A Rigidifying Salt-Bridge Favors the Activity of Thermophilic Enzyme at High Temperatures at the Expense of Low-Temperature Activity
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AbstractBackground: Thermophilic enzymes are often less active than their mesophilic homologues at low temperatures. One hypothesis to explain this observation is that the extra stabilizing interactions increase the rigidity of thermophilic enzymes and hence reduce their activity. Here we employed a thermophilic acylphosphatase from Pyrococcus horikoshii and its homologous mesophilic acylphosphatase from human as a model to study how local rigidity of an active-site residue affects the enzymatic activity.
All Author(s) ListLam SY, Yeung RCY, Yu TH, Sze KH, Wong KB
Journal namePLoS Biology
Year2011
Month3
Day1
Volume Number9
Issue Number3
PublisherPUBLIC LIBRARY SCIENCE
ISSN1544-9173
LanguagesEnglish-United Kingdom
Web of Science Subject CategoriesBiochemistry & Molecular Biology; BIOCHEMISTRY & MOLECULAR BIOLOGY; Biology; BIOLOGY; Life Sciences & Biomedicine - Other Topics

Last updated on 2020-20-09 at 02:34