Biomaterial Database

Penicillin-binding proteins in Streptomyces cacaoi. The effects on penicillin-binding proteins and the antibacterial activities of beta-lactams. 1980

H Ogawara, and S Horikawa

Penicillin-binding proteins (PBPs) in membrane of Streptomyces cacaoi were investigated by sodium dodecylsulfate-polyacrylamide gel electrophoresis-fluorography. At the same time, eleven beta-lactams were examined on the affinities for these PBPs and the antibacterial activities against S. cacaoi, comparing with those in Bacillus subtilis reported in the preceding paper. The affinity patterns of beta-lactams for PBPs both in S. cacaoi and B. subtilis were similar in many points. Here again, the grouping of beta-lactams based on the affinity for PBP-2 (M. W., 91,000) was in accord with that based on the antibacterial activity. These results suggest that among PBPs detected in S. cacaoi, PBP-2 is the most likely target of killing by these beta-lactam antibiotics.

UI	MeSH Term	Description	Entries
D008826	Microbial Sensitivity Tests	Any tests that demonstrate the relative efficacy of different chemotherapeutic agents against specific microorganisms (i.e., bacteria, fungi, viruses).	Bacterial Sensitivity Tests,Drug Sensitivity Assay, Microbial,Minimum Inhibitory Concentration,Antibacterial Susceptibility Breakpoint Determination,Antibiogram,Antimicrobial Susceptibility Breakpoint Determination,Bacterial Sensitivity Test,Breakpoint Determination, Antibacterial Susceptibility,Breakpoint Determination, Antimicrobial Susceptibility,Fungal Drug Sensitivity Tests,Fungus Drug Sensitivity Tests,Sensitivity Test, Bacterial,Sensitivity Tests, Bacterial,Test, Bacterial Sensitivity,Tests, Bacterial Sensitivity,Viral Drug Sensitivity Tests,Virus Drug Sensitivity Tests,Antibiograms,Concentration, Minimum Inhibitory,Concentrations, Minimum Inhibitory,Inhibitory Concentration, Minimum,Inhibitory Concentrations, Minimum,Microbial Sensitivity Test,Minimum Inhibitory Concentrations,Sensitivity Test, Microbial,Sensitivity Tests, Microbial,Test, Microbial Sensitivity,Tests, Microbial Sensitivity
D010406	Penicillins	A group of antibiotics that contain 6-aminopenicillanic acid with a side chain attached to the 6-amino group. The penicillin nucleus is the chief structural requirement for biological activity. The side-chain structure determines many of the antibacterial and pharmacological characteristics. (Goodman and Gilman's The Pharmacological Basis of Therapeutics, 8th ed, p1065)	Antibiotics, Penicillin,Penicillin,Penicillin Antibiotics
D010458	Peptidyl Transferases	Acyltransferases that use AMINO ACYL TRNA as the amino acid donor in formation of a peptide bond. There are ribosomal and non-ribosomal peptidyltransferases.	Peptidyl Transferase,Peptidyl Translocase,Peptidyl Translocases,Peptidyltransferase,Transpeptidase,Transpeptidases,Peptidyltransferases,Transferase, Peptidyl,Transferases, Peptidyl,Translocase, Peptidyl,Translocases, Peptidyl
D002267	Muramoylpentapeptide Carboxypeptidase	Enzyme which catalyzes the peptide cross-linking of nascent CELL WALL; PEPTIDOGLYCAN.	Carboxypeptidase Transpeptidase,Carboxypeptidase, Muramoylpentapeptide,Transpeptidase, Carboxypeptidase
D002352	Carrier Proteins	Proteins that bind or transport specific substances in the blood, within the cell, or across cell membranes.	Binding Proteins,Carrier Protein,Transport Protein,Transport Proteins,Binding Protein,Protein, Carrier,Proteins, Carrier
D005656	Fungal Proteins	Proteins found in any species of fungus.	Fungal Gene Products,Fungal Gene Proteins,Fungal Peptides,Gene Products, Fungal,Yeast Proteins,Gene Proteins, Fungal,Peptides, Fungal,Proteins, Fungal
D006602	Hexosyltransferases	Enzymes that catalyze the transfer of hexose groups. EC 2.4.1.-.
D001426	Bacterial Proteins	Proteins found in any species of bacterium.	Bacterial Gene Products,Bacterial Gene Proteins,Gene Products, Bacterial,Bacterial Gene Product,Bacterial Gene Protein,Bacterial Protein,Gene Product, Bacterial,Gene Protein, Bacterial,Gene Proteins, Bacterial,Protein, Bacterial,Proteins, Bacterial
D013302	Streptomyces	A genus of bacteria that form a nonfragmented aerial mycelium. Many species have been identified with some being pathogenic. This genus is responsible for producing a majority of the ANTI-BACTERIAL AGENTS of practical value.
D046915	Penicillin-Binding Proteins	Bacterial proteins that share the property of binding irreversibly to PENICILLINS and other ANTIBACTERIAL AGENTS derived from LACTAMS. The penicillin-binding proteins are primarily enzymes involved in CELL WALL biosynthesis including MURAMOYLPENTAPEPTIDE CARBOXYPEPTIDASE; PEPTIDE SYNTHASES; TRANSPEPTIDASES; and HEXOSYLTRANSFERASES.	Penicillin-Binding Protein,Penicillin-Binding Protein 1,Penicillin-Binding Protein 1A,Penicillin-Binding Protein 1b,Penicillin-Binding Protein 2,Penicillin-Binding Protein 2a,Penicillin-Binding Protein 2b,Penicillin-Binding Protein 3,Penicillin-Binding Protein 4,Penicillin-Binding Protein 5,Penicillin-Binding Protein 6,Penicillin-Binding Protein 7,Penicillin-Binding Protein-2a,Peptidoglycan Synthetase,Penicillin Binding Protein,Penicillin Binding Protein 1,Penicillin Binding Protein 1A,Penicillin Binding Protein 1b,Penicillin Binding Protein 2,Penicillin Binding Protein 2a,Penicillin Binding Protein 2b,Penicillin Binding Protein 3,Penicillin Binding Protein 4,Penicillin Binding Protein 5,Penicillin Binding Protein 6,Penicillin Binding Protein 7,Penicillin Binding Proteins,Protein 1A, Penicillin-Binding,Protein 1b, Penicillin-Binding,Proteins, Penicillin-Binding,Synthetase, Peptidoglycan