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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.
The protein is a member of the ferric uptake regulator family and binds zinc with high affinity. It typically functions as a repressor of zinc uptake proteins via binding to characteristic promoter DNA sequences in a dimer -of-dimers arrangement that creates strong cooperativity . [ 1 ]
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).
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.
Zinc pyrithione (or pyrithione zinc) is a coordination complex of zinc. It has fungistatic (inhibiting the division of fungal cells) and bacteriostatic (inhibiting bacterial cell division) properties and is used in the treatment of seborrhoeic dermatitis [ 2 ] and dandruff .
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.
Carboxypeptidase A, from bovine pancreas. A carboxypeptidase (EC number 3.4.16 - 3.4.18) is a protease enzyme that hydrolyzes (cleaves) a peptide bond at the carboxy-terminal (C-terminal) end of a protein or peptide.
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.