A1 Refereed original research article in a scientific journal
The 2.1 Å structure of Aerococcus viridans L-lactate oxidase (LOX)
Authors: Leiros I, Wang E, Rasmussen T, Oksanen E, Repo H, Petersen SB, Heikinheimo P, Hough E
Publisher: BLACKWELL PUBLISHING
Publication year: 2006
Journal:: Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Journal name in source: ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS
Journal acronym: ACTA CRYSTALLOGR F
Volume: 62
First page : 1185
Last page: 1190
Number of pages: 6
ISSN: 1744-3091
DOI: https://doi.org/10.1107/S1744309106044678
Abstract
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.
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.
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