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

BRENDA support

Literature summary extracted from

  • Harris, K.M.; Cockrell, G.M.; Puleo, D.E.; Kantrowitz, E.R.
    Crystallographic snapshots of the complete catalytic cycle of the unregulated aspartate transcarbamoylase from Bacillus subtilis (2011), J. Mol. Biol., 411, 190-200.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.3.2 ATCase overexpression in Escherichia coli strain strain EK1104 Bacillus subtilis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.1.3.2 purified recombinant enzyme alone or complex with substrate carbamoyl phosphate or inhibitor N-phosphonacetyl-L-aspartate, hanging drop vapor diffusion method, 12 mg/ml protein is mixed with an equal volume of crystallization buffer containing 1.7 M (NH4)2SO4, 0.1 M Tris-HCl, pH 8.5, and 2.0% PEG 200, and equilibratopn over a reservoir of 0.5 ml of crystallization buffer at 20°C, 1 week, for substrate bound enzyme the crystals are soaked in mother liquor containing the ligand at 13.3 mM, for inhibitor bound form, the enzyme is crystallized as described using crystallization buffer containing 0.1 M potassium bromide, 0.1 M N-cyclohexyl-3-aminopropanesulfonic acid, pH 10.0, and 18% PEG 8000, 20°C, 1 week, X-ray diffraction structure determination and analysis at 2.1-2.6 A resolution Bacillus subtilis

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.1.3.2 N-phosphonacetyl-L-aspartate a bisubstrate/transition state analogue, binding structure, in silico docking and electrostatic calculations, overview Bacillus subtilis

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 Bacillus subtilis
-
 phosphate + N-carbamoyl-L-aspartate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.1.3.2 Bacillus subtilis P05654
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.3.2 recombinant enzyme from Escherichia coli strain EK114 by anion exchange chromatography, ammonium sulfate fractionation, and hydrophobic interaction chromatography Bacillus subtilis

Reaction

EC Number Reaction Comment Organism Reaction ID
2.1.3.2 carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate the catalytic cycle of ATCase leads from the ordered binding of the substrates to the formation and decomposition of the tetrahedral intermediate and to the ordered release of the products from the active site, ordered-binding mechanism, detailed overview Bacillus subtilis
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.3.2 L-aspartate + carbamoyl phosphate
-
 Bacillus subtilis phosphate + N-carbamoyl-L-aspartate
-
 ?
2.1.3.2 L-aspartate + carbamoyl phosphate carbamoyl phosphate binding structure, in silico docking and electrostatic calculations, overview Bacillus subtilis phosphate + N-carbamoyl-L-aspartate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.1.3.2 aspartate transcarbamoylase
-
 Bacillus subtilis
2.1.3.2 ATCase
-
 Bacillus subtilis

General Information

EC Number General Information Comment Organism
2.1.3.2 malfunction analysis of the conformational changes shows that there is a lack of cooperativity in trimeric ATCases that do not possess regulatory subunits Bacillus subtilis
2.1.3.2 metabolism ATCase catalyzes one of the first reactions in pyrimidine nucleotide biosynthesis Bacillus subtilis