EC Number   |
Substrates |
Organism |
Products  |
Reversibility |
|---|
    2.1.3.2 | more |
link between enzyme activity and gametogenesis |
Mya arenaria |
? |
- |
? |
| 2.1.3.2 | more |
the allosteric enzyme shows homotropic cooperative interactions between the catalytic sites for the binding of aspartate due to a quarternary structure transition between high aspartate affinity T state and R state |
Escherichia coli |
? |
- |
? |
| 2.1.3.2 | more |
ACT-DHOD gene is transcribed to ACT-DHOD mRNA, translated to the single protein, ACT-DHOD, and finally converted to mature independent DHOD and ACT |
Neobodo saliens |
? |
- |
? |
| 2.1.3.2 | more |
concerted transition between structural and functional states of either low affinity, low activity or high affinity, high activity for aspartate. Addition of ATP along with the substrates increases the rate of the transition from the T to the R state and also decreases the duration of the R-state steady-state phase. Addition of CTP or the combination of CTP/UTP to the substrates significantly decreases the rate of the T-R transition and causes a shift in the enzyme population towards the T state even at saturating substrate concentrations |
Escherichia coli |
? |
- |
? |
| 2.1.3.2 | more |
direct intermolecular interactions between the enzymes catalyzing the first three reaction steps of the de novo pyrimidine biosynthetic pathway, carbamoylphosphate synthetase II (CPSII), aspartate transcarbamoylase (ATC), and dihydroorotase (DHO), of the parasitic protist Trypanosoma cruzi, interaction analysis, overview |
Trypanosoma cruzi |
? |
- |
? |
| 2.1.3.2 | more |
conformational changes due to nucleotide binding, overview |
Escherichia coli |
? |
- |
? |
| 2.1.3.2 | more |
in the structure of the enzyme trapped in the R state with specific disulfide bonds, two phosphate molecules are bound per active site. The position of the first phosphate corresponds to the position of the phosphate of carbamoyl phosphate and the position of the phosphonate of inhibitor N-phosphonacetyl-L-aspartate. However, the second, more weakly bound phosphate is bound in a positively charged pocket that is more accessible to the surface than the other phosphate. The second phosphate appears to be on the path that phosphate would have to take to exit the active site |
Escherichia coli |
? |
- |
? |
| 2.1.3.2 | more |
CAD is a rate-limiting enzyme required for the formation of UDP sugar, upstream of two different metabolic pathways; the de novo biosynthesis of pyrimidine and pyrimide-based nucleotides, and the formation of UDP sugar intermediates, required for UDP-dependent glycosylation events |
Danio rerio |
? |
- |
? |
| 2.1.3.2 | carbamoyl phosphate + L-asparagine |
the enzyme catalyzes the carbamoylation of L-Asn with a Km of 122 mM and a maximal velocity 10fold lower than observed with the natural substrate, L-Asp. As opposed to L-Asp, no cooperativity is observed with respect to L-Asn |
Escherichia coli |
phosphate + N-carbamoyl-L-asparagine |
- |
? |
| 2.1.3.2 | carbamoyl phosphate + L-aspartate |
- |
Salmonella enterica subsp. enterica serovar Typhimurium |
phosphate + N-carbamoyl-L-aspartate |
- |
? |
