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J Bacteriol. 2007 Oct;189(20):7310-5. Epub 2007 Aug 10.

The thiamine kinase (YcfN) enzyme plays a minor but significant role in cobinamide salvaging in Salmonella enterica.

Author information

1
Department of Bacteriology, University of Wisconsin-Madison, 144A Enzyme Institute, Madison, WI 53726-4087, USA.

Abstract

Cobinamide (Cbi) salvaging is impaired, but not abolished, in a Salmonella enterica strain lacking a functional cobU gene. CobU is a bifunctional enzyme (NTP:adenosylcobinamide [NTP:AdoCbi] kinase, GTP:adenosylcobinamide-phosphate [GTP:AdoCbi-P] guanylyltransferase) whose AdoCbi kinase activity is necessary for Cbi salvaging in this bacterium. Inactivation of the ycfN gene in a DeltacobU strain abrogated Cbi salvaging. Introduction of a plasmid carrying the ycfN(+) allele into a DeltacobU DeltaycfN strain substantially restored Cbi salvaging. Mass spectrometry data indicate that when YcfN-enriched cell extracts were incubated with AdoCbi and ATP, the product of the reaction was AdoCbi-P. Results from bioassays confirmed that YcfN converted AdoCbi to AdoCbi-P in an ATP-dependent manner. YcfN is a good example of enzymes that are used by the cell in multiple pathways to ensure the salvaging of valuable precursors.

PMID:
17693493
PMCID:
PMC2168424
DOI:
10.1128/JB.00822-07
[Indexed for MEDLINE]
Free PMC Article

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