- The 2.1 A structure of Aerococcus viridans L-lactate oxidase (LOX).
The 2.1 A structure of Aerococcus viridans L-lactate oxidase (LOX).
Acta crystallographica. Section F, Structural biology and crystallization communications (2006-12-05)
Ingar Leiros, Ellen Wang, Tonni Rasmussen, Esko Oksanen, Heidi Repo, Steffen B Petersen, Pirkko Heikinheimo, Edward Hough
PMID17142893
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.
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