Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.1.3.2 extracted from

  • Leiros, I.; Wang, E.; Rasmussen, T.; Oksanen, E.; Repo, H.; Petersen, S.B.; Heikinheimo, P.; Hough, E.
    The 2.1 A structure of Aerococcus viridans L-lactate oxidase (LOX) (2006), Acta Crystallogr. Sect. F, 62, 1185-1190 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
to 2.1 A resolution. LOX crystallizes as two tightly packed tetramers in the asymmetric unit, each having fourfold symmetry. Residues Tyr40, Arg268, His265, Tyr146 and Asp174 are involved in substrate binding Aerococcus viridans

Organism

Organism UniProt Comment Textmining
Aerococcus viridans Q44467
-
-

Synonyms

Synonyms Comment Organism
LOX
-
Aerococcus viridans

Cofactor

Cofactor Comment Organism Structure
FMN FMN is positioned deep down in the funnel-shaped substrate-binding site, behind (or underneath) the substrate when it is bound. Residues Tyr40, Pro93, Gln144, Tyr146, Thr172, Lys241, Asp296, Arg300 and Arg320 are involved in binding Aerococcus viridans