title: Characterization of a 38 kDa penicillin-binding protein and its possible involvement in maintaining stationary-phase cells of Shigella dysenteriae.
abstract: This paper reports the first attempt to characterize the penicillin-binding proteins (PBPs) of Shigella dysenteriae, an important human pathogen. The PBP pattern of the membranes of S. dysenteriae closely resembles that of Escherichia coli membranes. A 38 kDa PBP which is an important target for the penem SCH34343, the cephamycin cefoxitin and the oxacephem moxalactam, has been purified. This PBP is immunologically related to a PBP of similar molecular mass in E. coli and is present at high levels in stationary-phase cells of S. dysenteriae.
authors: Department of Chemistry, Bose Institute, Calcutta, India.
authors: S
authors: S
authors: Mahapatra
authors: J
authors: J
authors: Basu
authors: J
authors: J
authors: van Beeumen
authors: M
authors: M
authors: Kundu
mesh_terms: D000595:Amino Acid Sequence; D000900:Anti-Bacterial Agents / Q000378:metabolism* / Q000494:pharmacology; D001426:Bacterial Proteins; D002352:Carrier Proteins / Q000276:immunology / Q000302:isolation & purification*; D003429:Cross Reactions; D004150:Dipeptidases; D010450:Endopeptidases / Q000032:analysis; D004926:Escherichia coli / Q000737:chemistry / Q000276:immunology; D006602:Hexosyltransferases; D007769:Lactams; D008826:Microbial Sensitivity Tests; D008969:Molecular Sequence Data; D002267:Muramoylpentapeptide Carboxypeptidase / Q000276:immunology / Q000302:isolation & purification*; D046915:Penicillin-Binding Proteins; D010458:Peptidyl Transferases; D017421:Sequence Analysis; D012762:Shigella dysenteriae / Q000737:chemistry*
chemical_list: D000900:Anti-Bacterial Agents; D001426:Bacterial Proteins; D002352:Carrier Proteins; D007769:Lactams; D046915:Penicillin-Binding Proteins; D010458:Peptidyl Transferases; D006602:Hexosyltransferases; D010450:Endopeptidases; D004150:Dipeptidases; C019989:DD-carboxypeptidase-endopeptidase; D002267:Muramoylpentapeptide Carboxypeptidase