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carbamoyl phosphate + L-asparagine
phosphate + N-carbamoyl-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
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-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
L-aspartate + carbamoyl phosphate
phosphate + N-carbamoyl-L-aspartate
additional information
?
-
carbamoyl phosphate + L-aspartate

phosphate + N-carbamoyl-L-aspartate
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?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
the enzyme catalyzes the first committed step in pyrimidine biosynthesis
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
substrate binding causes significant conformational changes
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
Arg229, which interacts with the beta-carboxylate of L-Asp, plays a critical role in the orientation of L-Asp in the active site and demonstrates the requirement of the beta-carboxylate of L-Asp in the mechanism of domain closure and the allosteric transition in Escherichia coli ATCase
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-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
upon substrate binding, allosteric Escherichia coli aspartate transcarbamoylase adopts alternate quaternary structures, stabilized by a set of interdomain and intersubunit interactions, which are readily differentiated by their solution x-ray scattering curves. The cooperative binding of aspartate in aspartate transcarbamoylase appears to result from the combination of the preexisting quaternary structure equilibrium with local changes induced by binding of carbamoyl phosphate
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-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
the enzyme catalyzes the first step in the pyrimidine biosynthetic pathway
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
the enzyme catalyzes the first step in the pyrimidine biosynthetic pathway
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
Pigeon
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
Pseudomonas vulgaris
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
there is no preferential partitioning of carbamoyl phosphate between the arginine and pyrimidine biosynthetic pathways. Channeling must occur during the dynamic association of coupled enzymes pairs. The interaction of carbamoyl-phosphate synthetase/aspartate transcarbamoylase is demonstrated by the unexpectedly weak inhibition of the coupled reaction by the bisubstrate analog, N-(phosphonacetyl)-L-aspartate. In the coupled reaction, the effective concentration of carbamoyl phosphate in the vicinity of the aspartate transcarbamoylase active site is 96fold higher than the concentration in the bulk phase. Channeling probably plays an essential role in protecting this very unstable intermediate of metabolic pathways performing at extreme temperatures
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-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
specific for L-aspartate
-
?
carbamoylphosphate + L-aspartate

phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
second enzyme of pyrimidine synthesis
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
catalyzes the formation of carbamoyl-L-aspartate, the first compound unique to the biosynthetic pathway for pyrimidine nucleotides
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
catalyzes the formation of carbamoyl-L-aspartate, the first compound unique to the biosynthetic pathway for pyrimidine nucleotides
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
Pigeon
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
Pseudomonas vulgaris
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
L-aspartate + carbamoyl phosphate

phosphate + N-carbamoyl-L-aspartate
-
-
-
?
L-aspartate + carbamoyl phosphate
phosphate + N-carbamoyl-L-aspartate
carbamoyl phosphate binding structure, in silico docking and electrostatic calculations, overview
-
-
?
L-aspartate + carbamoyl phosphate
phosphate + N-carbamoyl-L-aspartate
-
-
-
-
?
L-aspartate + carbamoyl phosphate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
L-aspartate + carbamoyl phosphate
phosphate + N-carbamoyl-L-aspartate
-
-
i.e. ureidosuccinic acid
-
?
L-aspartate + carbamoyl phosphate
phosphate + N-carbamoyl-L-aspartate
-
ATCase displays ordered substrate binding and product release, remaining in the R state until substrates are exhausted. Wild-type ATCase is in a T-state structure with bound product phosphate
-
-
?
L-aspartate + carbamoyl phosphate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
additional information

