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A 10 10 Rate Enhancement of Phosphodiester Hydrolysis by a Dinuclear Aminopeptidase—Transition‐State Analogues as Substrates?
Author(s) -
Park Hyun Ik,
Ming LiJune
Publication year - 1999
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/(sici)1521-3773(19991004)38:19<2914::aid-anie2914>3.0.co;2-p
Subject(s) - phosphodiester bond , hydrolysis , aminopeptidase , chemistry , reaction rate constant , phosphodiesterase , stereochemistry , biochemistry , kinetics , enzyme , amino acid , leucine , rna , physics , quantum mechanics , gene
Streptomyces dizinc aminopeptidase (sAP) shows a specific activity of 33.7 nmol min −1 mg −1 toward the hydrolysis of the transition‐state analogue bis‐ p ‐nitrophenylphosphate with a rate constant of k cat / K m =100 M −1 s −1 and a first‐order rate enhancement of about 10 10 , which is much superior to several Zn chemical models and comparable to some phosphodiesterases. This study suggests that sAP can serve as a novel dinuclear model system to provide further insight into dinuclear hydrolysis.