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Literature summary for 2.1.3.2 extracted from

  • Kanagarajan, S.; Mutharasappan, N.; Dhamodharan, P.; Jeyaraman, M.; Ramadas, K.; Jeyaraman, J.
    Exploring the structural features of aspartate trans carbamoylase (TtATCase) from Thermus thermophilus HB8 through in silico approaches: a potential drug target for inborn error of pyrimidine metabolism (2014), J. Biomol. Struct. Dyn., 32, 591-601.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
carbamoyl phosphate + L-aspartate Thermus thermophilus
-
phosphate + N-carbamoyl-L-aspartate
-
?
carbamoyl phosphate + L-aspartate Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
phosphate + N-carbamoyl-L-aspartate
-
?

Organism

Organism UniProt Comment Textmining
Thermus thermophilus Q5SK66
-
-
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 Q5SK66
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
carbamoyl phosphate + L-aspartate
-
Thermus thermophilus phosphate + N-carbamoyl-L-aspartate
-
?
carbamoyl phosphate + L-aspartate
-
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 phosphate + N-carbamoyl-L-aspartate
-
?

Synonyms

Synonyms Comment Organism
aspartate trans carbamoylase
-
Thermus thermophilus
ATCase
-
Thermus thermophilus

General Information

General Information Comment Organism
additional information three-dimensional enzyme homology structure modeling using the crystal structure of ATCase from Pyrococcus abyssi, PDB ID:1ML4, molecular dynamics simulations and enzyme conformation stability, ligand binding study, overview. The residues Thr53, Arg104, and Gln219 are consistently involved in strong hydrogen-bonding interactions and play a vital role in the TtATCase activity Thermus thermophilus