HOLY PROTEINS .2. THE SOLUBLE LYTIC TRANSGLYCOSYLASE

被引:34
作者
DIJKSTRA, BW [1 ]
THUNNISSEN, AMWH [1 ]
机构
[1] UNIV GRONINGEN,BIOSON,RES INST,DEPT CHEM,9747 AG GRONINGEN,NETHERLANDS
关键词
D O I
10.1016/0959-440X(94)90261-5
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
Enzymes involved in the metabolism of the bacterial cell wall peptidoglycan are excellent targets for antibiotics. Penicillins and related beta-lactam antibiotics inhibit the enzymes that act on the peptide cross-links of the peptidoglycan. The X-ray structure of the transglycosylase revealed a two-layered ring of alpha-helices in a right-handed superhelical arrangement with a separate catalytic domain on top, which resembles the fold of goose-type lysozyme. Three sequence motifs were found that characterize the catalytic and substrate-binding sites in the enzyme. These motifs are present in a broad family of muramidases and chitinases.
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收藏
页码:810 / 813
页数:4
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