Cloned (Comment) | Organism |
---|---|
expressed in Escherichia coli DH1 | 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 | UniProt | Comment | Textmining |
---|---|---|---|
Aerococcus viridans | A9X9K8 | - |
- |
Purification (Comment) | Organism |
---|---|
by gel filtration | Aerococcus viridans |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
pyruvate + phosphate + O2 | - |
Aerococcus viridans | acetyl phosphate + CO2 + H2O2 | - |
? |
Subunits | Comment | Organism |
---|---|---|
homotetramer | crystallography | Aerococcus viridans |
Synonyms | Comment | Organism |
---|---|---|
POX | - |
Aerococcus viridans |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | - |
Aerococcus viridans | |
thiamine diphosphate | - |
Aerococcus viridans |