Analysis of ThiC variants in the context of the metabolic network of Salmonella enterica.

Abstract:

:In bacteria, the 4-amino-hydroxymethyl-2-methylpyrimidine (HMP) moiety of thiamine is synthesized from 5-aminoimidazole ribotide (AIR), a branch point metabolite of purine and thiamine biosynthesis. ThiC is a member of the radical S-adenosylmethionine (AdoMet) superfamily and catalyzes the complex chemical rearrangement of AIR to HMP-P. As reconstituted in vitro, the ThiC reaction requires AdoMet, AIR, and reductant. This study analyzed variants of ThiC in vivo and in vitro to probe the metabolic network surrounding AIR in Salmonella enterica. Several variants of ThiC that required metabolic perturbations to function in vivo were biochemically characterized in vitro. Results presented herein indicate that the subtleties of the metabolic network have not been captured in the current reconstitution of the ThiC reaction.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Palmer LD,Dougherty MJ,Downs DM

doi

10.1128/JB.01361-12

subject

Has Abstract

pub_date

2012-11-01 00:00:00

pages

6088-95

issue

22

eissn

0021-9193

issn

1098-5530

pii

JB.01361-12

journal_volume

194

pub_type

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