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A Unique cis-3-Hydroxy-l-proline Dehydratase in the Enolase Superfamily

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† ‡ Departments of Biochemistry and Chemistry and Institute for Genomic Biology, University of Illinois at Urbana−Champaign, Urbana, Illinois 61801, United States
§ Department of Biochemistry, Albert Einstein College of Medicine, Bronx, New York 10461, United States
Department of Pharmaceutical Chemistry, University of California, San Francisco, California 94143, United States
Cite this: J. Am. Chem. Soc. 2015, 137, 4, 1388–1391
Publication Date (Web):January 21, 2015
Copyright © 2015 American Chemical Society

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    Abstract Image

    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.

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    Cited By

    This article is cited by 11 publications.

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    5. Matthew D. Lloyd, Maksims Yevglevskis, Amit Nathubhai, Tony D. James, Michael D. Threadgill, Timothy J. Woodman. Racemases and epimerases operating through a 1,1-proton transfer mechanism: reactivity, mechanism and inhibition. Chemical Society Reviews 2021, 50 (10) , 5952-5984.
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    8. Seiya Watanabe, Fumiyasu Fukumori, Mao Miyazaki, Shinya Tagami, Yasuo Watanabe, . Characterization of a Novel cis -3-Hydroxy- l -Proline Dehydratase and a trans -3-Hydroxy- l -Proline Dehydratase from Bacteria. Journal of Bacteriology 2017, 199 (16)
    9. Seiya Watanabe, Kunihiko Tajima, Satoshi Fujii, Fumiyasu Fukumori, Ryotaro Hara, Rio Fukuda, Mao Miyazaki, Kuniki Kino, Yasuo Watanabe. Functional characterization of aconitase X as a cis-3-hydroxy-L-proline dehydratase. Scientific Reports 2016, 6 (1)
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    11. John A. Gerlt, Jason T. Bouvier, Daniel B. Davidson, Heidi J. Imker, Boris Sadkhin, David R. Slater, Katie L. Whalen. Enzyme Function Initiative-Enzyme Similarity Tool (EFI-EST): A web tool for generating protein sequence similarity networks. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 2015, 1854 (8) , 1019-1037.

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