L-lactate oxidase from Aerococcus viridans crystallized as an octamer. Preliminary X-ray studies.
Crystals of flavoenzyme L-lactate oxidase from Aerococcus viridans (LOX) have been obtained that diffract to 3.0 A resolution (P2(1)2(1)2(1), a = 118.4 A, b = 138.4 A, c = 194.6 A). Crystallographic studies suggest that the enzyme may exist as an octameric form with non-crystallographic two- and four-fold axes in the center of the octamer. The four-fold axis makes the tetramer tight, and the tetramers lie upon one another by the two-fold axis.
Faculty of Engineering, University of Tokushima.
Y
Y
Morimoto
K
K
Yorita
K
K
Aki
H
H
Misaki
V
V
Massey
D002850:Chromatography, Gel; D003460:Crystallization; D018360:Crystallography, X-Ray; D046911:Macromolecular Substances; D006899:Mixed Function Oxygenases / Q000737:chemistry* / Q000302:isolation & purification; D013289:Streptococcaceae / Q000201:enzymology*; D014462:Ultrafiltration
D046911:Macromolecular Substances; D006899:Mixed Function Oxygenases; C021497:lactate 2-monooxygenase