COASY conclusion
Bifunctional Coenzyme A Synthase is integral to the CoA synthesis pathway (Zhyvoloup et. al., 2002), and its two domains that of Dephospho-CoA Kinase (DPCK) and pantetheine-phosphate adenylyltransferase (PPAT), are necessary to complete the last two phases of this process (Figure 1). Structural analysis of sequence (Figure 10) and structure conservation (Figure 11) combined with electrostatic surface potential measurements(Figure 6), motif pattern searches (Table 1) and Multiple Sequence Alignments (Need figure from Rachael)have provided evidence for the location of the ATP binding P-Loop on the DPCK domain. This site is functionally significant as it forms one of the initial activating sites for the last stage of the CoA pathway (Zhyvoloup et. al., 2002).
The binding site for ACO was also identified on the DPCK domain (EMBL EBI, 2005). Whilst not directly related to the CoA pathway, ACO has a similar structure to Dephospho-CoA (Figure 14), 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 (Figure 1). The finding of a binding cleft(Figure 13) that may link the two domains provides support for the theory of a tunneling effect (Daugherty et. al., 2002) of passing produced Dephospho-CoA immediately to the DPCK domain for processing, negating the need to build up stores of Dephospho-CoA around CoAsy expressed locations (Figure 3).
Abstract | Introduction | Results | Discussion | Conclusion | Method | References
