Biochemistry, Department of
Document Type
Article
Date of this Version
2002
Citation
The Journal of Biological Chemistry, Vol. 277, No. 36, Issue of September 6, pp. 33127–33131, 2002
Abstract
The specificity of the ATP:corrinoid adenosyltransferase
(CobA) enzyme of Salmonella enterica serovar
Typhimurium LT2 for its nucleotide substrate was
tested using ATP analogs and alternative nucleotide donors.
The enzyme showed broad specificity for the nucleotide
base and required the 2’-OH group of the ribosyl
moiety of ATP for activity. 31P NMR spectroscopy
was used to identify inorganic triphosphate (PPPi) as
the byproduct of the reaction catalyzed by the CobA
enzyme. Cleavage of triphosphate into pyrophosphate
and orthophosphate did not occur, indicating that
triphosphate cleavage was not required for release of
the adenosylcorrinoid product. Triphosphate was a
strong inhibitor of the reaction, with 85% of CobA activity
lost when the ATP/PPPi ratio present in the reaction
mixture was 1:2.5.
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Comments
Copyright 2002 by The American Society for Biochemistry and Molecular Biology, Inc.