?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
conformational changes due to nucleotide binding, overview
-
-
?
additional information
?
-
-
conformational changes due to nucleotide binding, overview
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
link between enzyme activity and gametogenesis
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
L-aspartate + carbamoyl phosphate
phosphate + N-carbamoyl-L-aspartate
additional information
?
-
carbamoyl phosphate + L-aspartate

phosphate + N-carbamoyl-L-aspartate
-
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
the enzyme catalyzes the first committed step in pyrimidine biosynthesis
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
the enzyme catalyzes the first step in the pyrimidine biosynthetic pathway
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
the enzyme catalyzes the first step in the pyrimidine biosynthetic pathway
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
there is no preferential partitioning of carbamoyl phosphate between the arginine and pyrimidine biosynthetic pathways. Channeling must occur during the dynamic association of coupled enzymes pairs. The interaction of carbamoyl-phosphate synthetase/aspartate transcarbamoylase is demonstrated by the unexpectedly weak inhibition of the coupled reaction by the bisubstrate analog, N-(phosphonacetyl)-L-aspartate. In the coupled reaction, the effective concentration of carbamoyl phosphate in the vicinity of the aspartate transcarbamoylase active site is 96fold higher than the concentration in the bulk phase. Channeling probably plays an essential role in protecting this very unstable intermediate of metabolic pathways performing at extreme temperatures
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate

phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
second enzyme of pyrimidine synthesis
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
catalyzes the formation of carbamoyl-L-aspartate, the first compound unique to the biosynthetic pathway for pyrimidine nucleotides
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
catalyzes the formation of carbamoyl-L-aspartate, the first compound unique to the biosynthetic pathway for pyrimidine nucleotides
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
Pigeon
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
Pseudomonas vulgaris
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
L-aspartate + carbamoyl phosphate

phosphate + N-carbamoyl-L-aspartate
-
-
-
?
L-aspartate + carbamoyl phosphate
phosphate + N-carbamoyl-L-aspartate
-
-
-
-
?
L-aspartate + carbamoyl phosphate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
L-aspartate + carbamoyl phosphate
phosphate + N-carbamoyl-L-aspartate
-
-
i.e. ureidosuccinic acid
-
?
L-aspartate + carbamoyl phosphate
phosphate + N-carbamoyl-L-aspartate
-
-
-
?
additional information

?
-
-
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
-
-
?
additional information
?
-
-
link between enzyme activity and gametogenesis
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(2S)-2-(([hydroxy(hydroxymethyl)phosphoryl]acetyl)amino)butanedioic acid
-
competitive
(2S)-2-(([hydroxy(oxido)-lambda5-phosphanyl]acetyl)amino)butanedioic acid
-
competitive
1,4,6,7-tetrabromo-2,3-naphthalenediol
-
2,2-dimethylsuccinate
-
-
2,3-napthalenediol
non-competitive inhibitor
2-(4-hydroxy-2,4-dioxo-4lamdba5-[1,4]azaphosphinan-1-yl)-succinic acid
-
competitive
2-methylquinazolin-4(3H)-one
-
-
2-phenyl-1,3-4(H)benzothiazin-4-thione
-
noncompetitive inhibitor towards both aspartate and carbamoyl phosphate
3-amino-6,8-dibromo-2-methyl-4(3H)-quinazolinone
-
-
3-amino-6,8-dibromo-2-phenyl-4-(3H)-quinazolinone
-
noncompetitive
4,5-dicarboxy-2-ketopentylphosphonate
-
-
4-(3-methyl-2,4,6-trioxo-2,3,4,5,6,11-hexahydro-1H-indeno[2',1':5,6]pyrido[2,3-d]pyrimidin-5-yl)phenyl 2-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)propanoate
5'-UMP
-
2'-UMP and 3'-UMP have no effect
5-([6-[(2E)-2-([2-[(2,4-dichlorophenyl)methoxy]phenyl]methylidene)hydrazinyl][1,2,5]oxadiazolo[3,4-b]pyrazin-5-yl]amino)-1,3-dihydro-2H-benzimidazol-2-one
6,7-dibromo-2,3-naphthalenediol
-
Carbonyldiphosphonate
-
-
dichlormethylenediphosphonate
-
-
Diphosphate analogues
-
-
-
Guanidine-HCl
-
800 mM, almost complete inhibition
HgCl2
-
0.001 mM, 50% inhibition
Mersalyl
-
0.01 mM, 50% inhibition
Methylenediphosphonate
-
-
N-(2-hydroxy-acetyl)-L-aspartic acid-phosphate
-
competitive
N-(phosphonacetyl)-L-aspartate
N-(Phosphonoacetyl)-L-aspartate
N-(phosphonoacetyl)-L-aspartic acid
-
-
N-Diphosphoryl-L-aspartate
-
-
N-methyl phosphonoacetamide
-
-
N-phosphonacetyl-L-asparagine
-
potent inhibitor of ATCase
N-phosphonacetyl-L-aspartate
N-phosphonoacetyl-L-aspartate
N-phosphoryl-L-aspartate
-
-
N-pyrophosphoryl-L-aspartate
-
-
O-phosphonoacetyl-oxosuccinate
-
-
p-mercuribenzoate
-
0.01 mM, 50% inhibition
Phosphonoacetic acid
-
1 mM, 50% inhibition
S-diphosphoryl-mercaptosuccinate
-
-
S-phosphonoacetyl-mercaptosuccinate
-
-
Urea
-
2.5 M, almost complete inhibition
4-(3-methyl-2,4,6-trioxo-2,3,4,5,6,11-hexahydro-1H-indeno[2',1':5,6]pyrido[2,3-d]pyrimidin-5-yl)phenyl 2-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)propanoate

