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Article

Perturbing the hydrophobic pocket of mandelate racemase to probe phenyl motion during catalysis.

Biochemistry - 28 Jun 2005

Siddiqi Ferhan, Bourque Jennifer R, Jiang Haiyan, Gardner Marieke, St Maurice Martin, Blouin Christian, Bearne Stephen L

Abstract excerpt

Mandelate racemase (MR, EC 5.1.2.2) from Pseudomonas putida catalyzes the Mg(2+)-dependent 1,1-proton transfer that interconverts the enantiomers of mandelate. Crystal structures of MR reveal that the phenyl group of all ground-state ligands is located within a hydrophobic cavity, remote from the site of proton abstraction. MR forms numerous electrostatic and H-bonding interactions with the alpha-OH and carboxyl...

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PMID: 15966725
DOI: 10.1021/bi0473096

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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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