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Literature summary extracted from

  • Ruiz-Ramos, A.; Velazquez-Campoy, A.; Grande-Garcia, A.; Moreno-Morcillo, M.; Ramon-Maiques, S.
    Structure and functional characterization of human aspartate transcarbamoylase, the target of the anti-tumoral drug PALA (2016), Structure, 24, 1081-1094 .
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.1.3.2 free enzyme and bound to carbamoyl phosphate or N-phosphonacetyl-L-aspartate Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
2.1.3.2 D1958A the mutant shows 2.5fold reduced activity compared to the wild type enzyme Homo sapiens
2.1.3.2 E1954A the mutant shows 4fold reduced activity compared to the wild type enzyme Homo sapiens
2.1.3.2 R2024Q the mutation virtually inactivates the enzyme, reducing the activity about 1000fold Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.1.3.2 N-phosphonacetyl-L-aspartate
-
 Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.3.2 carbamoyl phosphate + L-aspartate Homo sapiens
-
 phosphate + N-carbamoyl-L-aspartate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.1.3.2 Homo sapiens P27708
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.3.2 HiTrap heparin column chromatography Homo sapiens

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
2.1.3.2 homotrimer
-
 Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
2.1.3.2 ATCase
-
 Homo sapiens
2.1.3.2 CAD multienzymatic protein with three functional domains: glutamine-dependent carbamoyl phosphate synthetase, aspartate transcarbamoylase and dihydroorotase Homo sapiens