A unique cis -3-hydroxy- l -proline dehydratase in the enolase superfamily

Xinshuai Zhang, Ritesh Kumar, Matthew W. Vetting, Suwen Zhao, Matthew P. Jacobson, Steven C. Almo, John A. Gerlt

Research output: Contribution to journalArticlepeer-review


The genome of Labrenzia aggregata IAM 12614 encodes an uncharacterized member of the muconate lactonizing enzyme (MLE) subgroup of the enolase superfamily (UniProt ID A0NXQ8). The gene encoding A0NXQ8 is located between genes that encode members of the proline racemase superfamily, 4R-hydroxyproline 2-epimerase (UniProt ID A0NXQ7; 4HypE) and trans-3-hydroxy-l-proline dehydratase (UniProt ID A0NXQ9; t3LHypD). A0NXQ8 was screened with a library of proline analogues; two reactions were observed with cis-3-hydroxy-l-proline (c3LHyp), competing 2-epimerization to trans-3-hydroxy-d-proline (1,1-proton transfer) and dehydration to δ1-pyrroline-2-carboxylate (β-elimination; c3LHyp dehydratase), with eventual total dehydration. The genome context encoding A0NXQ8 both (1) confirms its novel c3LHyp dehydratase function and (2) provides evidence for metabolic pathways that allow L. aggregata to utilize several isomeric 3- and 4-hydroxyprolines as sole carbon sources.

Original languageEnglish (US)
Pages (from-to)1388-1391
Number of pages4
JournalJournal of the American Chemical Society
Issue number4
StatePublished - Feb 4 2015

ASJC Scopus subject areas

  • Catalysis
  • General Chemistry
  • Biochemistry
  • Colloid and Surface Chemistry


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