-
4-(3-methyl-2,4,6-trioxo-2,3,4,5,6,11-hexahydro-1H-indeno[2',1':5,6]pyrido[2,3-d]pyrimidin-5-yl)phenyl 2-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)propanoate
-
-
5-([6-[(2E)-2-([2-[(2,4-dichlorophenyl)methoxy]phenyl]methylidene)hydrazinyl][1,2,5]oxadiazolo[3,4-b]pyrazin-5-yl]amino)-1,3-dihydro-2H-benzimidazol-2-one

-
5-([6-[(2E)-2-([2-[(2,4-dichlorophenyl)methoxy]phenyl]methylidene)hydrazinyl][1,2,5]oxadiazolo[3,4-b]pyrazin-5-yl]amino)-1,3-dihydro-2H-benzimidazol-2-one
-
-
acetyl phosphate

-
3 mM, 50% inhibition
ADP

-
5 mM, 19% residual activity
ADP
-
5 mM, 8% residual activity
aspartate

-
-
aspartate
-
at high concentrations
ATP

-
dual regulatory pattern, activating the enzyme at low concentrations and inhibiting it in the mM range
ATP
-
excess MgCl2 abolishes inhibition
ATP
-
5 mM, 8% residual activity
ATP
inhibitory effect on the catalytic subunits encoded by the sole pyrB gene. The complete ATCase purified from recombinant Escherichia coli is strongly activated
ATP
-
1 mM, 40% inhibition
carbamoyl aspartate

-
-
carbamoyl aspartate
-
noncompetitive vs. carbamoyl phosphate and aspartate
CDP

-
10 mM, 61% inhibition
CDP
-
5 mM, 23% residual activity
CTP

-
800-1000 mM urea lower or eliminate CTP inhibition
CTP
-
synergistic inhibition by CTP and UTP
CTP
-
competitive vs. carbamoyl phosphate
CTP
-
synergistic inhibition by CTP and UTP
CTP
-
CTP inhibits ATCase activity. Experimentally driven, statistical modeling approach (high-dimensional model representation, RS-HDMR) to investigate regulation of ATCase in response to varying concentrations of its nucleotide regulators ATP, CTP, GTP, and UTP (at fixed substrate concentrations)
CTP
-
addition of CTP or the combination of CTP/UTP to the substrates significantly decreases the rate of the low activity-high activity T-R transition and causes a shift in the enzymepopulation towards the T state even at saturating substrate concentrations
CTP
-
ATCase is feedback inhibited by CTP and synergistically by the combination of CTP plus UTP
CTP
aspartate transcarbamoylase is feedback inhibited by CTP in the presence of CTP. CTP and UTP do not bind competitively, CTP binding structure, overview
CTP
demetaled CTP, synergistic inhibition with UTP, while UTP alone has little or no influence on the enzyme activity, mechanism, overview. Binding of UTP can enhance the binding of CTP and presence of a metal ion such as Mg2+ is required for synergistic inhibition. Structure of the ATCase-CTP-UTP-Mg2+ complex
CTP
-
10 mM, 79% inhibition
CTP
-
5 mM, 4% residual activity
CTP
-
5 mM, 37% residual activity
CTP
-
allosteric inhibitor
CTP
inhibitory effect on the catalytic subunits encoded by the sole pyrB gene. The complete ATCase purified from recombinant Escherichia coli is strongly activated
CTP
2 mM, about 90% inhibition
diphosphate

