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Article

Kinetic isotope effects for alkaline phosphatase reactions: implications for the role of active-site metal ions in catalysis.

Journal of the American Chemical Society - 8 Aug 2007

Zalatan Jesse G, Catrina Irina, Mitchell Rebecca, Grzyska Piotr K, O'brien Patrick J, Herschlag Daniel, Hengge Alvan C

Abstract excerpt

Enzyme-catalyzed phosphoryl transfer reactions have frequently been suggested to proceed through transition states that are altered from their solution counterparts, with the alterations presumably arising from interactions with active-site functional groups. In particular, the phosphate monoester hydrolysis reaction catalyzed by Escherichia coli alkaline phosphatase (AP) has been the subject of intensive...

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Identifiers

PMID: 17630738
DOI: 10.1021/ja072196+
PMCID: PMC3171187

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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