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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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| Udgivet i: | Arch Biochem Biophys |
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| Main Authors: | , , , , , |
| Format: | Artigo |
| Sprog: | Inglês |
| Udgivet: |
2015
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| Fag: | |
| Online adgang: | 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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