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• W2056556323 startingPage "14635" @default.
• W2056556323 abstract "Coral allene oxide synthase (cAOS) catalyzes the formation of allene oxides from fatty acid hydroperoxides. Interestingly, its active site differs from that of catalase by only a single residue yet is incapable of catalase activity. That is, it is unable to catalyze the decomposition of hydrogen peroxide to molecular oxygen and water. However, the single active-site mutation T66V allows cAOS to exhibit catalase activity. We have performed a series of molecular dynamics (MD) simulations in order to gain insights into the differences in substrate (8R-hydroperoxyeicosatetraenoic) and H2O2 active site binding between wild-type cAOS and the T66V mutant cAOS. It is observed that in wild-type cAOS the active site Thr66 residue consistently forms a strong hydrogen-bonding interaction with H2O2 (catalase substrate) and, importantly, with the aid of His67 helps to pull H2O2 away from the heme Fe center. In contrast, in the T66V-cAOS mutant the H2O2 is much closer to the heme’s Fe center and now forms a consistent Fe···O2H2 interaction. In addition, the His67···H2O2 distance shortens considerably, increasing the likelihood of a Cpd I intermediate and hence exhibiting catalase activity." @default.
• W2056556323 created "2016-06-24" @default.
• W2056556323 creator A5001195523 @default.
• W2056556323 creator A5019227777 @default.
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• W2056556323 date "2013-11-14" @default.
• W2056556323 modified "2023-09-27" @default.
• W2056556323 title "A Molecular Dynamics Examination on Mutation-Induced Catalase Activity in Coral Allene Oxide Synthase" @default.
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• W2056556323 doi "https://doi.org/10.1021/jp408486n" @default.
• W2056556323 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/24164352" @default.
• W2056556323 hasPublicationYear "2013" @default.
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