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A pyridoxal phosphate–dependent enzyme that oxidizes an unactivated carbon-carbon bond

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Du, Yi-Ling, Singh, Rahul, Alkhalaf, Lona M., Kuatsjah, Eugene, He, Hai-Yan, Eltis, Lindsay D. and Ryan, Katherine S. (2016) A pyridoxal phosphate–dependent enzyme that oxidizes an unactivated carbon-carbon bond. Nature Chemical Biology, 12 (3). pp. 194-199. doi:10.1038/nchembio.2009

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Official URL: http://dx.doi.org/10.1038/nchembio.2009

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Abstract

Pyridoxal 5′-phosphate (PLP)-dependent enzymes have wide catalytic versatility but are rarely known for their ability to react with oxygen to catalyze challenging reactions. Here, using in vitro reconstitution and kinetic analysis, we report that the indolmycin biosynthetic enzyme Ind4, from Streptomyces griseus ATCC 12648, is an unprecedented O2- and PLP-dependent enzyme that carries out a four-electron oxidation of L-arginine, including oxidation of an unactivated carbon-carbon (C-C) bond. We show that the conjugated product of this reaction, which is susceptible to nonenzymatic deamination, is efficiently intercepted and stereospecifically reduced by the partner enzyme Ind5 to give D-4,5-dehydroarginine. Thus, Ind4 couples the redox potential of O2 with the ability of PLP to stabilize anions to efficiently oxidize an unactivated C-C bond, with the subsequent stereochemical inversion by Ind5 preventing off-pathway reactions. Altogether, these results expand our knowledge of the catalytic versatility of PLP-dependent enzymes and enrich the toolbox for oxidative biocatalysis.

Item Type: Journal Article
Divisions: Faculty of Science, Engineering and Medicine > Science > Chemistry
Journal or Publication Title: Nature Chemical Biology
Publisher: Nature Publishing Group
ISSN: 1552-4450
Official Date: 25 January 2016
Dates:
DateEvent
25 January 2016Published
2 December 2015Accepted
Volume: 12
Number: 3
Page Range: pp. 194-199
DOI: 10.1038/nchembio.2009
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Restricted or Subscription Access

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