1.1.3.2: L-lactate oxidase
This is an abbreviated version!
For detailed information about L-lactate oxidase, go to the full flat file.
Word Map on EC 1.1.3.2
Reaction
Synonyms
AvLOX, L-lactate oxidase, LctO, LOX
ECTree
1.1.3.2 L-lactate oxidaseAdvanced search results
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results (Crystallization
Crystallization on EC 1.1.3.2 - L-lactate oxidase
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CRYSTALLIZATION (Commentary) 
ORGANISM
UNIPROT
LITERATURE
1.9 A crystal structure, Y191F variant bound with FMN and pyruvate. Mutation has a strictly locally disruptive effect
in complex with pyruvate, to 1.9 A resolution. One pyruvate molecule binds to the active site and locates near the N5 position of FMN for subunits, A, B, and D in the asymmetric unit. The pyruvate molecule is stabilized by the interaction of its carboxylate group with the side-chain atoms of Tyr40, Arg181, His265, and Arg268, and of its keto-oxygen atom with the side-chain atoms of Tyr146, Tyr215, and His265
mutant A95G in complex with pyruvate, to 1.65 A resolution. Mutation leads to increased steric volume available in the active site
mutant Y215F in complex with pyruvate, to 2.6 A resolution. The hydrogen bond between the phenolic hydroxyl and the keto oxygen in pyruvate is replaced with a potentially stronger hydrophobic interaction between the phenylalanine and the methyl group of pyruvate. Residues 200 through 215 or 216 appear to be disordered
native enzyme and its complex with D-lactate at pH 4.5. In the complex structure, the D-lactate resides in the substrate-binding site, but acitve site His265 flips far away from the D-lactate, as compared with its conformation in the unbound state at pH 8.0. The flip of His265 triggers a large structural rearrangement. The reductive half-reaction mechanism may release pyruvate through hydride transfer. In the oxidative half-reaction, His265 flips back, pushing molecular oxygen into the substrate-binding site as the second substrate, and the reverse reaction takes place to produce hydrogen peroxide
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
to 2.1 A resolution. The LOX monomer structure has a typical alpha8/beta8 motif. Five residues around the FMN prosthetic group of LOX, act synergistically to discriminate between the L/D configurations of lactate. Space group I422 with unit-cell parameters a = b = 191.096 A , c = 194.497A and a = b = c = 90 with four monomers per asymmetric unit
to 3.0 A resolution, space group P212121 with unit cell parameters a = 118.4 A, b = 138.4 A, c = 104.6 A. The enzyme may exist as an octameric form with noncrystallographic two- and four-fold axes in the center of the octamer
