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Literature summary for 6.3.5.5 extracted from

  • Thoden, J.B.; Huang, X.; Kim, J.; Raushel, F.M.; Holden, H.M.
    Long-range allosteric transitions in carbamoyl phosphate synthetase (2004), Protein Sci., 13, 2398-2405.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
C248D mutant of small subunit, crystals are grown at 4°C by batch from 8% poly(ethylene glycol) 8000, 0.65 M tetraethylammonium chloride, 0.5 mM MnCl2, 100 mM KCl, 1.5 mM ADP, 25 mM GEPES, pH 7.4, 0.5 mM L-Orn. The crystals belong to the space group P2(1)2(1)2(1) with unit cell dimensions of a = 151.1 A, b = 164.2 A, and c = 331.5A and one complete (alphabeta)4-heeterotetramer per asymmetric unit Escherichia coli

Protein Variants

Protein Variants Comment Organism
C248D partial glutaminase activity of the mutant protein is increased 40fold relative to the wild-type enzyme Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 ATP + L-Gln + HCO3-
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Escherichia coli 2 ADP + phosphate + L-Glu + carbamoyl phosphate
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Subunits

Subunits Comment Organism
More the enzyme consists of two polypeptide chains referred to as small and large subunits, which contain a total of three separate active sites that are connected by an intramolecular tunnel Escherichia coli