Premium
Series mechanism of enzyme deactivation. Characterization of intermediate forms
Author(s) -
Gianfreda Liliana,
Marrucci Giuseppe,
Grizzuti Nino,
Greco Guido
Publication year - 1985
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260270618
Subject(s) - enzyme , chemistry , hydrolysis , kinetics , stereochemistry , phosphate , degradation (telecommunications) , organic chemistry , telecommunications , physics , quantum mechanics , computer science
Acid phosphatase (E.C. 3.1.3.2) undergoes complex thermal deactivation phenomena, as revealed by the two‐slope pattern of the enzyme logarithmic‐specific‐activity versus time curves. The native enzyme first decays toward an equilibrium distribution of less, but still active, intermediate structures and these, in turn, undergo a final degradation to a completely inactive form. The effect of the experimental conditions at which the enzyme is kept during the deactivation process on the characteristics of these intermediate enzymatic structures has been investigated. The kinetic parameters of p ‐nitro‐phenyl phosphate hydrolysis, as catalyzed by some of these intermediate forms, have been determined and the results compared to those obtained with the native enzyme.