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 Alan Gerlt

Research output: Contribution to journalArticle

Abstract

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
Volume137
Issue number4
DOIs
StatePublished - Feb 4 2015

Fingerprint

Hydroxyproline
Hydro-Lyases
Phosphopyruvate Hydratase
Proline
dehydration
genome
Genes
Dehydration
gene
Gene encoding
Proton transfer
Genome
enzyme
carbon
Carbon
Metabolic Networks and Pathways
Protons
Enzymes
library

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

Cite this

A unique cis -3-hydroxy- l -proline dehydratase in the enolase superfamily. / Zhang, Xinshuai; Kumar, Ritesh; Vetting, Matthew W.; Zhao, Suwen; Jacobson, Matthew P.; Almo, Steven C.; Gerlt, John Alan.

In: Journal of the American Chemical Society, Vol. 137, No. 4, 04.02.2015, p. 1388-1391.

Research output: Contribution to journalArticle

Zhang, X, Kumar, R, Vetting, MW, Zhao, S, Jacobson, MP, Almo, SC & Gerlt, JA 2015, 'A unique cis -3-hydroxy- l -proline dehydratase in the enolase superfamily', Journal of the American Chemical Society, vol. 137, no. 4, pp. 1388-1391. https://doi.org/10.1021/ja5103986
Zhang X, Kumar R, Vetting MW, Zhao S, Jacobson MP, Almo SC et al. A unique cis -3-hydroxy- l -proline dehydratase in the enolase superfamily. Journal of the American Chemical Society. 2015 Feb 4;137(4):1388-1391. https://doi.org/10.1021/ja5103986
Zhang, Xinshuai ; Kumar, Ritesh ; Vetting, Matthew W. ; Zhao, Suwen ; Jacobson, Matthew P. ; Almo, Steven C. ; Gerlt, John Alan. / A unique cis -3-hydroxy- l -proline dehydratase in the enolase superfamily. In: Journal of the American Chemical Society. 2015 ; Vol. 137, No. 4. pp. 1388-1391.
@article{b5974a6be43b4f9794a244db74a84df9,
title = "A unique cis -3-hydroxy- l -proline dehydratase in the enolase superfamily",
abstract = "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.",
author = "Xinshuai Zhang and Ritesh Kumar and Vetting, {Matthew W.} and Suwen Zhao and Jacobson, {Matthew P.} and Almo, {Steven C.} and Gerlt, {John Alan}",
year = "2015",
month = "2",
day = "4",
doi = "10.1021/ja5103986",
language = "English (US)",
volume = "137",
pages = "1388--1391",
journal = "Journal of the American Chemical Society",
issn = "0002-7863",
publisher = "American Chemical Society",
number = "4",

}

TY - JOUR

T1 - A unique cis -3-hydroxy- l -proline dehydratase in the enolase superfamily

AU - Zhang, Xinshuai

AU - Kumar, Ritesh

AU - Vetting, Matthew W.

AU - Zhao, Suwen

AU - Jacobson, Matthew P.

AU - Almo, Steven C.

AU - Gerlt, John Alan

PY - 2015/2/4

Y1 - 2015/2/4

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=84922366171&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84922366171&partnerID=8YFLogxK

U2 - 10.1021/ja5103986

DO - 10.1021/ja5103986

M3 - Article

VL - 137

SP - 1388

EP - 1391

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

SN - 0002-7863

IS - 4

ER -