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Literature summary for 2.1.3.2 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
Search for more literature for 2.1.3.2

Cloned(Commentary)

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

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Inhibitors Comment Organism Structure
CTP
-
 Escherichia coli
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
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)

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 P0A786 gene pyrB
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
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

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

Temperature Optimum [°C]

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

pH Optimum

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

General Information

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