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Isotope effects in the study of enzymatic phosphoryl transfer reactions
Author(s) -
Hengge Alvan C
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02638-2
Subject(s) - chemistry , serine , threonine , enzyme , phosphorylation , lability , tyrosine , phosphatase , catalysis , enzyme catalysis , stereochemistry , kinetic isotope effect , biochemistry , physics , deuterium , quantum mechanics
Protein‐tyrosine phosphatases and serine/threonine protein phosphatases utilize very different catalytic machinery to catalyze phosphoryl transfer reactions. Tyrosine is a better leaving group than serine or threonine, having a p K a more than three units lower. Has the difference in the catalytic machinery used by these enzyme families evolved as a result of the difference in the lability of their substrates? Are the transition states for phosphoryl transfer similar for the two classes of enzymes? This review summarizes what has been learned from kinetic isotope effects about the nature of enzymatic phosphoryl transfer, and how the enzymatic mechanisms compare to uncatalyzed phosphoryl transfer reactions.