Abstract
Creatininase from Pseudomonas putida is a member of the urease-related amidohydrolase superfamily.The crystal structures of Mn-activated creatininase, Mn-activated creatininasecreatine complex, and native creatininase have been determined. We found the cloverleafshaped creatininase hexamer to be roughly 100 Å in diameter and 50 Å in thickness and arranged as a trimer of dimers with 32 (D3) point group symmetry. Based on the high-resolution crystal structure of the creatininase-creative complex, we propose a new two-step catalytic mechanism possibly common to creatininases.
