EC Number   |
Reaction |
Reference |
|---|
    2.3.1.35 | N2-acetyl-L-ornithine + L-glutamate = L-ornithine + N-acetyl-L-glutamate |
- |
- |
| 2.3.1.35 | N2-acetyl-L-ornithine + L-glutamate = L-ornithine + N-acetyl-L-glutamate |
residue T181 becomes acetylated and the carbonyl oxygen of the acyl-enzyme complex is located in an oxyanion hole and positioned to hydrogen bond with the backbone amide-NH of G112 and the alcohol of T111. Presence of two distinct acyl-enzyme complex structures which can interconvert by movement of the T111 side-chain alcohol hydrogen away from the oxyanion hole to hydrogen bond with the backbone carbonyl of the acylated residue, T181 |
704194 |
| 2.3.1.35 | N2-acetyl-L-ornithine + L-glutamate = L-ornithine + N-acetyl-L-glutamate |
substrate binding structure, oxyanion stabilization mechanism of the enzyme-substrate complex, the ping pong reaction mechanism involves Gly112 and Thr181, active site structure |
660991 |
