PROTEOLYTIC INTERCONVERSION AND N-TERMINAL SEQUENCES OF THE CITROBACTER-DIVERSUS MAJOR BETA-LACTAMASES

被引:9
作者
FRANCESCHINI, N
AMICOSANTE, G
PERILLI, M
MACCARRONE, M
ORATORE, A
VANBEEUMEN, J
FRERE, JM
机构
[1] UNIV LAQUILA,DIPARTIMENTO SCI & TECNOL BIOMED & BIOMETRIA,CATTEDRA CHIM BIOL,I-67100 LAQUILA,ITALY
[2] STATE UNIV LIEGE,INST CHIM,ENZYMOL LAB,B-4000 LIEGE,BELGIUM
[3] STATE UNIV LIEGE,INST CHIM,SERV MICROBIOL,B-4000 LIEGE,BELGIUM
[4] STATE UNIV GHENT,MICROBIOL LAB,B-9000 GHENT,BELGIUM
关键词
D O I
10.1042/bj2750629
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 N-terminal sequences of the two major beta-lactamases produced by Citrobacter diversus differed only by the absence of the first residue in form II and the loss of five amino acid residues at the C-terminal end. Limited proteolysis of the homogeneous form I protein yielded a variety of enzymatically active products. In the major product obtained after the action of papain, the first three N-terminal residues of form I had been cleaved, whereas at the C-terminal end the treated enzyme lacked five residues. However, this cannot explain the different behaviours of form I, form II and papain digestion product upon chromatofocusing. Form I, which was sequenced up to position 56, exhibited a very high degree of similarity with a Klebsiella oxytoca beta-lactamase. The determined sequence, which contained the active serine residue, demonstrated that the chromosome-encoded beta-lactamase of Citrobacter diversus belong to class A.
引用
收藏
页码:629 / 633
页数:5
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