Activating Compound | Comment | Organism | Structure |
---|---|---|---|
acetate | 25 mM, 2.3fold activation | Bacillus subtilis | |
additional information | activity is not regulated by nucleotide triphosphates | Bacillus subtilis |
Cloned (Comment) | Organism |
---|---|
overexpression in Escherichia coli | Bacillus subtilis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | - |
Escherichia coli | |
additional information | - |
additional information | enzyme exhibits Michaelis-Menten kinetics for both of its substrates | Bacillus subtilis | |
0.11 | - |
Carbamoyl phosphate | - |
Bacillus subtilis | |
7 | - |
aspartate | - |
Bacillus subtilis |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
17000 | - |
6 * 33000 + 6 * 17000, 2C3/3R2 holoenzyme | Escherichia coli |
33000 | - |
6 * 33000 + 6 * 17000, 2C3/3R2 holoenzyme | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
carbamoylphosphate + L-aspartate | Bacillus subtilis | - |
phosphate + N-carbamoyl-L-aspartate | - |
? | |
carbamoylphosphate + L-aspartate | Escherichia coli | - |
phosphate + N-carbamoyl-L-aspartate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus subtilis | - |
- |
- |
Escherichia coli | - |
- |
- |
Purification (Comment) | Organism |
---|---|
Q-Sepharose, Matrex gel Red A, Matrex Phenyl Cellufine | Bacillus subtilis |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate | enzyme exhibits homotropic cooperativity for aspartate, is heterotropically activated by ATP and is heterotropically inhibited by CTP and UTP | Escherichia coli |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
148.3 | - |
recombinant enzyme | Bacillus subtilis |
333 | - |
recombinant enzyme, in the presence of 50 mM Tris-acetate | Bacillus subtilis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
carbamoyl phosphate + L-aspartate | - |
Bacillus subtilis | phosphate + N-carbamoyl-L-aspartate | - |
? | |
carbamoyl phosphate + L-aspartate | - |
Escherichia coli | phosphate + N-carbamoyl-L-aspartate | - |
? | |
carbamoylphosphate + L-aspartate | - |
Bacillus subtilis | phosphate + N-carbamoyl-L-aspartate | - |
? | |
carbamoylphosphate + L-aspartate | - |
Escherichia coli | phosphate + N-carbamoyl-L-aspartate | - |
? |
Subunits | Comment | Organism |
---|---|---|
dodecamer | 6 * 33000 + 6 * 17000, 2C3/3R2 holoenzyme | Escherichia coli |