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Literature summary extracted from

  • Cardia, J.P.; Eldo, J.; Xia, J.; ODay, E.M.; Tsuruta, H.; Gryncel, K.R.; Kantrowitz, E.R.
    Use of L-asparagine and N-phosphonacetyl-L-asparagine to investigate the linkage of catalysis and homotropic cooperativity in E. coli aspartate transcarbamoylase (2008), Proteins Struct. Funct. Bioinform., 71, 1088-1096.
No PubMed abstract available

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.1.3.2 X-ray crystal structure of the N-phosphonacetyl-L-asparagine complexed with ATCase. Analysis of the crystal structure of the enzyme in the presence of N-phosphonacetyl-L-asparagine reveals that the binding of N-phosphonacetyl-L-asparagine is similar to that of the R-state complex of ATCase with N-phosphonaceyl-L-aspartate, another potent inhibitor of the enzyme Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.1.3.2 N-phosphonacetyl-L-asparagine potent inhibitor of ATCase Escherichia coli
2.1.3.2 N-phosphonacetyl-L-aspartate
-
 Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.3.2 12
-
 L-aspartate
-
 Escherichia coli
2.1.3.2 122
-
 L-asparagine
-
 Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.3.2 carbamoyl phosphate + L-aspartate Escherichia coli
-
 phosphate + N-carbamoyl-L-aspartate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.1.3.2 Escherichia coli
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
-
 Escherichia coli phosphate + N-carbamoyl-L-aspartate
-
 ?
2.1.3.2 carbamoyl phosphate + 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 Escherichia coli phosphate + N-carbamoyl-L-aspartate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.1.3.2 aspartate transcarbamoylase
-
 Escherichia coli
2.1.3.2 ATCase
-
 Escherichia coli