PMID: 9003446Jan 4, 1997Paper

Additional data about thermolysin specificity in buffer- and glycerol-containing media

Biochimica Et Biophysica Acta
T LignéV Larreta-Garde

Abstract

Synthesis and use of various substrates permit an improved approach to thermolysin-peptide recognition and elucidation of several new criteria affecting enzyme specificity. Nature and position of the recognized residue, role of adjacent amino acids, lateral chain hydrophobicity, and volume and length of peptides were all considered. Hydrolysis reactions were also carried out in the presence of glycerol; the effect of microenvironment modifications was quantitative, for example in inducing variations in catalytic reaction rates, and also qualitative, such as in influencing affinity.

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Citations

Jun 23, 2000·Enzyme and Microbial Technology·G R Castro
Sep 2, 2009·Bioorganic & Medicinal Chemistry Letters·Ann-Kathrin Marguerre, Roland Krämer
Jan 21, 2009·Chemical Biology & Drug Design·Olayiwola A Adekoya, Ingebrigt Sylte
Feb 3, 1999·Annals of the New York Academy of Sciences·E PautheV Larreta-Garde
Feb 11, 2005·Journal of Biomolecular Structure & Dynamics·Olayiwola A AdekoyaIngebrigt Sylte
Apr 26, 2011·Journal of the American Chemical Society·Garima GhaleWerner M Nau
Oct 16, 2007·Bioorganic & Medicinal Chemistry Letters·Jennifer K MitchellRonald J Quinn
Jul 3, 2019·Journal of Agricultural and Food Chemistry·Ya-Hui ShihJue-Liang Hsu

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