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Papers In Press, published online ahead of print April 29, 2002
Department of Cell Regulation, Ludwig Institute for Cancer Research, London W1W 7BS
Corresponding Author: ivan{at}ludwig.ucl.ac.uk
Coenzyme A functions as a carrier of acetyl and acyl groups in living cells and is essential for numerous biosynthetic, energy-yielding and degradative metabolic pathways. There are five enzymatic steps in CoA biosynthesis. To date, molecular cloning of enzymes involved in the CoA biosynthetic pathway in mammals has been only reported for Pantothenate kinase. In this study, we present cDNA cloning and functional characterisation of CoA synthase. It has an open reading frame of 563aa and encodes a protein of approximately 60kDa. Sequence alignments suggested that the protein possesses both phosphopantetheine adenylyltransferase and dephospho-CoA kinase domains. Biochemical assays using wild type recombinant protein confirmed the gene product indeed contained both these enzymatic activities. The presence of intrinsic phosphopantetheine adenylyltransferase activity was further confirmed by site-directed mutagenesis. Therefore, this study describes the first cloning and characterisation of a mammalian CoA synthase and confirms this is a bifunctional enzyme containing the last two components of CoA biosynthesis.
J. Biol. Chem, 10.1074/jbc.C200195200
Submitted on April 1, 2002
Revised on April 29, 2002
Accepted on April 29, 2002
Molecular cloning of CoA synthase: the missing link in CoA biosynthesis
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