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Can I read The 2.1 Å structure of Aerococcus viridansl-lactate oxidase (LOX) on EtoBox?
The 2.1 Å structure of Aerococcus viridansl-lactate oxidase (LOX) by Ingar Leiros; Ellen Wang; Tonni Rasmussen; Esko Oksanen; Heidi Repo; Steffen B. Petersen; Pirkko Heikinheimo; Edward Hough is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.
What is The 2.1 Å structure of Aerococcus viridansl-lactate oxidase (LOX) about?
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.
Who reads The 2.1 Å structure of Aerococcus viridansl-lactate oxidase (LOX)?
It is typically read by researchers, students, and practitioners in Biochemistry, Genetics and Molecular Biology.
- Author
- Ingar Leiros; Ellen Wang; Tonni Rasmussen; Esko Oksanen; Heidi Repo; Steffen B. Petersen; Pirkko Heikinheimo; Edward Hough
- Publisher
- John Wiley and Sons; International Union of Crystallography; John Wiley and Sons Ltd; International Union of Crystallography (IUCr) (ISSN 1744-3091)
- Published
- 2006
- Language
- EN
- Field
- Biochemistry, Genetics and Molecular Biology (Life Sciences)