Function and mechanism of zinc metalloenzymes.

Article Details

Citation

Copy to clipboard

McCall KA, Huang C, Fierke CA

Function and mechanism of zinc metalloenzymes.

J Nutr. 2000 May;130(5S Suppl):1437S-46S.

PubMed ID

10801957 [ View in PubMed

]

Abstract

Zinc is required for the activity of > 300 enzymes, covering all six classes of enzymes. Zinc binding sites in proteins are often distorted tetrahedral or trigonal bipyramidal geometry, made up of the sulfur of cysteine, the nitrogen of histidine or the oxygen of aspartate and glutamate, or a combination. Zinc in proteins can either participate directly in chemical catalysis or be important for maintaining protein structure and stability. In all catalytic sites, the zinc ion functions as a Lewis acid. Researchers in our laboratory are dissecting the determinants of molecular recognition and catalysis in the zinc-binding site of carbonic anhydrase. These studies demonstrate that the chemical nature of the direct ligands and the structure of the surrounding hydrogen bond network are crucial for both the activity of carbonic anhydrase and the metal ion affinity of the zinc-binding site. An understanding of naturally occurring zinc-binding sites will aid in creating de novo zinc-binding proteins and in designing new metal sites in existing proteins for novel purposes such as to serve as metal ion biosensors.

DrugBank Data that Cites this Article

Drugs

Zinc

Zinc acetate

Drug Enzymes

Drug	Enzyme	Kind	Organism	Pharmacological Action	Actions
Zinc	Carbonic anhydrase 1	Protein	Humans	Unknown	Substrate	Details
Zinc acetate	Carbonic anhydrase 1	Protein	Humans	Unknown	Ligand	Details
Zinc chloride	Carbonic anhydrase 2	Protein	Humans	Unknown	Cofactor	Details
Zinc sulfate, unspecified form	Carbonic anhydrase 2	Protein	Humans	Unknown	Cofactor	Details