Crystallization (Comment) | Organism |
---|---|
structure of apo and holo-Ast C and of the enzyme complexed with its physiological substrate, succinylornithine, to 2.2-2.75 A resolution. Docking studies support that AstC has a strong preference for acylated ornithine species over ornithine itself, and suggest that the increase in specificity associated with acylation is caused by steric and desolvation effects rather than specific interactions between the substrate and enzyme | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.284 | - |
N2-succinyl-L-ornithine | pH 8.0, temperature not specified in the publication | Escherichia coli | |
0.338 | - |
N2-Acetyl-L-ornithine | pH 8.0, temperature not specified in the publication | Escherichia coli | |
4.391 | - |
L-ornithine | pH 8.0, temperature not specified in the publication | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | A0A140N9B6 | - |
- |
Escherichia coli BL21-DE3 | A0A140N9B6 | - |
- |
Renatured (Comment) | Organism |
---|---|
the holo-enzyme can be reconstituted by the addition of pyridoxal 5'-phosphate to the apo-protein. The reconstituted enzyme is more heat stable than the apo-protein | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-ornithine + 2-oxoglutarate | - |
Escherichia coli | L-glutamate 5-semialdehyde + L-glutamate | - |
? | |
L-ornithine + 2-oxoglutarate | - |
Escherichia coli BL21-DE3 | L-glutamate 5-semialdehyde + L-glutamate | - |
? | |
N2-acetyl-L-ornithine + 2-oxoglutarate | - |
Escherichia coli | N-acetyl-L-glutamate 5-semialdehyde + L-glutamate | - |
? | |
N2-acetyl-L-ornithine + 2-oxoglutarate | - |
Escherichia coli BL21-DE3 | N-acetyl-L-glutamate 5-semialdehyde + L-glutamate | - |
? | |
N2-succinyl-L-ornithine + 2-oxoglutarate | - |
Escherichia coli | N-succinyl-L-glutamate 5-semialdehyde + L-glutamate | - |
? | |
N2-succinyl-L-ornithine + 2-oxoglutarate | - |
Escherichia coli BL21-DE3 | N-succinyl-L-glutamate 5-semialdehyde + L-glutamate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
AstC | - |
Escherichia coli |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
43.5 | - |
apo-protein | Escherichia coli |
46 | - |
enzyme reconstituetd from apo-protein | Escherichia coli |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
3 | - |
N2-succinyl-L-ornithine | pH 8.0, temperature not specified in the publication | Escherichia coli | |
3.5 | - |
L-ornithine | pH 8.0, temperature not specified in the publication | Escherichia coli | |
4.7 | - |
N2-Acetyl-L-ornithine | pH 8.0, temperature not specified in the publication | Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyridoxal 5'-phosphate | - |
Escherichia coli |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.8 | - |
L-ornithine | pH 8.0, temperature not specified in the publication | Escherichia coli | |
10.56 | - |
N2-succinyl-L-ornithine | pH 8.0, temperature not specified in the publication | Escherichia coli | |
13.9 | - |
N2-Acetyl-L-ornithine | pH 8.0, temperature not specified in the publication | Escherichia coli |