EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
2.3.1.1 | arginine | - |
Homo sapiens | |
2.3.1.1 | arginine | 0.02 mM, 4.2fold activation | Rattus norvegicus | |
2.3.1.1 | Cationic polypeptides | 4fold activation | Rattus norvegicus | |
2.3.1.1 | Triton X-100 | 0.1%, 4fold activation | Rattus norvegicus |
EC Number | General Stability | Organism |
---|---|---|
2.3.1.1 | Triton X-100, 0.1%, stabilizes liver enzyme | Rattus norvegicus |
2.3.1.1 | use of silicone-treated glassware or plastic tubes, e.g. polyethylene, polycarbonate or polypropylene stabilizes the enzyme | Salmonella enterica subsp. enterica serovar Typhimurium |
2.3.1.1 | use of silicone-treated glassware or plastic tubes, e.g. polyethylene, polycarbonate or polypropylene stabilizes the enzyme | Escherichia coli |
2.3.1.1 | use of silicone-treated glassware or plastic tubes, e.g. polyethylene, polycarbonate or polypropylene stabilizes the enzyme | Homo sapiens |
2.3.1.1 | use of silicone-treated glassware or plastic tubes, e.g. polyethylene, polycarbonate or polypropylene stabilizes the enzyme | Rattus norvegicus |
2.3.1.1 | use of silicone-treated glassware or plastic tubes, e.g. polyethylene, polycarbonate or polypropylene stabilizes the enzyme | Pseudomonas aeruginosa |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
2.3.1.1 | coenzyme A | 2.5 mM, 50% inhibition | Escherichia coli | |
2.3.1.1 | coenzyme A | 1 mM, 20% inhibition | Rattus norvegicus | |
2.3.1.1 | high ionic strength | - |
Escherichia coli | |
2.3.1.1 | high ionic strength | - |
Rattus norvegicus | |
2.3.1.1 | N-acetylglutamate | - |
Escherichia coli | |
2.3.1.1 | N-acetylglutamate | 2 mM, 88% inhibition | Rattus norvegicus | |
2.3.1.1 | propionyl-CoA | - |
Rattus norvegicus |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.3.1.1 | 0.76 | - |
acetyl-CoA | - |
Rattus norvegicus | |
2.3.1.1 | 3.7 | - |
L-glutamate | - |
Rattus norvegicus | |
2.3.1.1 | 4.6 | - |
acetyl-CoA | - |
Salmonella enterica subsp. enterica serovar Typhimurium | |
2.3.1.1 | 4.7 | - |
L-glutamate | partially purified enzyme | Homo sapiens | |
2.3.1.1 | 8.1 | - |
acetyl-CoA | partially purified enzyme | Homo sapiens |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
2.3.1.1 | 57000 | - |
3 * 57000, SDS-PAGE | Rattus norvegicus |
2.3.1.1 | 160000 | - |
gel filtration, sucrose density gradient centrifugation | Rattus norvegicus |
2.3.1.1 | 190000 | - |
gel filtration | Homo sapiens |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.3.1.1 | acetyl-CoA + L-glutamate | Rattus norvegicus | - |
CoA + N-acetyl-L-glutamate | - |
? | |
2.3.1.1 | acetyl-CoA + L-glutamate | Salmonella enterica subsp. enterica serovar Typhimurium | enzyme catalyzes the first step in the biosynthesis of arginine | CoA + N-acetyl-L-glutamate | - |
? | |
2.3.1.1 | acetyl-CoA + L-glutamate | Escherichia coli | enzyme catalyzes the first step in the biosynthesis of arginine | CoA + N-acetyl-L-glutamate | - |
? | |
2.3.1.1 | acetyl-CoA + L-glutamate | Pseudomonas aeruginosa | enzyme catalyzes the first step in the biosynthesis of arginine | CoA + N-acetyl-L-glutamate | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.3.1.1 | Escherichia coli | - |
- |
- |
2.3.1.1 | Homo sapiens | - |
- |
- |
2.3.1.1 | Pseudomonas aeruginosa | - |
- |
- |
2.3.1.1 | Rattus norvegicus | - |
- |
- |
2.3.1.1 | Salmonella enterica subsp. enterica serovar Typhimurium | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.3.1.1 | ammonium sulfate, DEAE Biogel, Sephacryl S-200, aminoacetyl biogel A, affi-gel blue, sucrose gradient, isoelectric focusing | Rattus norvegicus |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
