ArticleArchives of biochemistry and biophysics2015
Contribution to catalysis of ornithine binding residues in ornithine N5-monooxygenase.
Article in Archives of biochemistry and biophysics, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 16 citations in OpenAlex.
- Article
- Functional analysis of R144 in the flavin oxidation mechanism of a flavin-dependent N-monooxygenase.Protein science : a publication of the Protein Society · 2025Article
- Unifying and versatile features of flavin-dependent monooxygenases: Diverse catalysis by a common C4a-(hydro)peroxyflavin.The Journal of biological chemistry · 2023Review
- Characterization of a broadly specific cadaverine N-hydroxylase involved in desferrioxamine B biosynthesis in Streptomyces sviceus.PloS one · 2021Article
- Trapping conformational states of a flavin-dependentThe Journal of biological chemistry · 2020Article
- Flavin-dependent N-hydroxylating enzymes: distribution and application.Applied microbiology and biotechnology · 2020Review
- Molecular characterization of siderophore biosynthesis inIMA fungus · 2020Article
- Flavin oxidation in flavin-dependent N-monooxygenases.Protein science : a publication of the Protein Society · 2019Article
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
The SidA ornithine N5-monooxygenase from Aspergillus 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. Mutation of Lys107 to Ala abolishes activity as measured in steady-state oxygen consumption and ornithine hydroxylation assays, indicating that the ionic interaction of Lys107 with the carboxylate of ornithine is essential for catalysis. Mutation of Asn293, Asn323, or Ser469 individually to Ala results in >14-fold increases in Km values for ornithine. Asn323 to Ala also increases the rate constant for flavin reduction by NADPH by 18-fold. Asn323 is unique among the four ornithine binding residues in that it also interacts with NADPH by forming a hydrogen bond with the nicotinamide ribose. The crystal structure of N323A complexed with NADP(+) and ornithine shows that the nicontinamide riboside group of NADP is disordered. This result suggests that the increase in flavin reduction rate results from an increase in conformational space available to the enzyme-bound NADP(H). Asn323 thus facilitates ornithine binding at the expense of hindering flavin reduction, which demonstrates the delicate balance that exists within protein-ligand interaction networks in enzyme active sites.
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