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.
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
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DOI: 10.1042/bj3200197 PMID: 8947487
摘要 Ai翻译
Keywords:penicillin-binding protein
关键词:青霉素结合蛋白
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