Cloned (Comment) | Organism |
---|---|
gene pyrB, recombinant enzyme overexpression in Escherichia coli strain EK1104 | Escherichia coli |
Crystallization (Comment) | Organism |
---|---|
purified recombinant enzyme, 20 mg/ml protein is mixed with 40 mM sodium citrate, 1 mM 2-mercaptoethanol, 0.2 mM EDTA, and 1.0 mM CTP, pH 5.7, at 20 °C, 1 week, X-ray diffraction structure determination and analysis at 2.1 A resolution | Escherichia coli |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
CTP | - |
Escherichia coli | |
additional information | CTP and dCTP bind in a very similar fashion, UTP, in the presence of dCTP or CTP, binds at a site that does not overlap the CTP/dCTP site, and the triphosphates of the two nucleotides are parallel to each other with a metal ion, in this case Mg2+, coordinated between the beta- and gamma-phosphates of the two nucleotides, synergistic Inhibition of ATCase by CTP and UTP is metal-dependent, Mg2+ and Mn2+ act best, binding structures, overview | Escherichia coli | |
UTP | UTP is able to synergistically inhibit ATCase in the presence of CTP, but UTP alone has little or no influence on activity | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
carbamoyl phosphate + L-aspartate | Escherichia coli | - |
phosphate + N-carbamoyl-L-aspartate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P0A786 | gene pyrB | - |
Purification (Comment) | Organism |
---|---|
recombinant enzyme from Escherichia coli strain EK1104 by ion exchange and hydrophobic interaction chromatography | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
carbamoyl phosphate + L-aspartate | - |
Escherichia coli | phosphate + N-carbamoyl-L-aspartate | - |
? |
Subunits | Comment | Organism |
---|---|---|
dodecamer | the Escherichia coli ATCase holoenzyme is a dodecamer composed of six regulatory chains and six catalytic chains arranged into three regulatory dimers and two catalytic trimers | Escherichia coli |
Synonyms | Comment | Organism |
---|---|---|
aspartate carbamoyltransferase | - |
Escherichia coli |
aspartate transcarbamoylase | - |
Escherichia coli |
ATCase | - |
Escherichia coli |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Escherichia coli |
General Information | Comment | Organism |
---|---|---|
additional information | nucleotide binding site specificity conformational changes due to nucleotide binding, overview | Escherichia coli |
physiological function | enzyme aspartate transcarbamoylase catalyzes the committed step in pyrimidine nucleotide biosynthesis and allosterically regulates the pathway in Escherichia coli | Escherichia coli |