Crystallographic study on the interaction of l-lactate oxidase with pyruvate at 1.9 Å resolution

Shu Jie Li, Yasufumi Umena, Kazuko Yorita, Takeshi Matsuoka, Akiko Kita, Kiyoshi Fukui, Yukio Morimoto

Research output: Contribution to journalArticle

17 Citations (Scopus)

Abstract

l-Lactate oxidase (LOX) from Aerococcus viridans catalyzes the oxidation of l-lactate to pyruvate by the molecular oxygen and belongs to a large family of 2-hydroxy acid-dependent flavoenzymes. To investigate the interaction of LOX with pyruvate in structural details and understand the chemical mechanism of flavin-dependent l-lactate dehydrogenation, the LOX-pyruvate complex was crystallized and the crystal structure of the complex has been solved at a resolution of 1.90 Å. One pyruvate molecule bound to the active site and located near N5 position of FMN for subunits, A, B, and D in the asymmetric unit, were identified. 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. The α-carbon of pyruvate is found to be 3.13 Å from the N5 atom of FMN at an angle of 105.4° from the flavin N5-N10 axis.

Original languageEnglish
Pages (from-to)1002-1007
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume358
Issue number4
DOIs
Publication statusPublished - Jul 13 2007
Externally publishedYes

Fingerprint

lactate 2-monooxygenase
Pyruvic Acid
Flavin Mononucleotide
Atoms
Lactic Acid
Aerococcus
Oxygen
Hydroxy Acids
Molecules
Molecular oxygen
Dehydrogenation
Catalytic Domain
Carbon
Crystal structure

Keywords

  • Crystal structure
  • Flavoenzyme
  • Interaction
  • Lactate oxidase
  • Pyruvate

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Crystallographic study on the interaction of l-lactate oxidase with pyruvate at 1.9 Å resolution. / Li, Shu Jie; Umena, Yasufumi; Yorita, Kazuko; Matsuoka, Takeshi; Kita, Akiko; Fukui, Kiyoshi; Morimoto, Yukio.

In: Biochemical and Biophysical Research Communications, Vol. 358, No. 4, 13.07.2007, p. 1002-1007.

Research output: Contribution to journalArticle

Li, Shu Jie ; Umena, Yasufumi ; Yorita, Kazuko ; Matsuoka, Takeshi ; Kita, Akiko ; Fukui, Kiyoshi ; Morimoto, Yukio. / Crystallographic study on the interaction of l-lactate oxidase with pyruvate at 1.9 Å resolution. In: Biochemical and Biophysical Research Communications. 2007 ; Vol. 358, No. 4. pp. 1002-1007.
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abstract = "l-Lactate oxidase (LOX) from Aerococcus viridans catalyzes the oxidation of l-lactate to pyruvate by the molecular oxygen and belongs to a large family of 2-hydroxy acid-dependent flavoenzymes. To investigate the interaction of LOX with pyruvate in structural details and understand the chemical mechanism of flavin-dependent l-lactate dehydrogenation, the LOX-pyruvate complex was crystallized and the crystal structure of the complex has been solved at a resolution of 1.90 {\AA}. One pyruvate molecule bound to the active site and located near N5 position of FMN for subunits, A, B, and D in the asymmetric unit, were identified. 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. The α-carbon of pyruvate is found to be 3.13 {\AA} from the N5 atom of FMN at an angle of 105.4° from the flavin N5-N10 axis.",
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AU - Li, Shu Jie

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AU - Matsuoka, Takeshi

AU - Kita, Akiko

AU - Fukui, Kiyoshi

AU - Morimoto, Yukio

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AB - l-Lactate oxidase (LOX) from Aerococcus viridans catalyzes the oxidation of l-lactate to pyruvate by the molecular oxygen and belongs to a large family of 2-hydroxy acid-dependent flavoenzymes. To investigate the interaction of LOX with pyruvate in structural details and understand the chemical mechanism of flavin-dependent l-lactate dehydrogenation, the LOX-pyruvate complex was crystallized and the crystal structure of the complex has been solved at a resolution of 1.90 Å. One pyruvate molecule bound to the active site and located near N5 position of FMN for subunits, A, B, and D in the asymmetric unit, were identified. 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. The α-carbon of pyruvate is found to be 3.13 Å from the N5 atom of FMN at an angle of 105.4° from the flavin N5-N10 axis.

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KW - Pyruvate

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