COASY conclusion: Difference between revisions
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Bifunctional Coenzyme A Synthase is integral to the CoA synthesis pathway and it's two domains, that of Dephospho-CoA Kinase (DPCK) and pantetheine-phosphate adenylyltransferase (PPAT), are necessary to complete the last two phases of this process. Structural analysis of sequence and structure conservation combined with electrostatic surface potential measurements, motif pattern searches and Multiple Sequence Alignments have provided evidence for the location of the ATP binding P-Loop on the DPCK domain. This site is fucntioanly significant as it forms one of the initial activating sites for the last stage of the CoA pathway. | Bifunctional Coenzyme A Synthase is integral to the CoA synthesis pathway and it's two domains, that of Dephospho-CoA Kinase (DPCK) and pantetheine-phosphate adenylyltransferase (PPAT), are necessary to complete the last two phases of this process. Structural analysis of sequence and structure conservation combined with electrostatic surface potential measurements, motif pattern searches and Multiple Sequence Alignments have provided evidence for the location of the ATP binding P-Loop on the DPCK domain. This site is fucntioanly significant as it forms one of the initial activating sites for the last stage of the CoA pathway. | ||
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The binding site for ACO was also identified on the DPCK domain. Whilst not directly related to the CoA pathway, ACO has a similar structure to Dephospho-CoA, which is created by the PPAT domain as the second last step of the CoA synthesis pathway, and the product which feeds into the DPCK domain to produce CoA. The finding of a binding cleft that may link the two domains provides support for the theory of a tunneling effect of passing produced Dephospho-CoA immediately to the DPCK domain for processing, negating the need to build up stores of Dephospho-CoA around the CoAsy expressed locations. | The binding site for ACO was also identified on the DPCK domain. Whilst not directly related to the CoA pathway, ACO has a similar structure to Dephospho-CoA, which is created by the PPAT domain as the second last step of the CoA synthesis pathway, and the product which feeds into the DPCK domain to produce CoA. The finding of a binding cleft that may link the two domains provides support for the theory of a tunneling effect of passing produced Dephospho-CoA immediately to the DPCK domain for processing, negating the need to build up stores of Dephospho-CoA around the CoAsy expressed locations. | ||
Revision as of 02:47, 10 June 2007
Bifunctional Coenzyme A Synthase is integral to the CoA synthesis pathway and it's two domains, that of Dephospho-CoA Kinase (DPCK) and pantetheine-phosphate adenylyltransferase (PPAT), are necessary to complete the last two phases of this process. Structural analysis of sequence and structure conservation combined with electrostatic surface potential measurements, motif pattern searches and Multiple Sequence Alignments have provided evidence for the location of the ATP binding P-Loop on the DPCK domain. This site is fucntioanly significant as it forms one of the initial activating sites for the last stage of the CoA pathway.
The binding site for ACO was also identified on the DPCK domain. Whilst not directly related to the CoA pathway, ACO has a similar structure to Dephospho-CoA, which is created by the PPAT domain as the second last step of the CoA synthesis pathway, and the product which feeds into the DPCK domain to produce CoA. The finding of a binding cleft that may link the two domains provides support for the theory of a tunneling effect of passing produced Dephospho-CoA immediately to the DPCK domain for processing, negating the need to build up stores of Dephospho-CoA around the CoAsy expressed locations.
Abstract | Introduction | Results | Discussion | Conclusion | Method | References
