Penicillin-binding and degrading enzymes

被引：53
作者：
Herzberg, Osnat [1 ]
Moult, John [1 ]
机构：
[1] Univ Maryland, Maryland Biotechnol Inst, Ctr Adv Res Biotechnol, 9600 Gudelsky Dr, Rockville, MD 20850 USA
来源：
CURRENT OPINION IN STRUCTURAL BIOLOGY | 1991年 / 1卷 / 06期
关键词：
D O I：
10.1016/0959-440X(91)90090-G
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Within the past year, two refined crystal structures of class-A beta-lactamases have been reported, adding accurate structural details to previous crystallographic work on various beta-lactamases and one penicillin-binding protein. In addition, mutagenesis data linked to kinetic analysis are accumulating rapidly. Proposals concerning the catalytic mechanism, substrate specificity, and folding properties of this important group of enzymes may now be tested more rigorously using these data.
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页码：946 / 953
页数：8
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