L-LACTATE OXIDASE FROM AEROCOCCUS-VIRIDANS CRYSTALLIZED AS AN OCTAMER- PRELIMINARY-X-RAY STUDIES

Citation
Y. Morimoto et al., L-LACTATE OXIDASE FROM AEROCOCCUS-VIRIDANS CRYSTALLIZED AS AN OCTAMER- PRELIMINARY-X-RAY STUDIES, Biochimie, 80(4), 1998, pp. 309-312
Citations number
16
Categorie Soggetti
Biology
Journal title
ISSN journal
03009084
Volume
80
Issue
4
Year of publication
1998
Pages
309 - 312
Database
ISI
SICI code
0300-9084(1998)80:4<309:LOFACA>2.0.ZU;2-G
Abstract
Crystals of flavoenzyme L-lactate oxidase from Aerococcus viridans (LO X) have been obtained that diffract to 3.0 Angstrom resolution (P2(1)2 (1)2(1), a = 118.4 Angstrom, b = 138.4 Angstrom, c = 194.6 Angstrom). Crystallographic studies suggest that the enzyme may exist as an octam eric form with non-crystallographic two-and four-fold axes in the cent er of the octamer. The four-fold axis makes the tetramer tight, and th e tetramers lie upon one another by the two-fold axis. (C) Societe fra ncaise de biochimie et biologie moleculaire/Elsevier, Paris.