Literature summary for 1.1.3.2 extracted from

Li, S.J.; Umena, Y.; Yorita, K.; Matsuoka, T.; Kita, A.; Fukui, K.; Morimoto, Y.
Crystallographic study on the interaction of L-lactate oxidase with pyruvate at 1.9 Angstrom resolution (2007), Biochem. Biophys. Res. Commun., 358, 1002-1007 .

Crystallization (Commentary)

Crystallization (Comment)	Organism
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	Aerococcus viridans

Crystallization (Comment)

Organism

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

Aerococcus viridans

Organism

Organism	UniProt	Comment	Textmining
Aerococcus viridans	Q44467	-	-

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Release 2023.1 (January 2023)