Biochemical characterization of the 49 kDa penicillin-binding protein of Mycobacterium smegmatis.
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.
Mukherjee
T
T
Department of Chemistry, Bose Institute, Calcutta, India.
Basu
D
D
Mahapatra
S
S
Goffin
C
C
van Beeumen
J
J
Basu
J
J
D000595:Amino Acid Sequence; D000900:Anti-Bacterial Agents / Q000378:metabolism; D001426:Bacterial Proteins; D002352:Carrier Proteins / Q000378:metabolism*; D002384:Catalysis; D006602:Hexosyltransferases; D006868:Hydrolysis; D007769:Lactams; D008969:Molecular Sequence Data; D002267:Muramoylpentapeptide Carboxypeptidase / Q000378:metabolism*; D009161:Mycobacterium / Q000378:metabolism*; D046915:Penicillin-Binding Proteins; D010406:Penicillins / Q000378:metabolism*; D010458:Peptidyl Transferases; D011485:Protein Binding; D017386:Sequence Homology, Amino Acid
D000900:Anti-Bacterial Agents; D001426:Bacterial Proteins; D002352:Carrier Proteins; D007769:Lactams; D046915:Penicillin-Binding Proteins; D010406:Penicillins; D010458:Peptidyl Transferases; D006602:Hexosyltransferases; D002267:Muramoylpentapeptide Carboxypeptidase