Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Mycobacterium tuberculosis |
Crystallization (Comment) | Organism |
---|---|
structures complexed with CoA and product bound N-acetylglutamine and the other complexed with acetyl-CoA and the inhibitor L-arginine at 2.3 and 3.0 A resolution, respectively. The ArgA protomer has a V cleft and a beta bulge. ArgA may also acetylate L-glutamine like L-glutamate. The active site is strongly inhibited by L-arginine resulting in a closed conformation of ArgA. Both L-arginine and N-acetylglutamine occupy the same active site | Mycobacterium tuberculosis |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
L-arginine | L-arginine does not act as an allosteric inhibitor | Mycobacterium tuberculosis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mycobacterium tuberculosis | O33289 | - |
- |
Mycobacterium tuberculosis H37Rv | O33289 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
acetyl-CoA + L-glutamate | - |
Mycobacterium tuberculosis | CoA + N-acetyl-L-glutamate | - |
? | |
acetyl-CoA + L-glutamate | - |
Mycobacterium tuberculosis H37Rv | CoA + N-acetyl-L-glutamate | - |
? | |
acetyl-CoA + L-glutamine | - |
Mycobacterium tuberculosis | CoA + N-acetyl-L-glutamine | - |
? | |
acetyl-CoA + L-glutamine | - |
Mycobacterium tuberculosis H37Rv | CoA + N-acetyl-L-glutamine | - |
? |
Synonyms | Comment | Organism |
---|---|---|
ArgA | - |
Mycobacterium tuberculosis |
Rv2747 | - |
Mycobacterium tuberculosis |
IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|
0.0012 | - |
substrate L-glutamate, pH 8.0, temperature not specified in the publication | Mycobacterium tuberculosis | L-arginine | |
0.00156 | - |
substrate L-glutamine, pH 8.0, temperature not specified in the publication | Mycobacterium tuberculosis | L-arginine |