1. Crystallographic study on the interaction of L-lactate oxidase with pyruvate at 1.9 Angstrom resolution.
- Author
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Li SJ, Umena Y, Yorita K, Matsuoka T, Kita A, Fukui K, and Morimoto Y
- Subjects
- Binding Sites, Computer Simulation, Enzyme Activation, Protein Binding, Protein Conformation, Sensitivity and Specificity, Crystallography methods, Mixed Function Oxygenases chemistry, Mixed Function Oxygenases ultrastructure, Models, Chemical, Models, Molecular, Pyruvic Acid chemistry
- Abstract
L-Lactate oxidase (LOX) from Aerococcus viridans catalyzes the oxidation of L-lactate to pyruvate by the molecular oxygen and belongs to a large family of 2-hydroxy acid-dependent flavoenzymes. To investigate the interaction of LOX with pyruvate in structural details and understand the chemical mechanism of flavin-dependent L-lactate dehydrogenation, the LOX-pyruvate complex was crystallized and the crystal structure of the complex has been solved at a resolution of 1.90 Angstrom. One pyruvate molecule bound to the active site and located near N5 position of FMN for subunits, A, B, and D in the asymmetric unit, were identified. The pyruvate molecule is stabilized by the interaction of its carboxylate group with the side-chain atoms of Tyr40, Arg181, His265, and Arg268, and of its keto-oxygen atom with the side-chain atoms of Tyr146, Tyr215, and His265. The alpha-carbon of pyruvate is found to be 3.13 Angstrom from the N5 atom of FMN at an angle of 105.4 degrees from the flavin N5-N10 axis.
- Published
- 2007
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