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Mutants of 4-oxalocrotonate tautomerase catalyze the decarboxylation of oxaloacetate through an imine mechanism.

Chembiochem : a European journal of chemical biology - 2 Sept 2002

Brik Ashraf, D'Souza Lawrence J, Keinan Ehud, Grynszpan Flavio, Dawson Philip E

Abstract excerpt

A designed single amino acid substitution can alter the catalytic activity and mechanism of 4-oxalocrotonate tautomerase (4-OT). While the wild-type enzyme catalyzes only the tautomerization of oxalocrotonate, the Pro1Ala mutant (P1A) catalyzes two reactions--the original tautomerization reaction...

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PMID: 12210985
DOI: 10.1002/1439-7633(20020902)3:9<845::AID-CBIC845>3.0.CO;2-2

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-12210985-2026-09-02.1. Manifest publication-graph-cohort-2026-09-02.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

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