| Literature DB >> 17142893 |
Ingar Leiros1, Ellen Wang, Tonni Rasmussen, Esko Oksanen, Heidi Repo, Steffen B Petersen, Pirkko Heikinheimo, Edward Hough.
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.Entities:
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Year: 2006 PMID： 17142893 PMCID： PMC2225357 DOI： 10.1107/S1744309106044678
Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN： 1744-3091