-
-
diphosphate
-
5 mM, 6% residual activity
diphosphate
-
5 mM, 10% residual activity
GDP

-
5 mM, 39% residual activity
GDP
-
5 mM, 38% residual activity
GTP

-
-
GTP
-
GTP inhibits ATCase activity. Experimentally driven, statistical modeling approach (high-dimensional model representation, RS-HDMR) to investigate regulation of ATCase in response to varying concentrations of its nucleotide regulators ATP, CTP, GTP, and UTP (at fixed substrate concentrations)
GTP
-
5 mM, 11% residual activity
GTP
inhibitory effect on the catalytic subunits encoded by the sole pyrB gene. The complete ATCase purified from recombinant Escherichia coli is strongly activated
GTP
-
1 mM, 20% inhibition
iodoacetate

-
-
Maleate

-
-
Maleate
-
15 mM, 50% inhibition
N-(phosphonacetyl)-L-aspartate

-
treatment of seedling with 1 mM, results in delayed germination, inhibition of cotyledon expansion, leaf development and root growth. 2fold increase in enzyme activity and protein level
N-(phosphonacetyl)-L-aspartate
-
-
N-(phosphonacetyl)-L-aspartate
-
-
N-(phosphonacetyl)-L-aspartate
there is no preferential partitioning of carbamoyl phosphate between the arginine and pyrimidine biosynthetic pathways. Channeling must occur during the dynamic association of coupled enzymes pairs. The interaction of carbamoyl-phosphate synthetase/aspartate transcarbamoylase is demonstrated by the unexpectedly weak inhibition of the coupled reaction by the bisubstrate analog, N-(phosphonacetyl)-L-aspartate
N-(Phosphonoacetyl)-L-aspartate

-
-
N-(Phosphonoacetyl)-L-aspartate
-
-
N-(Phosphonoacetyl)-L-aspartate
-
0.0001 mM, 50% inhibition
N-(Phosphonoacetyl)-L-aspartate
-
-
N-(Phosphonoacetyl)-L-aspartate
-
0.011 mM, 50% inhibition, low concentrations activate
N-(Phosphonoacetyl)-L-aspartate
0.002 mM, 50% inhibition of catalytic subunit
N-(Phosphonoacetyl)-L-aspartate
-
-
N-(Phosphonoacetyl)-L-aspartate
-
competitive vs. carbamoyl phosphate, noncompetitive vs. aspartate
N-phosphonacetyl-L-aspartate

