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-CHR3-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 Mr 52000 is present in M. tuberculosis. The 49 kDa PBP is sensitive towards amoxycillin, imipenem, flomoxef and cefoxitin.
Biochemical characterization of the 49 kDa penicillin-binding protein of Mycobacterium smegmatis
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Tapan MUKHERJEE, Dhiman BASU, Sebabrata MAHAPATRA, Colette GOFFIN, Jos van BEEUMEN, Joyoti BASU; Biochemical characterization of the 49 kDa penicillin-binding protein of Mycobacterium smegmatis. Biochem J 15 November 1996; 320 (1): 197–200. doi: https://doi.org/10.1042/bj3200197
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