Identification of a penicillin-sensitive carboxypeptidase in the cellular slime mold Dictyostelium discoideum.
Penicillin binding proteins (PBPs) are penicillin-sensitive DD-peptidases catalyzing the terminal stages of bacterial cell wall assembly. We identified a Dictyostelium discoideum gene that encodes a protein of 522 amino acids showing similarity to Escherichia coli PBP4. The D. discoideum protein conserves three consensus sequences (SXXK, SXN and KTG) that are responsible for the catalytic activities of PBPs. The gene product prepared in the cell-free translation system showed carboxypeptidase activity but the activity was not detected in the presence of penicillin G. These results demonstrate that the D. discoideum gene encodes a eukaryotic form of penicillin-sensitive carboxypeptidase.
Yasukawa
Hiro
H
Division of Bioengineering, Faculty of Engineering, Toyama University, Japan. hiro@eng.toyama-u.ac.jp
Kuroita
Toshihiro
T
Tamura
Kentaro
K
Yamaguchi
Kazuo
K
D000595:Amino Acid Sequence / Q000187:drug effects / Q000502:physiology; D000818:Animals; D001483:Base Sequence / Q000187:drug effects / Q000502:physiology; D002268:Carboxypeptidases / Q000235:genetics / Q000378:metabolism*; D016837:Dictyosteliida / Q000187:drug effects* / Q000201:enzymology; D004023:Dictyostelium / Q000187:drug effects* / Q000201:enzymology; D004789:Enzyme Activation / Q000187:drug effects / Q000502:physiology; D008969:Molecular Sequence Data; D010406:Penicillins / Q000494:pharmacology*
D010406:Penicillins; D002268:Carboxypeptidases