COASY abstract: Difference between revisions

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Eukaryotic bifunctional Coenzyme A Synthase (CoAsy) plays an integral role in Coenzyme A (CoA) synthesis. CoAsy catalyses the final two steps of the CoA synthesis pathway, and therefore has two catalytic domains, PPAT and DPCK. The structure of part of mouse CoAsy (chain A) has recently been determined. Based on this structure, and using structural, functional and evolutionary analysis, we have further characterised CoAsy. It was found that chain A contained the DPCK, but not the PPAT domain of CoAsy. The DPCK domain was found to have structural, sequence and functional conservation, and putative ligand binding sites (for ATP and dephospho-CoA) were identified. However, further experimental approaches are needed to confirm these sites, and to obtain more information about the PPAT domain of CoAsy.  
Eukaryotic bifunctional CoAsy is an integral part of the production of CoA. CoAsy catalyses the final two steps of this pathway, and as such has two catalytic domains, PPAT and DPCK. Through structural, functional and evolutionary analysis, CoAsy has been further characterised. It was found that the DPCK domain contained an ATP and an ACO binding site. Further, the DPCK domain has structural, sequence and functional conservation, particularly in the binding sites. However, further experimental approaches need to be completed before definite catalytic binding sites and ligand binding residues are fully determined.




Revision as of 22:35, 10 June 2007

Eukaryotic bifunctional Coenzyme A Synthase (CoAsy) plays an integral role in Coenzyme A (CoA) synthesis. CoAsy catalyses the final two steps of the CoA synthesis pathway, and therefore has two catalytic domains, PPAT and DPCK. The structure of part of mouse CoAsy (chain A) has recently been determined. Based on this structure, and using structural, functional and evolutionary analysis, we have further characterised CoAsy. It was found that chain A contained the DPCK, but not the PPAT domain of CoAsy. The DPCK domain was found to have structural, sequence and functional conservation, and putative ligand binding sites (for ATP and dephospho-CoA) were identified. However, further experimental approaches are needed to confirm these sites, and to obtain more information about the PPAT domain of CoAsy.


Abstract | Introduction | Results | Discussion | Conclusion | Method | References


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