-
binding of the bisubstrate analogue N-phosphonacetyl-L-aspartate to the aspartate transcarbamoylase subunit inhibits the activity of the distal dihydroorotase subunit
N-phosphonacetyl-L-aspartate
a bisubstrate/transition state analogue, binding structure, in silico docking and electrostatic calculations, overview
N-phosphonacetyl-L-aspartate
-
-
N-phosphonacetyl-L-aspartate
-
PALA, a bisubstrate transition state analogue, and shows also ability of PALA to enhance the activity of ATCase at low concentrations of aspartate, in the presence of a saturating concentration of carbamoyl phosphat. Interactions between the side chain of Gln137 and the backbone carbonyl oxygen of Pro266 to the amino group on the tetrahedral carbon and the side chain of Arg54 with the ester oxygen between the phosphorus and the tetrahedral carbone
N-phosphonacetyl-L-aspartate
-
i.e. PALA, a bisubstrate analogue, the binding of PALA is able to stabilize the enzyme in the high-activity, high-affinity R state because its structure mimics the reaction's transition state structure. The concerted transition to the R state allows a majority of active sites free to react with substrates and release products while a minority of active sites bound with PALA are inactive but stabilize the enzyme in the R state. Therefore, at low concentrations of PALA the activity increases; however, as the concentration of PALA is increased more and more of the active sites are filled by the non-hydrolyzable bisubstrate analog and the activity drops. At high concentrations of Asp and a saturating concentration of carbamoyl phosphate, no PALA activation is observed. In the absence of allosteric effectors the average KD of PALA is 110 nM, decreasing to 65 nM in the presence of ATP and increasing to 266 nM in the presence of CTP
N-phosphonacetyl-L-aspartate
-
-
N-phosphonacetyl-L-aspartate
-
N-phosphonoacetyl-L-aspartate

-
competitive
N-phosphonoacetyl-L-aspartate
-
after addition of N-phosphonacetyl-L-aspartate to the enzyme, the transition rate is more than 1 order of magnitude slower than with the natural substrates
N-phosphonoacetyl-L-aspartate
binding structure, overview
nucleotides

-
-
-
p-chloromercuribenzoate

-
-
p-chloromercuribenzoate
-
6 mM, almost complete inhibition
p-hydroxymercuribenzoate

-
-
p-hydroxymercuribenzoate
-
strong inhibition
Phenobarbital

-
-
phosphate

-
-
phosphate
-
competitive vs. carbamoyl phosphate, noncompetitive vs. aspartate
succinate

-
-
succinate
-
10 mM, 50% inhibition
succinate
-
activator at low concentrations of both succinate and aspartate, inhibitor at high succinate concentrations and at high aspartate concentrations
Thiobarbituric acid

-
most potent inhibitor
Thiobarbituric acid
-
most potent inhibitor
thymidine

-
-
UDP

-
5 mM, 11% residual activity
UDP
-
5 mM, 7% residual activity
UDP
-
1 mM, 45% inhibition
UMP

-
-
UMP
-
5 mM, 6% residual activity
UMP
-
5 mM, 21% residual activity
UMP
-
0.1 mM, 25% inhibition, inhibition increases to 80% and 90% in the presence of 0.2 mM and 0.6 mM deoxycholate respectively
UMP
-
fatty acids with chains of C8 or longer, dodecylsulfate and decylsulfonate potentiate inhibition
UMP
-
0.8 mM, 85% inhibition
UMP
-
1 mM, 75% inhibition
UTP

-
weak inhibition
UTP
-
synergistic inhibition by CTP and UTP, no inhibition unless CTP is present
UTP
-
UTP inhibits ATCase activity. Experimentally driven, statistical modeling approach (high-dimensional model representation, RS-HDMR) to investigate regulation of ATCase in response to varying concentrations of its nucleotide regulators ATP, CTP, GTP, and UTP (at fixed substrate concentrations)
UTP
-
addition of CTP or the combination of CTP/UTP to the substrates significantly decreases the rate of the low activity-high activity T-R transition and causes a shift in the enzymepopulation towards the T state even at saturating substrate concentrations
UTP
aspartate transcarbamoylase is feedback inhibited by UTP in the presence of CTP. UTP binds to a unique site on each regulatory chain of the enzyme that is near but not overlapping with the known CTP site. CTP and UTP do not bind competitively, UTP binds to the r6 regulatory chain of ATCase, UTP binding structure, overview
UTP
inhibition with CTP, while UTP alone has little or no influence on the enzyme activity, mechanism, overview. UTP, in the presence of dCTP or CTP, binds at a site on a regulatory side chain 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. UTP binds more tightly in the presence of CTP. Structure of the ATCase-CTP-UTP-Mg2+ complex
UTP
UTP is able to synergistically inhibit ATCase in the presence of CTP, but UTP alone has little or no influence on activity
UTP
-
allosteric inhibitor
UTP
inhibitory effect on the catalytic subunits encoded by the sole pyrB gene. The complete ATCase purified from recombinant Escherichia coli is strongly activated
UTP
2 mM, about 90% inhibition
UTP
-
1 mM, 40% inhibition
additional information

