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Literature summary extracted from

  • Cockrell, G.M.; Zheng, Y.; Guo, W.; Peterson, A.W.; Truong, J.K.; Kantrowitz, E.R.
    New paradigm for allosteric regulation of Escherichia coli aspartate transcarbamoylase (2013), Biochemistry, 52, 8036-8047.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.3.2 gene pyrB, recombinant enzyme overexpression in Escherichia coli strain EK1104 Escherichia coli

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.1.3.2 purified recombinant enzyme, 20 mg/ml protein is mixed with 40 mM sodium citrate, 1 mM 2-mercaptoethanol, 0.2 mM EDTA, and 1.0 mM CTP, pH 5.7, at 20 °C, 1 week, X-ray diffraction structure determination and analysis at 2.1 A resolution Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.1.3.2 CTP
-
 Escherichia coli
2.1.3.2 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 Escherichia coli
2.1.3.2 UTP UTP is able to synergistically inhibit ATCase in the presence of CTP, but UTP alone has little or no influence on activity 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 P0A786 gene pyrB
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.3.2 recombinant enzyme from Escherichia coli strain EK1104 by ion exchange and hydrophobic interaction chromatography Escherichia coli

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
2.1.3.2 dodecamer the Escherichia coli ATCase holoenzyme is a dodecamer composed of six regulatory chains and six catalytic chains arranged into three regulatory dimers and two catalytic trimers Escherichia coli

Synonyms

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.1.3.2 25
-
 assay at Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.1.3.2 7.5
-
 assay at Escherichia coli

General Information

EC Number General Information Comment Organism
2.1.3.2 additional information nucleotide binding site specificity conformational changes due to nucleotide binding, overview Escherichia coli
2.1.3.2 physiological function enzyme aspartate transcarbamoylase catalyzes the committed step in pyrimidine nucleotide biosynthesis and allosterically regulates the pathway in Escherichia coli Escherichia coli