EC Number |
Reaction |
Reference |
---|
3.5.3.6 | L-arginine + H2O = L-citrulline + NH3 |
catalytic mechanism, active site residues Asp160, Glu212, His268, and Asp270 are highly conserved and crucial for activity |
689924 |
3.5.3.6 | L-arginine + H2O = L-citrulline + NH3 |
catalytic mechanism, substrate binding mode |
652524 |
3.5.3.6 | L-arginine + H2O = L-citrulline + NH3 |
chemical mechanism for ADI catalysis involves initial formation and subsequent hydrolysis of a Cys-alkylthiouronium ion intermediate, PaADI employs an active site Cys in nucleophilic catalysis |
687300 |
3.5.3.6 | L-arginine + H2O = L-citrulline + NH3 |
Cys406, His278, Asp280, and Asp166 residues form the catalytic motif, function of Cys406 in nucleophilic catalysis, detailed reaction mechanism and enzyme-intermediate structures, substrate-induced fit in ADI catalysis, overview |
680632 |
3.5.3.6 | L-arginine + H2O = L-citrulline + NH3 |
mechanism, nucleophilic catalysis |
651600 |
3.5.3.6 | L-arginine + H2O = L-citrulline + NH3 |
mechanistic study |
209450 |
3.5.3.6 | L-arginine + H2O = L-citrulline + NH3 |
residues Cys406, His278, and Asp166 and the contribution from the neighboring Asp280 are important in catalysis of the formation and hydrolysis of the Cys406-alkyluronium intermediate, structure and kinetic analysis |
664123 |
3.5.3.6 | L-arginine + H2O = L-citrulline + NH3 |
substrate binding and catalytic mechanism |
653916 |
3.5.3.6 | L-arginine + H2O = L-citrulline + NH3 |
the catalytic triad is formed by Cys398, His269, and Glu213, active site and substrate binding structure, six-step reaction mechanism with two key reaction intermediates, Cys398 is responsible for the nucleophilic attack, His269 is the proton acceptor |
685929 |
3.5.3.6 | L-arginine + H2O = L-citrulline + NH3 |
the catalytic triad is formed by Cys406, His278, and Glu224, active site and substrate binding structure, reaction mechanism with Cys406 being the key residue for the nucleophilic attack, and His278 as general base in the proton transfer chain |
685929 |