EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.1.3.2 | carbamoyl phosphate + L-aspartate | Thermus thermophilus | - |
phosphate + N-carbamoyl-L-aspartate | - |
? | |
2.1.3.2 | carbamoyl phosphate + L-aspartate | Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | - |
phosphate + N-carbamoyl-L-aspartate | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.1.3.2 | Thermus thermophilus | Q5SK66 | - |
- |
2.1.3.2 | Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | Q5SK66 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.1.3.2 | carbamoyl phosphate + L-aspartate | - |
Thermus thermophilus | phosphate + N-carbamoyl-L-aspartate | - |
? | |
2.1.3.2 | carbamoyl phosphate + L-aspartate | - |
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | phosphate + N-carbamoyl-L-aspartate | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.1.3.2 | aspartate trans carbamoylase | - |
Thermus thermophilus |
2.1.3.2 | ATCase | - |
Thermus thermophilus |
EC Number | General Information | Comment | Organism |
---|---|---|---|
2.1.3.2 | 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 |