SEQUENCE-ANALYSIS OF THE L1 METALLO-BETA-LACTAMASE FROM XANTHOMONAS-MALTOPHILIA

被引:141
作者
WALSH, TR
HALL, L
ASSINDER, SJ
NICHOLS, WW
CARTWRIGHT, SJ
MACGOWAN, AP
BENNETT, PM
机构
[1] UNIV BRISTOL,DEPT BIOCHEM,BRISTOL,ENGLAND
[2] ZENECA PHARMACEUT,MACCLESFIELD,ENGLAND
[3] NHS TRUST,SOUTHMEAD HLTH SERV,REG ANTIMICROBIAL REFERENCE LAB,BRISTOL,AVON,ENGLAND
[4] UNIV OXFORD,SIR WILLIAM DUNN SCH PATHOL,OXFORD OX1 3RE,ENGLAND
来源
BIOCHIMICA ET BIOPHYSICA ACTA-GENE STRUCTURE AND EXPRESSION | 1994年 / 1218卷 / 02期
关键词
METALLOENZYME; BETA-LACTAMASE; CARBAPENEM RESISTANCE;
D O I
10.1016/0167-4781(94)90011-6
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
The amino acid sequence deduced from the L1 beta-lactamase gene of Xanthomonas maltophilia shows a significant variation from that of the CphA and Blm metallo-beta-lactamases of Aeromonas hydrophila and Bacillus cereus, respectively. Whilst the N-terminus of the L1 protein shows some similarity, particularly at the histidine residues previously suggested as a zinc-binding motif, the C-terminus of the protein demonstrates very little similarity. Such differences amongst this group of enzymes would argue for at least three subclasses within the Group 3 beta-lactamases. However, in order to predict their phylogenetic ancestry more sequence data are required from other possible metallo-beta-lactamases.
引用
收藏
页码:199 / 201
页数:3
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