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Literature summary extracted from

  • Guo, W.; West, J.M.; Dutton, A.S.; Tsuruta, H.; Kantrowitz, E.R.
    Trapping and structure determination of an intermediate in the allosteric transition of aspartate transcarbamoylase (2012), Proc. Natl. Acad. Sci. USA, 109, 7741-7746.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.3.2 expression of wild-type and mutant enzymes in Escherichia coli strain EK1104 containing the plasmid pEK695 Escherichia coli

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.1.3.2 purified recombinant mutant enzyme K164E/E239K, mixing of 10 mg/ml enzyme in 50 mM Tris-acetate, pH 8.3, with 0.002 ml of crystallization buffer containing 16% w/v PEG 4000, 0.04 M Na2MoO4-2H2O, 0.04 M N-cyclohexyl-3-aminopropanesulfonic acid, and 30 mM Tris-acetate, pH 8.75, and equilibration over a reservoir of crystallization buffer of 1.0 ml, 20°C, 2 weeks, X-ray diffraction structure determination and analysis Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
2.1.3.2 D236A site-directed mutagenesis, the wild-type enzyme shows o change in structure by SAXS through the temperature range of 4°C to 55°C, whereas the D236A ATCase exhibits a large shift toward the T state between 4°C and 30°C, with a minor shift back toward the R state between 30°C and 45°C Escherichia coli
2.1.3.2 K164E/E239K site-directed mutagenesis, a mutant aspartate transcarbamoylase exists in an intermediate quaternary structure between the canonical T and R structures, crystal structure and quaternary conformation analysis, detailed overview. pH-Dependent structural alteration consistent with either a pH-induced conformational change or a pH-induced alteration in the T to R equilibrium 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 L-aspartate + carbamoyl phosphate Escherichia coli
-
 phosphate + N-carbamoyl-L-aspartate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.1.3.2 Escherichia coli P0A786
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.3.2 recombinant wild-type and mutant enzymes from Escherichia coli strain EK1104 by isoelectric precipitation, anion exchange, and hydrophobic interaction chromatography, and gel filtration Escherichia coli

Substrates and Products (Substrate)

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

Synonyms

EC Number Synonyms Comment Organism
2.1.3.2 aspartate transcarbamoylase
-
 Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.1.3.2 37
-
 assay at Escherichia coli

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
2.1.3.2 additional information
-
 the wild-type enzyme shows o change in structure by SAXS through the temperature range of 4°C to 55°C, whereas the D236A ATCase exhibits a large shift toward the T state between 4°C and 30°C, with a minor shift back toward the R state between 30°C and 45°C 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 allosteric transition between the T and R enzyme states Escherichia coli