Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The crystal structure of L-lactate oxidase (LOX) from Aerococcus viridans has been determined at 2.1 A resolution. LOX catalyzes the flavin mononucleotide (FMN) dependent oxidation of lactate to pyruvate and hydrogen peroxide. LOX belongs to the alpha-hydroxy-acid oxidase flavoenzyme family; members of which bind similar substrates and to some extent have conserved catalytic properties and structural motifs. LOX crystallized as two tightly packed tetramers in the asymmetric unit, each having fourfold symmetry. The present structure shows a conserved FMN coordination, but also reveals novel residues involved in substrate binding compared with other family members.
The 2.1 A structure of Aerococcus viridans L-lactate oxidase (LOX).,Leiros I, Wang E, Rasmussen T, Oksanen E, Repo H, Petersen SB, Heikinheimo P, Hough E Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Dec 1;62(Pt, 12):1185-90. Epub 2006 Nov 4. PMID:17142893[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Leiros I, Wang E, Rasmussen T, Oksanen E, Repo H, Petersen SB, Heikinheimo P, Hough E. The 2.1 A structure of Aerococcus viridans L-lactate oxidase (LOX). Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Dec 1;62(Pt, 12):1185-90. Epub 2006 Nov 4. PMID:17142893 doi:10.1107/S1744309106044678
