Probing the specificity of the S1 binding site of M222 mutants of subtilisin B. lentus with boronic acid inhibitors

Autor:	W. George Lai, J. Bryan Jones, Thomas P. Graycar, Grace Desantis, Richard R. Bott, Colin Mitchinson, Marvin Gold, Michele R. Stabile, Chung-Cheng Liu
Rok vydání:	1996
Předmět:	inorganic chemicals chemistry.chemical_classification Stereochemistry Chemistry Organic Chemistry Clinical Biochemistry Mutant Subtilisin Pharmaceutical Science Biochemistry chemistry.chemical_compound Enzyme Drug Discovery Electrophile Molecular Medicine Binding site Molecular Biology Boronic acid
Zdroj:	Bioorganic & Medicinal Chemistry Letters. 6:2501-2506
ISSN:	0960-894X
Popis:	Specificity differences between the S1-pockets of subtilisin B. lentus (SBL), and its M222C/S mutants have been explored with boronic acid inhibitors. Similar binding trends were noted, with 2,4-dichlorophenylboronic acid being the best overall inhibitor for each enzyme. In addition, a correlation between inhibitor binding and the electrophilicity of boron was found for both the M222C and M222S enzymes. Specificity differences between the S 1-pockets of subtilisin from B. lentus (SBL), and its M222C/S mutants, have been explored with boronic acid inhibitors. Similar binding trends were noted, with 2,4-dichlorophenyl boronic acid being the best overall inhibitor for each enzyme. In addition, a correlation between inhibitor binding and the electrophilicity of boron was found for both M222C and M222S enzymes.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::5cd1e41c7539f4e021c1296837b6b9af https://doi.org/10.1016/0960-894x(96)00466-0 Zobrazit plný text záznamu Full Text from ScienceDirect