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The Biochemical journal. 1996 Nov 15;320 ( Pt 1)(Pt 1):197-200. doi: 10.1042/bj3200197 Q24.32025

Biochemical characterization of the 49 kDa penicillin-binding protein of Mycobacterium smegmatis

龟分枝杆菌49千道尔顿肽聚糖交联酶的生化性质研究 翻译改进

T Mukherjee  1, D Basu, S Mahapatra, C Goffin, J van Beeumen, J Basu

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  • 1 Department of Chemistry, Bose Institute, Calcutta, India.
  • DOI: 10.1042/bj3200197 PMID: 8947487

    摘要 Ai翻译

    The 49 kDa penicillin-binding protein (PBP) of Mycobacterium smegmatis catalyses the hydrolysis of the peptide or S-ester bond of carbonyl donors R1-CONH-CHR2-COX-CHR2-COO- (where X is NH or S). In the presence of a suitable amino acceptor, the reaction partitions between the transpeptidation and hydrolysis pathways, with the amino acceptor, behaving as a simple alternative nucleophile at the level of the acyl-enzyme. By virtue of its N-terminal sequence similarity, the 49 kDa PBP represents one of the class of monofunctional low-molecular-mass PBPs. An immunologically related protein of M(r) 52,000 is present in M. tuberculosis. The 49 kDa PBP is sensitive towards amoxycillin, imipenem, flomoxef and cefoxitin.

    Keywords:penicillin-binding protein

    关键词:青霉素结合蛋白

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    期刊名:Biochemical journal

    缩写:BIOCHEM J

    ISSN:0264-6021

    e-ISSN:1470-8728

    IF/分区:4.3/Q2

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    Biochemical characterization of the 49 kDa penicillin-binding protein of Mycobacterium smegmatis