Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.1.3.2 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
Search for more literature for 2.1.3.2

Crystallization (Commentary)

Crystallization (Comment) Organism
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

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

KM Value [mM]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

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

Synonyms Comment Organism
aspartate transcarbamoylase
-
 Escherichia coli
ATCase
-
 Escherichia coli