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

Published

Journal Article

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.

Full Text

Duke Authors

Cited Authors

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

Published Date

  • December 1, 2006

Published In

Volume / Issue

  • 62 / Pt 12

Start / End Page

  • 1185 - 1190

PubMed ID

  • 17142893

Pubmed Central ID

  • 17142893

Electronic International Standard Serial Number (EISSN)

  • 1744-3091

Digital Object Identifier (DOI)

  • 10.1107/S1744309106044678

Language

  • eng

Conference Location

  • England