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Zinc fingers help read DNA sequences.. Zinc is an essential trace element for humans [1] [2] [3] and other animals, [4] for plants [5] and for microorganisms. [6] Zinc is required for the function of over 300 enzymes and 1000 transcription factors, [3] and is stored and transferred in metallothioneins.
Similarly, it has been demonstrated that zinc chelators can inhibit the hydrolytic activity of metallo-β-lactamases against β-lactam antibiotics, restoring the activity of the latter. [6] Metallo-beta-lactamases are important enzymes because they are involved in the breakdown of antibiotics by antibiotic-resistant bacteria. [7]
Most metalloproteases require zinc, but some use cobalt. The metal ion is coordinated to the protein via three ligands. The ligands coordinating the metal ion can vary with histidine, glutamate, aspartate, lysine, and arginine. [clarification needed] The fourth coordination position is taken up by a labile water molecule.
Zinc finger. The zinc ion (green) is coordinated by two histidine residues and two cysteine residues. Many transcription factors contain a structure known as a zinc finger, a structural module in which a region of protein folds around a zinc ion. The zinc does not directly contact the DNA that these proteins bind to.
The succinate dehydrogenase complex showing several cofactors, including flavin, iron–sulfur centers, and heme.. A cofactor is a non-protein chemical compound or metallic ion that is required for an enzyme's role as a catalyst (a catalyst is a substance that increases the rate of a chemical reaction).
A prosthetic group is the non-amino acid component that is part of the structure of the heteroproteins or conjugated proteins, being tightly linked to the apoprotein.. Not to be confused with the cosubstrate that binds to the enzyme apoenzyme (either a holoprotein or heteroprotein) by non-covalent binding a non-protein (non-amino acid)
The carboxypeptidase A family can be divided into two subfamilies: carboxypeptidase H (regulatory) and carboxypeptidase A (digestive). [1] Members of the H family have longer C-termini than those of family A, [2] and carboxypeptidase M (a member of the H family) is bound to the membrane by a glycosylphosphatidylinositol anchor, unlike the majority of the M14 family, which are soluble.
Pages in category "Zinc enzymes" The following 28 pages are in this category, out of 28 total. This list may not reflect recent changes. 0–9.
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