ArticleProtein science : a publication of the Protein Society2019
Flavin oxidation in flavin-dependent N-monooxygenases.
Article in Protein science : a publication of the Protein Society, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 13 citations in OpenAlex.
- Characterization of the N-Hydroxylating Monooxygenase TheA from Thermocrispum agreste Reveals a Broad Substrate Spectrum.Chembiochem : a European journal of chemical biology · 2025Article
- Functional analysis of R144 in the flavin oxidation mechanism of a flavin-dependent N-monooxygenase.Protein science : a publication of the Protein Society · 2025Article
- A biosynthetic aspartate N-hydroxylase performs successive oxidations by holding intermediates at a site away from the catalytic center.The Journal of biological chemistry · 2023Article
- Substrate Electronics Dominate the Rate of Reductive Dehalogenation Promoted by the Flavin-Dependent Iodotyrosine Deiodinase.Biochemistry · 2023Article
- Photoinduced Covalent Irreversible Inactivation of Proline Dehydrogenase by S-Heterocycles.ACS chemical biology · 2021Article
- Trapping conformational states of a flavin-dependentThe Journal of biological chemistry · 2020Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Siderophore A (SidA) from Aspergillus fumigatus is a flavin-containing monooxygenase that hydroxylates ornithine (Orn) at the amino group of the side chain. Lysine (Lys) also binds to the active site of SidA; however, hydroxylation is not efficient and H
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Registered trials
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