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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 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).
In molecular biology, zinc-dependent phospholipases C is a family of bacterial phospholipases C enzymes, some of which are also known as alpha toxins.. Bacillus cereus contains a monomeric phospholipase C EC 3.1.4.3 (PLC) of 245 amino-acid residues.
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 ]
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]
Re-ingestion allows for absorption of nutrients made available by bacterial fermentation, and also of vitamins and other nutrients synthesized by the gut bacteria, including vitamin B 12. [ 74 ] Non-ruminant, non-hindgut herbivores may have an enlarged forestomach and/or small intestine to provide a place for bacterial fermentation and B ...
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 domain was originally discovered in the bacterial stress response to cadmium. Further studies have found that it binds to cadmium, zinc, nickel, and mercury, but not other common metals such as cobalt, copper, iron, and manganese. [1] [6] It may have a secondary function in managing heavy-metal toxicity. [7]