Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Leishmania major |
Crystallization (Comment) | Organism |
---|---|
apo-enzyme and in complex with orotate and with fumarate, to 2.0 A, 2.5 A and 1.9 A resolution, respectively. Both orotate and fumarate bind to the same active site and exploit similar interactions, consistent with a ping-pong mechanism. Rearrangements in the conformation of the catalytic loop have direct influence on the dimeric interface | Leishmania major |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Leishmania major | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(S)-dihydroorotate + fumarate | - |
Leishmania major | orotate + succinate | - |
? |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FMN | two molecules per dimer in the asymmetric crystal unit | Leishmania major |