Misra, A and Surolia, N and Surolia, A (2007) Unveiling the unusual acylation behavior of type II fatty acid biosynthesis acyl carrier proteins. In: FEBS Journal, 274 (s1). 221 -244.
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Acyl carrier protein (ACP) plays a central role in most metabolic processes inside the cell and almost 4% of the total enzymes inside the cell require it as a cofactor. Self-acylation of ACPs involved in polyketide biosynthesis pathways and absence of such an autocatalytic process for ACPs involved in fatty acid biosynthesis has been noted. Here, we demonstrate self-acylation property in ACPs from P. falciparum and B. napus that are essential components of type II fatty acid biosynthesis (FAS), disapproving the existing notion that this phenomenon is restricted only to ACPs involved in polyketide biosynthesis. We also provide strong evidences to suggest that catalytic self-acylation is intrinsic to the individual acyl carrier protein. Mutational analysis of P. falciparum and B. napus acyl carrier proteins revealed the key residue(s) involved in this phenomenon. We also demonstrate that these ACPs involved in fatty acid synthesis exhibit a high degree of selectivity for self-acylation employing only dicarboxylic acids as substrates. A plausible mechanism for the self-acylation reaction is also proposed. Furthermore, we have also demonstrated that some type II FAS ACPs exhibit acyl-transferase behavior and self-acylation and acyl-transferase behavior are totally uncoupled.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to Federation of European Biochemical Societies.|
|Department/Centre:||Division of Biological Sciences > Molecular Biophysics Unit|
|Date Deposited:||26 Aug 2008|
|Last Modified:||19 Sep 2010 04:49|
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