Literature summary for 1.1.3.2 extracted from

Furuichi, M.; Suzuki, N.; Dhakshnamoorhty, B.; Minagawa, H.; Yamagishi, R.; Watanabe, Y.; Goto, Y.; Kaneko, H.; Yoshida, Y.; Yagi, H.; Waga, I.; Kumar, P.K.; Mizuno, H.
X-ray structures of Aerococcus viridans lactate oxidase and its complex with D-lactate at pH 4.5 show an alpha-hydroxyacid oxidation mechanism (2008), J. Mol. Biol., 378, 436-446 .

Crystallization (Commentary)

Crystallization (Comment)	Organism
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	Aerococcus viridans

Crystallization (Comment)

Organism

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

Aerococcus viridans

Organism

Organism	UniProt	Comment	Textmining
Aerococcus viridans	Q44467	-	-

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Release 2023.1 (January 2023)