Mukherjee T, Basu D, Mahapatra S, Goffin C, van Beeumen J, Basu J
Department of Chemistry, Bose Institute, Calcutta, India.
Biochem J. 1996 Nov 15;320 ( Pt 1)(Pt 1):197-200. doi: 10.1042/bj3200197.
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.
耻垢分枝杆菌的49 kDa青霉素结合蛋白（PBP）催化羰基供体R1-CONH-CHR2-COX-CHR2-COO-（其中X为NH或S）的肽键或S-酯键水解。在合适的氨基受体存在下，反应在转肽和水解途径之间进行分配，氨基受体在酰基酶水平上作为简单的替代亲核试剂。由于其N端序列相似性，49 kDa PBP代表单功能低分子量PBPs类别之一。结核分枝杆菌中存在一种分子量为52,000的免疫相关蛋白。49 kDa PBP对阿莫西林、亚胺培南、氟氧头孢和头孢西丁敏感。
