EC Number |
Reference |
---|
3.5.4.2 | modeling of structure reveals (beta/alpha)8 barrel and amino acids H15, H17, H214, D295, E217 and H238 involved in catalytic mechanism |
669825 |
3.5.4.2 | molecular docking studies. Substrate adenine is unable to properly orient in the active site in the C127A and C127S mutant structures due to distinct differences in active site conformation and rotation of residue D261 |
755347 |
3.5.4.2 | the three-dimensional structure of adenine deaminase from Agrobacterium tumefaciens (Atu4426) is determined by X-ray crystallography at 2.2 A resolution |
718893 |
3.5.4.2 | X-ray structures of Pa0148 (Pseudomonas aeruginos) and AAur1117 (Arthrobacter aurescens) are determined and reveal nearly identical distorted (beta/alpha)8 barrels with a single zinc ion that is characteristic of members of the amidohydrolase superfamily |
718906 |