Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli BL21(DE3) | Bacillus subtilis |
Crystallization (Comment) | Organism |
---|---|
X-ray crystal structure with bound uridine 5-monophosphate | Bacillus subtilis |
General Stability | Organism |
---|---|
unliganded enzyme without bound UMP or OMP forms heavy precipitates during purification | Bacillus subtilis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
Orotidine 5'-phosphate | Bacillus subtilis | catalyzes the final step in the de novo biosynthesis of uridine monophosphate | UMP + CO2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus subtilis | P25971 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant enzyme | Bacillus subtilis |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
orotidine 5'-phosphate = UMP + CO2 | reaction mechanism | Bacillus subtilis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
Orotidine 5'-phosphate | catalytic mechanism, bimolecular electrophilic substitution mechanism in which decarboxylation and carbon-carbon bond protonation by Lys-62 occur in a concerted action, enzyme/active site structure, one active site per monomer, located near the dimer interface | Bacillus subtilis | UMP + CO2 | - |
? | |
Orotidine 5'-phosphate | catalyzes the final step in the de novo biosynthesis of uridine monophosphate | Bacillus subtilis | UMP + CO2 | - |
? |
Subunits | Comment | Organism |
---|---|---|
homodimer | active form, subunit structure | Bacillus subtilis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
additional information | no cofactor requirement | Bacillus subtilis |