EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
6.3.5.5 | ornithine | - |
Aquifex aeolicus |
EC Number | Cloned (Comment) | Organism |
---|---|---|
6.3.5.5 | expression in Escherichia coli | Aquifex aeolicus |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
6.3.5.5 | UMP | - |
Aquifex aeolicus |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
6.3.5.5 | additional information | - |
additional information | - |
Aquifex aeolicus |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
6.3.5.5 | 45000 | - |
CPS.A-subunit, CPS.B-subunit and glutaminase-subunit, 1* 64000 Da, 1 * 63000 Da and 1 * 45000 Da, but only the CPS.A-CPS.B-dimer has catalytic activity, SDS-PAGE | Aquifex aeolicus |
6.3.5.5 | 63000 | - |
CPS.A-subunit, CPS.B-subunit and glutaminase-subunit, 1* 64000 Da, 1 * 63000 Da and 1 * 45000 Da, but only the CPS.A-CPS.B-dimer has catalytic activity, SDS-PAGE | Aquifex aeolicus |
6.3.5.5 | 171000 | - |
- |
Aquifex aeolicus |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
6.3.5.5 | 2 ATP + L-Gln + HCO3- | Aquifex aeolicus | the product carbamoyl phosphate is the initial intermediate in the biosynthesis of both pyrimidine and arginine | 2 ADP + phosphate + L-Glu + carbamoyl phosphate | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
6.3.5.5 | Aquifex aeolicus | - |
- |
- |
6.3.5.5 | Bacillus subtilis | - |
- |
- |
6.3.5.5 | Cricetinae | - |
- |
- |
6.3.5.5 | Escherichia coli | - |
- |
- |
6.3.5.5 | Methanocaldococcus jannaschii | - |
- |
- |
6.3.5.5 | Pseudomonas aeruginosa | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
6.3.5.5 | recombinant enzyme | Aquifex aeolicus |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
6.3.5.5 | 0.041 | - |
recombinant enzyme | Aquifex aeolicus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
6.3.5.5 | 2 ATP + L-Gln + HCO3- | - |
Bacillus subtilis | 2 ADP + phosphate + L-Glu + carbamoyl phosphate | - |
? | |
6.3.5.5 | 2 ATP + L-Gln + HCO3- | - |
Escherichia coli | 2 ADP + phosphate + L-Glu + carbamoyl phosphate | - |
? | |
6.3.5.5 | 2 ATP + L-Gln + HCO3- | - |
Pseudomonas aeruginosa | 2 ADP + phosphate + L-Glu + carbamoyl phosphate | - |
? | |
6.3.5.5 | 2 ATP + L-Gln + HCO3- | - |
Methanocaldococcus jannaschii | 2 ADP + phosphate + L-Glu + carbamoyl phosphate | - |
? | |
6.3.5.5 | 2 ATP + L-Gln + HCO3- | - |
Cricetinae | 2 ADP + phosphate + L-Glu + carbamoyl phosphate | - |
? | |
6.3.5.5 | 2 ATP + L-Gln + HCO3- | - |
Aquifex aeolicus | 2 ADP + phosphate + L-Glu + carbamoyl phosphate | - |
? | |
6.3.5.5 | 2 ATP + L-Gln + HCO3- | the product carbamoyl phosphate is the initial intermediate in the biosynthesis of both pyrimidine and arginine | Aquifex aeolicus | 2 ADP + phosphate + L-Glu + carbamoyl phosphate | - |
? | |
6.3.5.5 | 2 ATP + NH4+ + HCO3- | - |
Aquifex aeolicus | 2 ADP + phosphate + carbamoyl phosphate | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
6.3.5.5 | heterotrimer | CPS.A-subunit, CPS.B-subunit and glutaminase-subunit, 1* 64000 Da, 1 * 63000 Da and 1 * 45000 Da, but only the CPS.A-CPS.B-dimer has catalytic activity, SDS-PAGE | Aquifex aeolicus |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
6.3.5.5 | 70 | 80 | CPS.A-CPS.B complex | Aquifex aeolicus |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
6.3.5.5 | 25 | 80 | The activity of the CPS.A-CPS.B complex remains unchanged between 25-60 °C and then increases 54% at 70°C. The loss of catalytic activity above 80°C is indicated of thermal denaturation. The large increase in thermal stability at temperatures prior to thermal denaturation is not observed in the CPS.A-CPS.B-glutaminase-subunit complex. | Aquifex aeolicus |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
6.3.5.5 | additional information | - |
additional information | - |
Aquifex aeolicus |