The Library
A pyridoxal phosphate–dependent enzyme that oxidizes an unactivated carbon-carbon bond
Tools
Tools
Tools
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
Research output not available from this repository.
Request-a-Copy directly from author or use local Library Get it For Me service.
Official URL: http://dx.doi.org/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.
| 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: |
|
||||||
| 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 |
Request changes or add full text files to a record
Repository staff actions (login required)
 |
View Item |
