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Salvage of the 5-deoxyribose byproduct of radical SAM enzymes.

Abstract：

:5-Deoxyribose is formed from 5'-deoxyadenosine, a toxic byproduct of radical S-adenosylmethionine (SAM) enzymes. The degradative fate of 5-deoxyribose is unknown. Here, we define a salvage pathway for 5-deoxyribose in bacteria, consisting of phosphorylation, isomerization, and aldol cleavage steps. Analysis of bacterial genomes uncovers widespread, unassigned three-gene clusters specifying a putative kinase, isomerase, and sugar phosphate aldolase. We show that the enzymes encoded by the Bacillus thuringiensis cluster, acting together in vitro, convert 5-deoxyribose successively to 5-deoxyribose 1-phosphate, 5-deoxyribulose 1-phosphate, and dihydroxyacetone phosphate plus acetaldehyde. Deleting the isomerase decreases the 5-deoxyribulose 1-phosphate pool size, and deleting either the isomerase or the aldolase increases susceptibility to 5-deoxyribose. The substrate preference of the aldolase is unique among family members, and the X-ray structure reveals an unusual manganese-dependent enzyme. This work defines a salvage pathway for 5-deoxyribose, a near-universal metabolite.

journal_name

Nat Commun

journal_title

Nature communications

authors

Beaudoin GAW,Li Q,Folz J,Fiehn O,Goodsell JL,Angerhofer A,Bruner SD,Hanson AD

doi

10.1038/s41467-018-05589-4

subject

Has Abstract

pub_date

2018-08-06 00:00:00

pages

3105

issue

1

issn

2041-1723

pii

10.1038/s41467-018-05589-4

journal_volume

9

pub_type

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