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Article

Mutational analysis of the active site flap (20s loop) of mandelate racemase.

Biochemistry - 15 Jan 2008

Bourque Jennifer R, Bearne Stephen L

Abstract excerpt

Mandelate racemase from Pseudomonas putida catalyzes the Mg2+-dependent 1,1-proton transfer that interconverts the enantiomers of mandelate. Residues of the 20s and 50s loops determine, in part, the topology and polarity of the active site and hence the substrate specificity. Previously, we proposed that, during racemization, the phenyl ring of mandelate moves between an S-pocket comprised of residues from the...

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PMID: 18092808
DOI: 10.1021/bi7015525

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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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