CLOSE AMINO-ACID-SEQUENCE RELATIONSHIP BETWEEN THE NEW PLASMID-MEDIATED EXTENDED-SPECTRUM BETA-LACTAMASE-BULLET-MEN-1 AND CHROMOSOMALLY ENCODED ENZYMES OF KLEBSIELLA-OXYTOCA

被引：123

作者：

BARTHELEMY, M

PEDUZZI, J

BERNARD, H

TANCREDE, C

LABIA, R

机构：

[1] MUSEUM NATL HIST NAT, CNRS, URA 401, 63 RUE BUFFON, F-75231 PARIS 05, FRANCE

[2] INST GUSTAVE ROUSSY, SERV MICROBIOL MED, F-94805 VILLEJUIF, FRANCE

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1992年 / 1122卷 / 01期

关键词：

BETA-LACTAMASE; PLASMID-MEDIATED CEFOTAXIME-RESISTANCE; AMINO ACID SEQUENCE;

D O I：

10.1016/0167-4838(92)90121-S

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：

Isolated from an Escherichia coli strain MEN-1 is a plasmid-mediated beta-lactamase that confers resistance to methoxy imino third-generation cephalosporins. The protein purified to homogeneity was digested by trypsin, chymotrypsin and endoproteinase Asp-N. Amino acid sequence determinations of the resulting peptides gave rise to the alignment of the 263 residues of the beta-lactamase. From amino acid sequence comparison MEN-1 was found to share more than 72% identity with the chromosomally mediated beta-lactamases of Klebsiella oxytoca. Therefore, MEN-1 is the first transferable extended-spectrum beta-lactamase which is not directly derived from the widespread TEMs or SHV-1 penicillinases with which it presents less than 39% identity.

引用

页码：15 / 22

页数：8

共 49 条

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