COASY abstract: Difference between revisions
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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. | 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 08:34, 10 June 2007
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.
Abstract | Introduction | Results | Discussion |
Conclusion | Method | References