conformational changes due to nucleotide binding, overview
-
additional information
-
conformational changes due to nucleotide binding, overview
-
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
-
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
-
additional information
not inhibited by fluorouracil
-
additional information
-
not inhibited by fluorouracil
-
additional information
-
not inhibited by CTP
-
additional information
-
50% inhibition at 80 MPa; not inhibited by phosphonoacetate, diphosphate or phosphate
-
additional information
-
kinetic analysis of properties of allosteric effectors alone and in combination with each other
-
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Anemia, Hypochromic
Mode of Action of the Toxin from Pseudomonas phaseolicola: I. Toxin Specificity, Chlorosis, and Ornithine Accumulation.
Anemia, Hypoplastic, Congenital
Elevation of pyrimidine enzyme activities in the RBC of patients with congenital hypoplastic anaemia and their parents.
Brain Neoplasms
Pyrimidine pathways enzymes in human tumors of brain and associated tissues: potentialities for the therapeutic use of N-(phosphonacetyl-L-aspartate and 1-beta-D-arabinofuranosylcytosine.
Carcinoma
The effects of pH and inhibitors upon the catalytic activity of the dihydroorotase of multienzymatic protein pyr1-3 from mouse Ehrlich ascites carcinoma.
Carcinoma, Ehrlich Tumor
Binding of radiolabeled N-(phosphonacetyl)-L-aspartate to aspartate transcarbamylase from Ehrlich ascites tumor cells.
Carcinoma, Hepatocellular
A multienzyme complex of carbamoyl-phosphate synthase (glutamine): aspartate carbamoyltransferase: dihydoorotase (rat ascites hepatoma cells and rat liver).
Carcinoma, Hepatocellular
Aspartate carbamoyltransferase inhibition and uridylate trapping result in a synergistic depression of uridine triphosphate in hepatoma cells.
Carcinoma, Hepatocellular
Feedback inhibition of aspartate transcarbamylase in liver and in hepatoma.
Carcinoma, Hepatocellular
Phosphorylation and dephosphorylation of carbamoyl-phosphate synthetase II complex of rat ascites hepatoma cells.
Carcinoma, Hepatocellular
Purification of homogeneous glutamine-dependent carbamyl phosphate synthetase from ascites hepatoma cells as a complex with aspartate transcarbamylase and dihydroorotase.
Colonic Neoplasms
Phase II trial of N-(phosphonacetyl)-L-aspartate (PALA), 5-fluorouracil and recombinant interferon-alpha-2b in patients with advanced gastric carcinoma.
Herpes Simplex
A continuous spectrophotometric assay for aspartate transcarbamylase and ATPases.
Hypothyroidism
Effect of hypothyroidism on aspartate transcarbamylase, uridine kinase, and DNA biosynthesis during cerebellar development in the rat.
hypoxanthine phosphoribosyltransferase deficiency
Elevated aspartate transcarbamylase and dihydroorotase activities in erythrocytes from patients with hypoxanthine guanine phosphoribosyltransferase deficiency.
Infections
Activity of some hepatic enzymes in schistosomiasis and concomitant alteration of arylsulfatase B.
Infections
Metabolic Reprogramming of Host Cells in Response to Enteroviral Infection.
Lesch-Nyhan Syndrome
Elevated aspartate transcarbamylase and dihydroorotase activities in erythrocytes from patients with hypoxanthine guanine phosphoribosyltransferase deficiency.
Leukemia
Inhibition of cell growth by N-(phosphonacetyl)-L-aspartate in human and murine cells in vitro.
Melanoma
Inhibition of cell growth by N-(phosphonacetyl)-L-aspartate in human and murine cells in vitro.
Melanoma
Kinetic parameters of aspartate transcarbamylase in human normal and tumoral cell lines.
Melanoma, Experimental
