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EC Number Substrates Commentary Substrates Organism Products Commentary (Products) Reversibility
Show all pathways known for 2.1.3.2Display the word mapDisplay the reaction diagram Show all sequences 2.1.3.2more 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 ? - ?
Show all pathways known for 2.1.3.2Display the word mapDisplay the reaction diagram Show all sequences 2.1.3.2more 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 ? - ?
Show all pathways known for 2.1.3.2Display the word mapDisplay the reaction diagram Show all sequences 2.1.3.2more conformational changes due to nucleotide binding, overview Escherichia coli ? - ?
Show all pathways known for 2.1.3.2Display the word mapDisplay the reaction diagram Show all sequences 2.1.3.2more 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 ? - ?
Show all pathways known for 2.1.3.2Display the word mapDisplay the reaction diagram Show all sequences 2.1.3.2more 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 ? - ?
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