title: Additional data about thermolysin specificity in buffer- and glycerol-containing media.
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.
authors.affiliation: Laboratoire de Technologie Enzymatique, URA 1442 CNRS, Compiègne University, France.
authors.forename: T
authors.initials: T
authors.lastname: Ligné
authors.forename: E
authors.initials: E
authors.lastname: Pauthe
authors.forename: J P
authors.initials: JP
authors.lastname: Monti
authors.forename: G
authors.initials: G
authors.lastname: Gacel
authors.forename: V
authors.initials: V
authors.lastname: Larreta-Garde
mesh_terms: D002021:Buffers; D004305:Dose-Response Relationship, Drug; D005990:Glycerol / Q000494:pharmacology; D006868:Hydrolysis; D007700:Kinetics; D009842:Oligopeptides / Q000138:chemical synthesis / Q000378:metabolism; D013379:Substrate Specificity; D013820:Thermolysin / Q000187:drug effects / Q000378:metabolism*
chemical_list: D002021:Buffers; D009842:Oligopeptides; D013820:Thermolysin; D005990:Glycerol