D O I
10.1089/mdr.1996.2.163
中图分类号
R51 [传染病];
学科分类号
100401 ;
摘要
As the protein sequence and structure databases expand, the relationships between proteins, the notion of protein superfamily, and the driving forces of evolution are better understood, Key steps of the synthesis of the bacterial cell wall peptidoglycan are revisited in light of these advances. The reactions through which the D-alanyl-D-alanine depeptide is formed, utilized, and hydrolyzed and the sites of action of the glycopeptide and beta-lactam antibiotics illustrate the concept according to which new enzyme Functions evolve as a result of tinkering of existing proteins, This occurs by the acquisition of local structural changes, the fusion into multimodular polypeptides, and the association into multiprotein complexes.
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收藏
页码:163 / 175
页数:13
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