期刊
NATURE CHEMICAL BIOLOGY
卷 12, 期 3, 页码 194-199出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/NCHEMBIO.2009
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资金
- Genome British Columbia [SOF148]
- Natural Sciences and Engineering Research Council of Canada [402631-2011, 171359-13]
- Michael Smith Foundation for Health Research Trainee Award
- Canadian Institutes of Health Research New Investigator Award
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 O-2- 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 02 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.
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