| Literature DB >> 29106396 |
Jun Yan1,2,3,4,5, Meng Bi1, Allen K Bourdon6, Abigail T Farmer6, Po-Hsiang Wang7, Olivia Molenda7, Andrew T Quaile7, Nannan Jiang3,4,5,8, Yi Yang3,9, Yongchao Yin1, Burcu Şimşir3,9, Shawn R Campagna6, Elizabeth A Edwards7, Frank E Löffler1,3,4,5,8,9,10.
Abstract
Cobamides such as vitamin B12 are structurally conserved, cobalt-containing tetrapyrrole biomolecules that have essential biochemical functions in all domains of life. In organohalide respiration, a vital biological process for the global cycling of natural and anthropogenic organohalogens, cobamides are the requisite prosthetic groups for carbon-halogen bond-cleaving reductive dehalogenases. This study reports the biosynthesis of a new cobamide with unsubstituted purine as the lower base and assigns unsubstituted purine a biological function by demonstrating that Coα-purinyl-cobamide (purinyl-Cba) is the native prosthetic group in catalytically active tetrachloroethene reductive dehalogenases of Desulfitobacterium hafniense. Cobamides featuring different lower bases are not functionally equivalent, and purinyl-Cba elicits different physiological responses in corrinoid-auxotrophic, organohalide-respiring bacteria. Given that cobamide-dependent enzymes catalyze key steps in essential metabolic pathways, the discovery of a novel cobamide structure and the realization that lower bases can effectively modulate enzyme activities generate opportunities to manipulate functionalities of microbiomes.Entities:
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Year: 2017 PMID： 29106396 PMCID： PMC6081238 DOI： 10.1038/nchembio.2512
Source DB: PubMed Journal: Nat Chem Biol ISSN： 1552-4450 Impact factor: 15.040