Literature DB >> 16511063

Crystallization and preliminary X-ray diffraction study of L-lactate oxidase (LOX), R181M mutant, from Aerococcus viridans.

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:  

Mesh:

Substances:

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


  14 in total

1.  Structure of an active soluble mutant of the membrane-associated (S)-mandelate dehydrogenase.

Authors:  N Sukumar; Y Xu; D L Gatti; B Mitra; F S Mathews
Journal:  Biochemistry       Date:  2001-08-21       Impact factor: 3.162

2.  Matthews coefficient probabilities: Improved estimates for unit cell contents of proteins, DNA, and protein-nucleic acid complex crystals.

Authors:  Katherine A Kantardjieff; Bernhard Rupp
Journal:  Protein Sci       Date:  2003-09       Impact factor: 6.725

3.  Refined structure of spinach glycolate oxidase at 2 A resolution.

Authors:  Y Lindqvist
Journal:  J Mol Biol       Date:  1989-09-05       Impact factor: 5.469

4.  The active site of spinach glycolate oxidase.

Authors:  Y Lindqvist; C I Brändén
Journal:  J Biol Chem       Date:  1989-02-25       Impact factor: 5.157

5.  Purification and properties of Aerococcus viridans lactate oxidase.

Authors:  J D Duncan; J O Wallis; M R Azari
Journal:  Biochem Biophys Res Commun       Date:  1989-10-31       Impact factor: 3.575

6.  Processing of X-ray diffraction data collected in oscillation mode.

Authors:  Z Otwinowski; W Minor
Journal:  Methods Enzymol       Date:  1997       Impact factor: 1.600

7.  Solvent content of protein crystals.

Authors:  B W Matthews
Journal:  J Mol Biol       Date:  1968-04-28       Impact factor: 5.469

8.  Interaction of two arginine residues in lactate oxidase with the enzyme flavin: conversion of FMN to 8-formyl-FMN.

Authors:  K Yorita; T Matsuoka; H Misaki; V Massey
Journal:  Proc Natl Acad Sci U S A       Date:  2000-11-21       Impact factor: 11.205

9.  Amino acid sequence of long chain alpha-hydroxy acid oxidase from rat kidney, a member of the family of FMN-dependent alpha-hydroxy acid-oxidizing enzymes.

Authors:  K H Diêp Lê; F Lederer
Journal:  J Biol Chem       Date:  1991-11-05       Impact factor: 5.157

10.  Molecular structure of flavocytochrome b2 at 2.4 A resolution.

Authors:  Z X Xia; F S Mathews
Journal:  J Mol Biol       Date:  1990-04-20       Impact factor: 5.469

View more
  2 in total

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

Authors:  Ingar Leiros; Ellen Wang; Tonni Rasmussen; Esko Oksanen; Heidi Repo; Steffen B Petersen; Pirkko Heikinheimo; Edward Hough
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2006-11-04

2.  Host-directed evolution of a novel lactate oxidase in Streptococcus iniae isolates from barramundi (Lates calcarifer).

Authors:  Roslina A Nawawi; Justice C F Baiano; E Charlotte E Kvennefors; Andrew C Barnes
Journal:  Appl Environ Microbiol       Date:  2009-03-06       Impact factor: 4.792

  2 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.