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 con...

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Bibliographic Details
Published in:Biological & Pharmaceutical Bulletin 2003, Vol.26(7), pp.1018-1020
Main Authors: Yasukawa, Hiro, Kuroita, Toshihiro, Tamura, Kentaro, Yamaguchi, Kazuo
Format: Article
Language:English
Subjects:
Amino Acid Sequence - drug effects
Amino Acid Sequence - physiology
Analytical, structural and metabolic biochemistry
Animals
Base Sequence - drug effects
Base Sequence - physiology
Biological and medical sciences
carboxypeptidase
Carboxypeptidases - genetics
Carboxypeptidases - metabolism
Dictyosteliida - drug effects
Dictyosteliida - enzymology
Dictyostelium - drug effects
Dictyostelium - enzymology
Dictyostelium discoideum
Enzyme Activation - drug effects
Enzyme Activation - physiology
Fundamental and applied biological sciences. Psychology
Medical sciences
Molecular Sequence Data
penicillin binding protein
Penicillins - pharmacology
Pharmacology. Drug treatments
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Summary: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.
ISSN:0918-6158
1347-5215
DOI:10.1248/bpb.26.1018