Binuclear metallohydrolases

Article Abstract:

Metallohydrolases with two metal atoms held together by bridging ligands have peptidase or phosphoesterase activity. These include enzymes that catalyze the hydrolysis of the C-N bond of urea and guanidine, the N-terminal peptide bond of proteins and the P-O bond of phosphate monoesters. The peptidase hydrolytic activity involves a nucleophilic attack on the carbonyl carbon, whereas in phosphatases the nucleophilic attack occurs at the phosphorous atom opposite the leaving group. Binuclear metallohydrolases contain a metal-bound solvent nucleophile.

Proteases, Phosphatases

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Manganese enzymes with binuclear active sites

Article Abstract:

The binuclear metal centers in enzymes containing manganese share a common bridging ligand derived from a solvent, protein, nucleoside or an amino acid residue. The metal centers exhibit electronic coupling between the metals. The bonds are either covalent or ionic that are formed through ligands or via direct metal-metal forces. The enzymes activate the substrate for oxidation, reduction or deprotonation; ionize water molecules; and stabilize the transition state of the intermediate.

Binding sites (Biochemistry), Active sites (Biochemistry)

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The catalytic mechanisms of binuclear metallohydrolases

Article Abstract:

Four specific binuclear metallohydrolases, which are experimentally well-developed systems showing the geometric and electronic structures of active sites and transition states for these binuclear metal centers are highlighted. The discussion presented on binuclear metallohydrolases illustrates both mechanistic similarities and functional variations.

Electric properties, Catalysis, Hydrolases, Structure

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