A1 Vertaisarvioitu alkuperäisartikkeli tieteellisessä lehdessä
The 2.1 Å structure of Aerococcus viridans L-lactate oxidase (LOX)
Tekijät: Leiros I, Wang E, Rasmussen T, Oksanen E, Repo H, Petersen SB, Heikinheimo P, Hough E
Kustantaja: BLACKWELL PUBLISHING
Julkaisuvuosi: 2006
Lehti:: Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Tietokannassa oleva lehden nimi: ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS
Lehden akronyymi: ACTA CRYSTALLOGR F
Vuosikerta: 62
Aloitussivu: 1185
Lopetussivu: 1190
Sivujen määrä: 6
ISSN: 1744-3091
DOI: https://doi.org/10.1107/S1744309106044678
Tiivistelmä
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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