Application | Comment | Organism |
---|---|---|
medicine | ornithine carbamoyltransferase is acetylated at lysine resiudes, including K88, which is also mutated in ornithine carbamoyltransferase-deficient patients. K88 acetylation decreases the affinity for carbamoyl phosphate, and the maximum velocity, whereas the Km for ornithine is not affected | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
K88Q | less than 1% of wild-type activity | Homo sapiens |
K88R | mutant retains substantial enzymatic activity | Homo sapiens |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.13 | - |
Carbamoyl phosphate | wild-type, pH 7.7, 37°C | Homo sapiens | |
0.15 | - |
Carbamoyl phosphate | mutant K88R, pH 7.7, 37°C | Homo sapiens | |
0.36 | - |
L-ornithine | wild-type, pH 7.7, 37°C | Homo sapiens | |
0.42 | - |
L-ornithine | mutant K88R, pH 7.7, 37°C | Homo sapiens | |
0.55 | - |
L-ornithine | mutant K88Q, pH 7.7, 37°C | Homo sapiens | |
1.24 | - |
Carbamoyl phosphate | mutant K88Q, pH 7.7, 37°C | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
additional information | ornithine carbamoyltransferase is acetylated at lysine residues, including K88, which is also mutated in ornithine carbamoyltransferase-deficient patients. K88 acetylation decreases the affinity for carbamoyl phosphate, and the maximum velocity, whereas the Km for ornithine is not affected. K88 acetylation is regulated by both extracellular glucose and amino acid availabilit | Homo sapiens |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
Chang liver cell | - |
Homo sapiens | - |
HEK-293T cell | - |
Homo sapiens | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
carbamoyl phosphate + L-ornithine | - |
Homo sapiens | phosphate + L-citrulline | - |
? |