| Literature DB >> 16511063 |
Yasufumi Umena1, Kazuko Yorita, Takeshi Matsuoka, Makoto Abe, Akiko Kita, Kiyoshi Fukui, Tomitake Tsukihara, Yukio Morimoto.
Abstract
L-Lactate oxidase (LOX) from Aerococcus viridans is a member of the alpha-hydroxyacid oxidase flavoenzyme family. An X-ray crystallographic study of a LOX mutant in which Arg181 is replaced by Met was initiated in order to understand the functions of the conserved amino-acid residues around the FMN in the enzyme active site. LOX-R181M crystals belong to the tetragonal space group I422, with unit-cell parameters a = b = 192.632, c = 200.263 A, alpha = beta = gamma = 90 degrees. There are four monomers in the asymmetric unit. Diffraction data were collected under cryogenic conditions to 2.44 A resolution from LOX-R181M crystals at BL41XU, SPring-8.Entities:
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Year: 2005 PMID: 16511063 PMCID: PMC1952436 DOI: 10.1107/S1744309105009152
Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN: 1744-3091