2.3.1.1 | liver | - |
Homo sapiens | - |
2.3.1.1 | liver | - |
Rattus norvegicus | - |
2.3.1.1 | small intestine | - |
Homo sapiens | - |
2.3.1.1 | small intestine | mucosa | Rattus norvegicus | - |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
2.3.1.1 | 0.000014 | - |
- |
Rattus norvegicus |
2.3.1.1 | 0.00013 | - |
- |
Salmonella enterica subsp. enterica serovar Typhimurium |
2.3.1.1 | 0.00013 | - |
- |
Escherichia coli |
2.3.1.1 | 0.000268 | - |
activity in liver of adult | Rattus norvegicus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.3.1.1 | acetyl-CoA + DL-2-aminopimelate | - |
Escherichia coli | CoA + 2-acetylaminoheptanedioate | - |
? | |
2.3.1.1 | acetyl-CoA + DL-2-aminopimelate | 5.2% of activity with L-glutamate | Rattus norvegicus | CoA + 2-acetylaminoheptanedioate | - |
? | |
2.3.1.1 | acetyl-CoA + glycine | 2.9% of activity with L-glutamate | Rattus norvegicus | CoA + acetylaminoacetate | - |
? | |
2.3.1.1 | acetyl-CoA + L-2-aminoadipate | - |
Rattus norvegicus | CoA + 2-acetylaminohexanedioate | - |
? | |
2.3.1.1 | acetyl-CoA + L-2-aminoadipate | 1.3% of activity with L-glutamate | Escherichia coli | CoA + 2-acetylaminohexanedioate | - |
? | |
2.3.1.1 | acetyl-CoA + L-glutamate | - |
Salmonella enterica subsp. enterica serovar Typhimurium | CoA + N-acetyl-L-glutamate | - |
? | |
2.3.1.1 | acetyl-CoA + L-glutamate | - |
Escherichia coli | CoA + N-acetyl-L-glutamate | - |
? | |
2.3.1.1 | acetyl-CoA + L-glutamate | - |
Homo sapiens | CoA + N-acetyl-L-glutamate | - |
? | |
2.3.1.1 | acetyl-CoA + L-glutamate | - |
Rattus norvegicus | CoA + N-acetyl-L-glutamate | - |
? | |
2.3.1.1 | acetyl-CoA + L-glutamate | - |
Pseudomonas aeruginosa | CoA + N-acetyl-L-glutamate | - |
? | |
2.3.1.1 | acetyl-CoA + L-glutamate | enzyme catalyzes the first step in the biosynthesis of arginine | Salmonella enterica subsp. enterica serovar Typhimurium | CoA + N-acetyl-L-glutamate | - |
? | |
2.3.1.1 | acetyl-CoA + L-glutamate | enzyme catalyzes the first step in the biosynthesis of arginine | Escherichia coli | CoA + N-acetyl-L-glutamate | - |
? | |
2.3.1.1 | acetyl-CoA + L-glutamate | enzyme catalyzes the first step in the biosynthesis of arginine | Pseudomonas aeruginosa | CoA + N-acetyl-L-glutamate | - |
? | |
2.3.1.1 | acetyl-CoA + L-glutamine | 5% of activity with acetyl-CoA | Escherichia coli | ? | - |
? | |
2.3.1.1 | acetyl-CoA + L-glutamine | 6.8% of activity with L-glutamate | Rattus norvegicus | ? | - |
? | |
2.3.1.1 | propionyl-CoA + L-glutamate | 4% of activity with acetyl-CoA | Escherichia coli | CoA + N-propionyl-L-glutamate | - |
? | |
2.3.1.1 | propionyl-CoA + L-glutamate | 4.3% of activity with acetyl-CoA | Rattus norvegicus | CoA + N-propionyl-L-glutamate | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.3.1.1 | trimer | 3 * 57000, SDS-PAGE | Rattus norvegicus |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.3.1.1 | 8 | - |
liver enzyme, in the absence of arginine | Rattus norvegicus |
2.3.1.1 | 8.5 | - |
- |
Rattus norvegicus |
2.3.1.1 | 8.5 | - |
liver enzyme, in the presence of arginine | Homo sapiens |
2.3.1.1 | 10 | - |
- |
Escherichia coli |
EC Number | pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|---|
2.3.1.1 | 7 | - |
highest stability | Escherichia coli |
EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.3.1.1 | 0.71 | - |
propionyl-CoA | - |
Rattus norvegicus |