ArticleScientific reports2016
Conformational flexibility related to enzyme activity: evidence for a dynamic active-site gatekeeper function of Tyr(215) in Aerococcus viridans lactate oxidase.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Creating highly active fluoroacetate dehalogenases via gate-based synergetic chain design.Nature communications · 2026Article
- More Than One Enzyme: Exploring Alternative FMN-Dependent L-Lactate Oxidases for Biosensor Development.ACS omega · 2024Article
- Further evidence in favour of a carbanion mechanism for glycolate oxidase.FEBS open bio · 2023Article
- Activation of L-lactate oxidase by the formation of enzyme assemblies through liquid-liquid phase separation.Scientific reports · 2023Article
- Enzymes Encapsulated within Alginate Hydrogels: Bioelectrocatalysis and Electrochemiluminescence Applications.Analytical chemistry · 2022Article
- Flavin Mononucleotide-Dependent l-Lactate Dehydrogenases: Expanding the Toolbox of Enzymes for l-Lactate Biosensors.ACS omega · 2022Article
- Structure of lactate oxidase from Enterococcus hirae revealed new aspects of active site loop function: Product-inhibition mechanism and oxygen gatekeeper.Protein science : a publication of the Protein Society · 2022Article
- TiOACS applied materials & interfaces · 2021Article
- Article
- FMN-dependent oligomerization of putative lactate oxidase from Pediococcus acidilactici.PloS one · 2020Article
- Structure and role for active site lid of lactate monooxygenase from Mycobacterium smegmatis.Protein science : a publication of the Protein Society · 2019Article
- Roles of Active-Site Aromatic Residues in Cold Adaptation ofACS omega · 2017Article
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4 authors.
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Abstract
L-Lactate oxidase (LOX) belongs to a large family of flavoenzymes that catalyze oxidation of α-hydroxy acids. How in these enzymes the protein structure controls reactivity presents an important but elusive problem. LOX contains a prominent tyrosine in the substrate binding pocket (Tyr(215) in Aerococcus viridans LOX) that is partially responsible for securing a flexible loop which sequesters the active site. To characterize the role of Tyr(215), effects of substitutions of the tyrosine (Y215F, Y215H) were analyzed kinetically, crystallographically and by molecular dynamics simulations. Enzyme variants showed slowed flavin reduction and oxidation by up to 33-fold. Pyruvate release was also decelerated and in Y215F, it was the slowest step overall. A 2.6-Å crystal structure of Y215F in complex with pyruvate shows the hydrogen bond between the phenolic hydroxyl and the keto oxygen in pyruvate is replaced with a potentially stronger hydrophobic interaction between the phenylalanine and the methyl group of pyruvate. Residues 200 through 215 or 216 appear to be disordered in two of the eight monomers in the asymmetric unit suggesting that they function as a lid controlling substrate entry and product exit from the active site. Substitutions of Tyr(215) can thus lead to a kinetic bottleneck in product release.
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