P. K. Mishra, Peter K. Park, D. Drueckhammer
May 1, 2001
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Influential Citations
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Journal
Journal of Bacteriology
Abstract
ABSTRACT Dephosphocoenzyme A (dephospho-CoA) kinase catalyzes the final step in coenzyme A biosynthesis, the phosphorylation of the 3′-hydroxy group of the ribose sugar moiety. Wild-type dephospho-CoA kinase fromCorynebacterium ammoniagenes was purified to homogeneity and subjected to N-terminal sequence analysis. A BLAST search identified a gene from Escherichia coli previously designated yacE encoding a highly homologous protein. Amplification of the gene and overexpression yielded recombinant dephospho-CoA kinase as a 22.6-kDa monomer. Enzyme assay and nuclear magnetic resonance analyses of the product demonstrated that the recombinant enzyme is indeed dephospho-CoA kinase. The activities with adenosine, AMP, and adenosine phosphosulfate were 4 to 8% of the activity with dephospho-CoA. Homologues of the E. colidephospho-CoA kinase were identified in a diverse range of organisms.