Crystallographic study on the interaction of L-lactate oxidase with pyruvate at 1.9 A resolution
- Institute for Protein Research, Osaka University, Suita, Osaka 565-0871 (Japan)
- Institute for Enzyme Research, University of Tokushima, Tokushima 770-8503 (Japan)
- Diagnostics Division, Asahi Kasei Pharma, Shizuoka 410-2321 (Japan)
- Research Reactor Institute, Kyoto University, Kumatori-cho, Sennan-gun, Osaka 590-0494 (Japan)
- Research Reactor Institute, Kyoto University, Kumatori-cho, Sennan-gun, Osaka 590-0494 (Japan) and RIKEN, Harima Institute at SPring-8, Kohto, Mikazuki, Hyogo 679-5148 (Japan)
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 A. 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 A from the N5 atom of FMN at an angle of 105.4{sup o} from the flavin N5-N10 axis.
- OSTI ID:
- 20991434
- Journal Information:
- Biochemical and Biophysical Research Communications, Vol. 358, Issue 4; Other Information: DOI: 10.1016/j.bbrc.2007.05.021; PII: S0006-291X(07)00958-8; Copyright (c) 2007 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
- Country of Publication:
- United States
- Language:
- English
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