@article{10902/18120,
year = {2018},
month = {8},
url = {http://hdl.handle.net/10902/18120},
abstract = {Omega-3 polyunsaturated fatty acids (PUFA) are produced in some unicellular organisms, such as marine gammaproteobacteria, myxobacteria, and thraustochytrids, by large enzyme complexes called PUFA synthases. These enzymatic complexes resemble bacterial antibiotic-producing proteins known as polyketide synthases (PKS). One of the PUFA synthase subunits is a conserved large protein (PfaA in marine proteobacteria) that contains three to nine tandem acyl carrier protein (ACP) domains as well as condensation and modification domains. In this work, a study of the PfaA architecture and its ability to initiate the synthesis by selecting malonyl units has been carried out. As a result, we have observed a self-acylation ability in tandem ACPs whose biochemical mechanism differ from the previously described for type II PKS. The acyltransferase domain of PfaA showed a high selectivity for malonyl-CoA that efficiently loads onto the ACPs domains. These results, together with the structural organization predicted for PfaA, suggest that this protein plays a key role at early stages of the anaerobic pathway of PUFA synthesis.},
publisher = {American Society for Biochemistry and Molecular Biology Inc.},
publisher = {J Biol Chem 2018, 293 (32), 12491-12501},
title = {Loading of malonyl-CoA Onto Tandem Acyl Carrier Protein Domains of Polyunsaturated Fatty Acid Synthases},
author = {Santín, Omar and Moncalián Montes, Gabriel},
}