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.




[[COASY abstract | Abstract]] | [[COASY intro| Introduction]] | [[COASY results| Results]] | [[COASY discussion| Discussion]] |
[[DAP abstract | Abstract]] | [[DAP intro| Introduction]] | [[DAP results| Results]] | [[DAP discussion| Discussion]] |
[[COASY conclusion| Conclusion]] | [[COASY method| Method]] | [[COASY references| References]]
[[DAP conclusion| Conclusion]] | [[DAP method| Method]] | [[DAP references| References]]




[[Bifunctional coenzyme A synthase (CoA synthase)| Back To Main CoA Synthase Page]]
[[Aspartyl Aminopeptidase (DAP)| Back To Main Aspartyl Aminopeptidase Page]]

Revision as of 07:33, 3 June 2008