title: Metal ions in enzymes using ammonia or amides.
abstract: In an attempt to understand the role of nickel in jack bean urease (1), we turned to a variety of other enzymes important in the utilization, production, or transfer of ammonia. We found several, including the L-histidine and L-phenylalanine ammonialyases and some enzymes that utilize glutamine or ammonia in amidotransferase reactions, all of which show evidence for the involvement of as yet unreported transition metal ions in their mechanism of action. We support the view that catalysis by metalloenzymes may be a reflection of the chemistry of the metal ion itself as a Lewis acid, and that perhaps too much emphasis has been placed on supposed special characteristics (such as strains, "entasis") of the enzyme-metal ion association. In this context, we have discussed the mechanism of catalysis of hydrolysis of specific substrates by carboxypeptidase A, and have returned to urease to examine the role of nickel in its mechanism of action.
mesh_terms: D000641:Ammonia / Q000378:metabolism*; D001665:Binding Sites; D002268:Carboxypeptidases / Q000378:metabolism; D004798:Enzymes / Q000378:metabolism*; D005973:Glutamine / Q000378:metabolism; D008670:Metals / Q000378:metabolism; D009532:Nickel / Q000378:metabolism; D011766:Pyruvate Carboxylase / Q000378:metabolism; D013438:Sulfhydryl Compounds / Q000378:metabolism; D014510:Urease / Q000378:metabolism; D015032:Zinc / Q000378:metabolism
chemical_list: D004798:Enzymes; D008670:Metals; D013438:Sulfhydryl Compounds; D005973:Glutamine; D000641:Ammonia; D009532:Nickel; D002268:Carboxypeptidases; D014510:Urease; D011766:Pyruvate Carboxylase; D015032:Zinc