Cloned (Comment) | Organism |
---|---|
gene argF | Thermus thermophilus |
Crystallization (Comment) | Organism |
---|---|
purified enzyme, sitting drop vapor diffusion method, mixing of 0.001 ml of protein in 20 mM Tris-HCl, pH 8.0, and 200 mM NaCl, with 0.001 ml of well solution containing 10% PEG 4000, 0.1 M NaCl, 0.1 M HEPES-Na, pH 7.5, 20°C, 1 week, X-ray diffraction structure determination and analysis at 2.0 A resolution, modeling | Thermus thermophilus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
carbamoyl phosphate + L-ornithine | Thermus thermophilus | - |
phosphate + L-citrulline | - |
? | |
carbamoyl phosphate + L-ornithine | Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | - |
phosphate + L-citrulline | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermus thermophilus | Q5SJ15 | gene argF | - |
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | Q5SJ15 | gene argF | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
carbamoyl phosphate + L-ornithine | - |
Thermus thermophilus | phosphate + L-citrulline | - |
? | |
carbamoyl phosphate + L-ornithine | - |
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | phosphate + L-citrulline | - |
? | |
additional information | both substrates are unable to bind in a proper orientation in the active site pocket and this can be due to the differently oriented side chains. This suggests that the active site geometry should also undergo fine tuning besides the large structural changes as the enzyme switches from completely open to a substrate bound closed state | Thermus thermophilus | ? | - |
? | |
additional information | both substrates are unable to bind in a proper orientation in the active site pocket and this can be due to the differently oriented side chains. This suggests that the active site geometry should also undergo fine tuning besides the large structural changes as the enzyme switches from completely open to a substrate bound closed state | Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
aTtOTCase | - |
Thermus thermophilus |
ornithine transcarbamylase | - |
Thermus thermophilus |
otcase | - |
Thermus thermophilus |
General Information | Comment | Organism |
---|---|---|
additional information | the putative L-ornithine binding residues in aTtOTCase are Asn164, Asn165, Asp220, Ser224 and Met225. The active site geometry of the enzyme is unique among its homologs where the side chain of certain residues (Leu57, Arg58 and Arg288) is oriented differently, substrate binding in the enzyme, docking of carbamoyl phosphate (CP) and ornithine, structure analysis, overview | Thermus thermophilus |