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Article

Kinetic isotope effects in the characterization of catalysis by protein tyrosine phosphatases.

Biochimica et biophysica acta - 1 Nov 2015

Hengge Alvan C

Abstract excerpt

Although thermodynamically favorable, the uncatalyzed hydrolysis of phosphate monoesters is extraordinarily slow, making phosphatases among the most catalytically efficient enzymes known. Protein-tyrosine phosphatases (PTPs) are ubiquitous in biology, and kinetic isotope effects were one of the key mechanistic tools used to discern molecular details of their catalytic mechanism and the transition state for...

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Identifiers

PMID: 25840000
DOI: 10.1016/j.bbapap.2015.03.010
PMCID: PMC4591087

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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