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B6db references: 26807714

type Journal Article
authors Du YL, Singh R, Alkhalaf LM, Kuatsjah E, He HY, Eltis LD, Ryan KS
title A pyridoxal phosphate-dependent enzyme that oxidizes an unactivated carbon-carbon bond
journal Nat Chem Biol
Activity ind4
Family ind4
sel selected
ui 26807714
year (2016)
volume 12
number 3
pages 194-9
keywords DOI: 10.1038/nchembio.2009
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.
last changed 2018/02/27 13:25

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