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



: Leiros I, Wang E, Rasmussen T, Oksanen E, Repo H, Petersen SB, Heikinheimo P, Hough E

Publisher: BLACKWELL PUBLISHING

: 2006

Acta Crystallographica Section F: Structural Biology and Crystallization Communications

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS

: ACTA CRYSTALLOGR F

: 62

: 1185

: 1190

: 6

: 1744-3091

DOI: https://doi.org/10.1107/S1744309106044678


The crystal structure of L-lactate oxidase (LOX) from Aerococcus viridans has been determined at 2.1 angstrom 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.



Last updated on 2025-14-10 at 09:56