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Literature summary extracted from

  • Fetler, L.; Kantrowitz, E.R.; Vachette, P.
    Direct observation in solution of a preexisting structural equilibrium for a mutant of the allosteric aspartate transcarbamoylase (2007), Proc. Natl. Acad. Sci. USA, 104, 495-500.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
2.1.3.2 D236A the small-angle x-ray scattering pattern of unliganded D236A ATCase differs from the scattering pattern of the wild-type enzyme Escherichia coli

Organism

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

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.3.2 carbamoyl phosphate + L-aspartate upon substrate binding, allosteric Escherichia coli aspartate transcarbamoylase adopts alternate quaternary structures, stabilized by a set of interdomain and intersubunit interactions, which are readily differentiated by their solution x-ray scattering curves. The cooperative binding of aspartate in aspartate transcarbamoylase appears to result from the combination of the preexisting quaternary structure equilibrium with local changes induced by binding of carbamoyl phosphate Escherichia coli phosphate + N-carbamoyl-L-aspartate
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Synonyms

EC Number Synonyms Comment Organism
2.1.3.2 aspartate transcarbamoylase
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 Escherichia coli