Zinc and Metalloenzymes

作者: Bert L. Vallee

DOI: 10.1016/S0065-3233(08)60108-4

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摘要: Publisher Summary The chapter discusses the zinc and metalloenzymes. Two groups of proteins that associate with metals can be differentiated. Members each group may or not possess known enzymatic activities.In one group, metalloproteins, a given metal is combined protein in unique manner, such two thought as an “entity” nature. A second which combines reversibly several different cations, metal-protein complexes, has been much more resistant to definitive appraisal. Metal-enzyme subgroup exhibit activity consequent readily dissociable combination variety ions. study complexes particularly chelates provided both new experimental theoretical backgrounds for relation specificity enzyme action, metal-enzyme, metal-substrate, metalloenzyme interaction, well nietal-enzyme inhibition. elaborates on metalloenzymes distinct characteristics, inspect analyze. characteristics bond serve primary parameter differentiation from metal-enzyme complexes. For metalloenzymes, empirical formula based molecular weight protein, ratio moles metal/moles nietal/moles coenzyme when present, expresses stoichiometric relationships components active holoenzyme another. Four metalloproteins have characterized chapter: carbonic anhydrase ox erythrocytes, zinc-containing human leukocytes, carboxypeptidase bovine pancreas, alcohol dehydrogenase yeast.

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