Biomaterial Database

Interaction between the exocellular DD-carboxypeptidase-transpeptidase from Streptomyces R61, substrate and beta-lactam antibiotics. A choice of models. 1975

J M Frère, and J M Ghuysen, and H R Perkins

The interaction between the exocellular DD-carboxypeptidase-transpeptidase of Streptomyces R61 and beta-lactam antibiotics is a multistep process during which a rather stable enzyme - antibiotic complex is formed. This mechanism of interaction is compatible with Lineweaver-Burk plots that are typical of a competitive inhibition of the hydrolysis of the peptide donor by the antibiotic. In fact, however, the same Lineweaver-Burk plots can be obtained on the basis of a non-competitive type of inhibition. At present, a choice between the two models cannot be made.

UI	MeSH Term	Description	Entries
D007700	Kinetics	The rate dynamics in chemical or physical systems.
D008433	Mathematics	The deductive study of shape, quantity, and dependence. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)	Mathematic
D008956	Models, Chemical	Theoretical representations that simulate the behavior or activity of chemical processes or phenomena; includes the use of mathematical equations, computers, and other electronic equipment.	Chemical Models,Chemical Model,Model, Chemical
D010400	Penicillin G	A penicillin derivative commonly used in the form of its sodium or potassium salts in the treatment of a variety of infections. It is effective against most gram-positive bacteria and against gram-negative cocci. It has also been used as an experimental convulsant because of its actions on GAMMA-AMINOBUTYRIC ACID mediated synaptic transmission.	Benzylpenicillin,Benpen,Benzylpenicillin Potassium,Coliriocilina,Crystapen,Or-pen,Parcillin,Pekamin,Pengesod,Penibiot,Penicilina G Llorente,Penicillin G Jenapharm,Penicillin G Potassium,Penicillin G Sodium,Penicillin Grünenthal,Penilevel,Peniroger,Pfizerpen,Sodiopen,Sodipen,Sodium Benzylpenicillin,Sodium Penicillin,Unicilina,Ursopen,Van-Pen-G
D010404	Penicillin V	A broad-spectrum penicillin antibiotic used orally in the treatment of mild to moderate infections by susceptible gram-positive organisms.	Penicillin, Phenoxymethyl,Apocillin,Beromycin,Beromycin, Penicillin,Berromycin, Penicillin,Betapen,Fenoxymethylpenicillin,Pen VK,Penicillin V Potassium,Penicillin V Sodium,Penicillin VK,Phenoxymethylpenicillin,V-Cillin K,Vegacillin,Penicillin Beromycin,Penicillin Berromycin,Phenoxymethyl Penicillin,Potassium, Penicillin V,Sodium, Penicillin V,V Cillin K,V Sodium, Penicillin,VCillin K
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
D011485	Protein Binding	The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.	Plasma Protein Binding Capacity,Binding, Protein
D002228	Carbenicillin	Broad-spectrum semisynthetic penicillin derivative used parenterally. It is susceptible to gastric juice and penicillinase and may damage platelet function.	Carboxybenzyl Penicillin,Anabactyl,Carbapen,Carbecin,Carbenicillin Disodium,Geopen,Microcillin,Pyopen,Disodium, Carbenicillin,Penicillin, Carboxybenzyl
D002268	Carboxypeptidases	Enzymes that act at a free C-terminus of a polypeptide to liberate a single amino acid residue.	Carboxypeptidase