The 2.1 A structure of Aerococcus viridans L-lactate oxidase (LOX).
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.
Leiros
Ingar
I
NorStruct, University of Tromsø, N-9037 Tromsø, Norway.
Wang
Ellen
E
Rasmussen
Tonni
T
Oksanen
Esko
E
Repo
Heidi
H
Petersen
Steffen B
SB
Heikinheimo
Pirkko
P
Hough
Edward
E
D000595:Amino Acid Sequence; D001665:Binding Sites; D003460:Crystallization; D018360:Crystallography, X-Ray; D005486:Flavin Mononucleotide / Q000737:chemistry; D006899:Mixed Function Oxygenases / Q000737:chemistry*; D008969:Molecular Sequence Data; D020836:Protein Structure, Quaternary; D016415:Sequence Alignment; D013289:Streptococcaceae / Q000201:enzymology*
D005486:Flavin Mononucleotide; D006899:Mixed Function Oxygenases; C021497:lactate 2-monooxygenase