TY - JOUR
T1 - Crystallographic study on the interaction of l-lactate oxidase with pyruvate at 1.9 Å resolution
AU - Li, Shu Jie
AU - Umena, Yasufumi
AU - Yorita, Kazuko
AU - Matsuoka, Takeshi
AU - Kita, Akiko
AU - Fukui, Kiyoshi
AU - Morimoto, Yukio
PY - 2007/7/13
Y1 - 2007/7/13
N2 - 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.
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.
KW - Crystal structure
KW - Flavoenzyme
KW - Interaction
KW - Lactate oxidase
KW - Pyruvate
UR - http://www.scopus.com/inward/record.url?scp=34249745601&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=34249745601&partnerID=8YFLogxK
U2 - 10.1016/j.bbrc.2007.05.021
DO - 10.1016/j.bbrc.2007.05.021
M3 - Article
C2 - 17517371
AN - SCOPUS:34249745601
SN - 0006-291X
VL - 358
SP - 1002
EP - 1007
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 4
ER -