ArticleFEBS letters2014
Steady-state kinetic mechanism of LodA, a novel cysteine tryptophylquinone-dependent oxidase.
Article in FEBS letters, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 12 citations in OpenAlex.
- Structural Determinants of the Specific Activities of an L-Amino Acid Oxidase fromMolecules (Basel, Switzerland) · 2022Article
- Characterization of PlGoxB, a flavoprotein required for cysteine tryptophylquinone biosynthesis in glycine oxidase from Pseudoalteromonas luteoviolacea.Archives of biochemistry and biophysics · 2019Article
- Structural and Spectroscopic Characterization of a Product Schiff Base Intermediate in the Reaction of the Quinoprotein Glycine Oxidase, GoxA.Biochemistry · 2019Article
- Diversity of structures, catalytic mechanisms and processes of cofactor biosynthesis of tryptophylquinone-bearing enzymes.Archives of biochemistry and biophysics · 2018Review
- Protein-Derived Cofactors Revisited: Empowering Amino Acid Residues with New Functions.Biochemistry · 2018Review
- Kinetic characteristics of L-lysineBiochemistry and biophysics reports · 2017Article
- Roles of Copper and a Conserved Aspartic Acid in the Autocatalytic Hydroxylation of a Specific Tryptophan Residue during Cysteine Tryptophylquinone Biogenesis.Biochemistry · 2017Article
- Roles of Conserved Residues of the Glycine Oxidase GoxA in Controlling Activity, Cooperativity, Subunit Composition, and Cysteine Tryptophylquinone Biosynthesis.The Journal of biological chemistry · 2016Article
- Roles of active site residues in LodA, a cysteine tryptophylquinone dependent ε-lysine oxidase.Archives of biochemistry and biophysics · 2015Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
LodA is a novel lysine-ε-oxidase which possesses a cysteine tryptophylquinone cofactor. It is the first tryptophylquinone enzyme known to function as an oxidase. A steady-state kinetic analysis shows that LodA obeys a ping-pong kinetic mechanism with values of kcat of 0.22±0.04 s(-1), Klysine of 3.2±0.5 μM and KO2 of 37.2±6.1 μM. The kcat exhibited a pH optimum at 7.5 while kcat/Klysine peaked at 7.0 and remained constant to pH 8.5. Alternative electron acceptors could not effectively substitute for O2 in the reaction. A mechanism for the reductive half reaction of LodA is proposed that is consistent with the ping-pong kinetics.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.