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Journal of Bacteriology, May 2001, p. 2774-2778, Vol. 183, No. 9
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.9.2774-2778.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Identification of yacE (coaE) as the Structural Gene for Dephosphocoenzyme A Kinase in Escherichia coli K-12

Pranab k. Mishra, Peter K. Park, and Dale G. Drueckhammer*

Department of Chemistry, State University at Stony Brook, Stony Brook, New York

Received 29 November 2000/Accepted 6 February 2001

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 from Corynebacterium 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. coli dephospho-CoA kinase were identified in a diverse range of organisms.

* Corresponding author. Mailing address: Department of Chemistry, State University at Stony Brook, Stony Brook, NY 11794-3400. Phone: (631) 632-7923. Fax: (631) 632-7960. E-mail: dale.drueckhammer{at}sunysb.edu.

Journal of Bacteriology, May 2001, p. 2774-2778, Vol. 183, No. 9
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.9.2774-2778.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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