European Journal of Biomedical and Pharmaceutical Sciences

ZINC METALLOENZYMES AND MODEL COMPOUNDS FOR CARBONIC ANHYDRASE: A REVIEW ARTICLE

Dr. Shalu Tyagi* and Dr. Ravindra Singh Yadav

ABSTRACT

Zinc has been demonstrated to be essential for the growth, development and differentiation of all types of life, including microorganisms, plants and animals. After iron, zinc is the second most abundant trace metal in the human body A zinc-bound water molecule rapidly exchanges, because the ligand-zinc bond is kinetically labile. These features provide an effective hydrolysis function of the zinc complex through the activation of coordinated water. Therefore, it is of particular interest to study the metabolic conversion or degradation of biomolecules catalyzed by zinc enzymes. However, the mechanistic details of the enzyme function in the protein matrix are sometimes complicated, even though the structures of many zinc enzymes can be characterized by several different spectroscopies. On the other hand, a synthetic zinc complex related to the active site sphere will be a good tool with which to understand the role of the zinc ion and the complicated mechanism of catalytic reactions. A great deal of interest focused on the design of excellent functional or structural models on zinc enzymes. In this article, several representative zinc enzymes and related functional models of carbonic anhydrase will be discussed.

Keywords: Zinc, carbonic anhydrase, metalloenzyme, zinc-binding sites, zinc enzyme, enzyme model, catalytic hydrolysis, zinc hydroxide, carboxypeptidase, carbonic anhydrase, alcohol dehydrogenase.