Study of nucleophile binding in the penicillin acylase active center. Kinetic analysis

Autor:	M I, Youshko, A L, Bukhanov, V K, Svedas
Rok vydání:	2003
Předmět:	Kinetics Binding Sites Escherichia coli Proteins Hydrolysis Penicillanic Acid Reproducibility of Results Aminobenzoates Penicillin Amidase Catalysis Substrate Specificity
Zdroj:	Biochemistry. Biokhimiia. 68(3)
ISSN:	0006-2979
Popis:	The influence of the external nucleophile (6-aminopenicillanic acid) on the kinetics of the penicillin acylase-catalyzed acyl transfer reactions was studied using a highly sensitive spectrophotometric assay. An adequate kinetic scheme is suggested based on kinetic analysis of the experimental dependencies of the k(cat) and K(m) values on the nucleophile concentration. The proposed kinetic scheme has been verified by a quantitative description of the above-mentioned experimental dependencies using the set of kinetic parameters obtained from independent experiments. Such an approach can be used for modeling of different penicillin acylase-catalyzed acyl transfer reactions.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::fd83d81897b82fc75c4247bfa8e33243 https://pubmed.ncbi.nlm.nih.gov/12733976 Zobrazit plný text záznamu Full text from SpringerLink