Literature summary for 1.2.3.3 extracted from

Juan, E.C.; Hoque, M.M.; Hossain, M.T.; Yamamoto, T.; Imamura, S.; Suzuki, K.; Sekiguchi, T.; Takenaka, A.
The structures of pyruvate oxidase from Aerococcus viridans with cofactors and with a reaction intermediate reveal the flexibility of the active-site tunnel for catalysis (2007), Acta Crystallogr. Sect. F, 63, 900-907.

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli DH1	Aerococcus viridans

Crystallization (Commentary)

Crystallization (Comment)	Organism
by the hanging-drop vapour-diffusion method. POX complexed with FAD, with FAD and thiamine diphosphate, and with FAD and the 2-acetyl-thiamine diphosphate intermediate at 1.6, 1.8 and 1.9 A resolution, respectively. Each subunit of the homotetrameric POX enzyme consists of three domains. FAD is bound within one subunit in the elongated conformation and with the flavin moiety being planar in the oxidized form, while thiamine diphosphate is bound in a conserved V-conformation at the subunit-subunit interface. The structures reveal flexible regions in the active-site tunnel which may undergo conformational changes to allow the entrance of the substrates and the exit of the reaction products. Lys478, the side chain of which may be bent or extended depending on the stage of catalysis	Aerococcus viridans

Crystallization (Comment)

Organism

by the hanging-drop vapour-diffusion method. POX complexed with FAD, with FAD and thiamine diphosphate, and with FAD and the 2-acetyl-thiamine diphosphate intermediate at 1.6, 1.8 and 1.9 A resolution, respectively. Each subunit of the homotetrameric POX enzyme consists of three domains. FAD is bound within one subunit in the elongated conformation and with the flavin moiety being planar in the oxidized form, while thiamine diphosphate is bound in a conserved V-conformation at the subunit-subunit interface. The structures reveal flexible regions in the active-site tunnel which may undergo conformational changes to allow the entrance of the substrates and the exit of the reaction products. Lys478, the side chain of which may be bent or extended depending on the stage of catalysis

Aerococcus viridans

Organism

Organism	UniProt	Comment	Textmining
Aerococcus viridans	A9X9K8	-	-

Purification (Commentary)

Purification (Comment)	Organism
by gel filtration	Aerococcus viridans

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
pyruvate + phosphate + O2	-	Aerococcus viridans	acetyl phosphate + CO2 + H2O2	-	?

Subunits

Subunits	Comment	Organism
homotetramer	crystallography	Aerococcus viridans

Synonyms

Synonyms	Comment	Organism
POX	-	Aerococcus viridans

Cofactor

Cofactor	Comment	Organism	Structure
FAD	-	Aerococcus viridans
thiamine diphosphate	-	Aerococcus viridans