Inhibition of cell growth by N-(phosphonacetyl)-L-aspartate in human and murine cells in vitro.
Mycoses
The Asc locus for resistance to Alternaria stem canker in tomato does not encode the enzyme aspartate carbamoyltransferase.
Myocardial Infarction
Further heterogeneity demonstrated for serum creatine kinase isoenzyme MM.
Neoplasms
Activity of aspartate transcarbamylase in mammary tumours induced by 7,12-dimethyl-benzanthracene in the rat.
Neoplasms
Binding of radiolabeled N-(phosphonacetyl)-L-aspartate to aspartate transcarbamylase from Ehrlich ascites tumor cells.
Neoplasms
Diversion of aspartate in ASS1-deficient tumours fosters de novo pyrimidine synthesis.
Neoplasms
Effects of N-(phosphonacetyl)-L-aspartate on murine tumors and normal tissues in vivo and in vitro and the relationship of sensitivity to rate of proliferation and level of aspartate transcarbamylase.
Neoplasms
Flux through the de novo pyrimidine pathway in vivo. Effect of N-phosphonacetyl-L-aspartate, a potent inhibitor of aspartate transcarbamylase.
Neoplasms
Increased incidence of CAD gene amplification in tumorigenic rat lines as an indicator of genomic instability of neoplastic cells.
Neoplasms
Long-term association of N-(phosphonacetyl)-L-aspartate with bone.
Neoplasms
Mechanisms of sensitivity or resistance of murine tumors to N-(phosphonacetyl)-L-aspartate (PALA).
Neoplasms
N-(Phosphonacetyl)-L-aspartate inhibition of the enzyme complex of pyrimidine biosynthesis.
Neoplasms
New regulatory mechanism-based inhibitors of aspartate transcarbamoylase for potential anticancer drug development.
Neoplasms
Phase I study of N-(phosphonacetyl)-L-aspartic acid (PALA).
Neoplasms
Pyrimidine pathways enzymes in human tumors of brain and associated tissues: potentialities for the therapeutic use of N-(phosphonacetyl-L-aspartate and 1-beta-D-arabinofuranosylcytosine.
Neoplasms
Targeting pyrimidine synthesis accentuates molecular therapy response in glioblastoma stem cells.
Neoplasms
Urea Cycle Dysregulation Generates Clinically Relevant Genomic and Biochemical Signatures.
ornithine carbamoyltransferase deficiency
Expression, purification and kinetic characterization of wild-type human ornithine transcarbamylase and a recurrent mutant that produces 'late onset' hyperammonaemia.
Ornithine Carbamoyltransferase Deficiency Disease
Expression, purification and kinetic characterization of wild-type human ornithine transcarbamylase and a recurrent mutant that produces 'late onset' hyperammonaemia.
Pre-Eclampsia
Insulin-like growth factor binding protein-1 at the maternal-fetal interface and insulin-like growth factor-I, insulin-like growth factor-II, and insulin-like growth factor binding protein-1 in the circulation of women with severe preeclampsia.
Sarcoma, Yoshida
Intracellular distribution of various enzymes concerned with DNA synthesis from normal and regenerating rat liver, and Yoshida sarcoma.
Starvation
19F nuclear magnetic resonance studies of fluorotyrosine-labeled aspartate transcarbamoylase. Properties of the enzyme and its catalytic and regulatory subunits.
Starvation
CAD gene expression in serum-starved and serum-stimulated hamster cells.
Starvation
Characterization of a Salmonella typhimurium mutant defective in phosphoribosylpyrophosphate synthetase.
Starvation
Effects of phosphate limitation on expression of genes involved in pyrimidine synthesis and salvaging in Arabidopsis.
Starvation
The Escherichia coli K-12 'wild types' W3110 and MG1655 have an rph frameshift mutation that leads to pyrimidine starvation due to low pyrE expression levels.
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