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The 2.1 A structure of Aerococcus viridans L-lactate oxidase (LOX).

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.

SUBMITTER: Leiros I

PROVIDER: S-EPMC2225357 | biostudies-literature | 2006 Dec

REPOSITORIES: biostudies-literature

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The 2.1 A structure of Aerococcus viridans L-lactate oxidase (LOX).

Leiros Ingar I Wang Ellen E Rasmussen Tonni T Oksanen Esko E Repo Heidi H Petersen Steffen B SB Heikinheimo Pirkko P Hough Edward E

Acta crystallographica. Section F, Structural biology and crystallization communications 20061104 Pt 12

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 fou ...[more]

PMID: 17142893

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