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Contribution to catalysis of ornithine binding residues in ornithine N5-monooxygenase

The SidA ornithine N5-monooxygenase from A. fumigatus is a flavin monooxygenase that catalyzes the NADPH-dependent hydroxylation of ornithine. Herein we report a mutagenesis study targeting four residues that contact ornithine in crystal structures of SidA: Lys107, Asn293, Asn323, and Ser469. Mutati...

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Detalles Bibliográficos
Publicado en:Arch Biochem Biophys
Main Authors: Robinson, Reeder, Qureshi, Insaf A., Klancher, Catherine A., Rodriguez, Pedro J., Tanner, John J., Sobrado, Pablo
Formato: Artigo
Idioma:Inglês
Publicado: 2015
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Acceso en liña:https://ncbi.nlm.nih.gov/pmc/articles/PMC6467063/
https://ncbi.nlm.nih.gov/pubmed/26375201
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.abb.2015.09.008
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