The 2.1 Å structure ofAerococcus viridansL-lactate oxidase (LOX)
- 4 November 2006
- journal article
- Published by International Union of Crystallography (IUCr) in Acta Crystallographica Section F Structural Biology and Crystallization Communications
- Vol. 62 (12), 1185-1190
- https://doi.org/10.1107/s1744309106044678
Abstract
The crystal structure of L-lactate oxidase (LOX) from Aerococcus viridans has been determined at 2.1 A resolution. LOX catalyzes the flavin mononucleotide (FMN) dependent oxidation of lactate to pyruvate and hydrogen peroxide. LOX belongs to the alpha-hydroxy-acid oxidase flavoenzyme family; members of which bind similar substrates and to some extent have conserved catalytic properties and structural motifs. LOX crystallized as two tightly packed tetramers in the asymmetric unit, each having fourfold symmetry. The present structure shows a conserved FMN coordination, but also reveals novel residues involved in substrate binding compared with other family members.Keywords
This publication has 30 references indexed in Scilit:
- A novel continuous subcutaneous lactate monitoring system☆Biosensors and Bioelectronics, 2005
- Crystal Structure Analysis of Recombinant Rat Kidney Long Chain Hydroxy Acid Oxidase,Biochemistry, 2005
- Regulation of D‐amino acid oxidase expression in the yeast Rhodotorula gracilisYeast, 2003
- Geometry of metal–ligand interactions in proteinsActa Crystallographica Section D-Biological Crystallography, 2001
- The x-ray structure of d -amino acid oxidase at very high resolution identifies the chemical mechanism of flavin-dependent substrate dehydrogenationProceedings of the National Academy of Sciences, 2000
- Involvement of Tyr24 and Trp108 in substrate binding and substrate specificity of glycolate oxidase.1995
- Purification and properties of Aerococcusviridans lactate oxidaseBiochemical and Biophysical Research Communications, 1989
- The Active Site of Spinach Glycolate OxidaseJournal of Biological Chemistry, 1989
- Three-dimensional structure of flavocytochrome b2 from baker's yeast at 3.0-A resolution.Proceedings of the National Academy of Sciences, 1987
- A comparative carbon-13, nitrogen-15, and phosphorus-31 nuclear magnetic resonance study on the flavodoxins from Clostridium MP, Megasphaera elsdenii, and Azotobacter vinelandiiBiochemistry, 1986