The ATP:Co(I)rrinoid Adenosyltransferase (CobA) Enzyme ofSalmonella enterica Requires the 2′-OH Group of ATP for Function and Yields Inorganic Triphosphate as Its Reaction Byproduct
Year: 2002
Type: article
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. (31)P NMR spectroscopy was used to identify inorganic triphosphate (PPP(i)) 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/PPP(i) ratio present in the reaction mixture was 1:2.5.
Source: Journal of Biological Chemistry
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: hybrid
Estimated APC paid: $3,430
Awards: G1150701164, G1203322648, G1651520518, G1916166509, WIDE-BORE 9.4 TESLA NMR SPECTROMETER FOR UW-MADISON, B12 Biosysthesis and Anaerobic Metabolism in Salmonella, National Biological NMR Facility at Madison, Biotechnology Training Program, Development of 750 MHz Spectroscopy at the National Magnetic Resonance Facility at Madison., National Biomedical NMR Resource at Madison, G6383842392, G8509822677, ENZYMES INVOLVED IN COENZYME B12 SYNTHESIS
OpenAlex ID: W2069695966