The reductase domain in a Type I fatty acid synthase from the apicomplexan <Emphasis Type="Italic">Cryptosporidium parvum</Emphasis>: Restricted substrate preference towards very long chain fatty acyl thioesters |
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Authors: | Guan Zhu Xiangyu Shi Xiaomin Cai |
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Institution: | (1) Department of Veterinary Pathobiology, College of Veterinary Medicine & Biomedical Sciences, Texas A&M University, College Station, Texas 77843-4467, USA;(2) Faculty of Genetics Program, Texas A&M University, College Station, Texas 77843-4467, USA |
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Abstract: | Background The apicomplexan Cryptosporidium parvum genome possesses a 25-kb intronless open reading frame (ORF) that predicts a multifunctional Type I fatty acid synthase (CpFAS1)
with at least 21 enzymatic domains. Although the architecture of CpFAS1 resembles those of bacterial polyketide synthases
(PKSs), this megasynthase is predicted to function as a fatty acyl elongase as our earlier studies have indicated that the
N-terminal loading unit (acyl-ACP] ligase) prefers using intermediate to long chain fatty acids as substrates, and each of
the three internal elongation modules contains a complete set of enzymes to produce a saturated fatty acyl chain. Although
the activities of almost all domains were confirmed using recombinant proteins, that of the C-terminal reductase domain (CpFAS1-R)
was yet undetermined. In fact, there were no published studies to report the kinetic features of any reductase domains in
bacterial PKSs using purified recombinant or native proteins. |
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