Ads
related to: is zinc a coenzyme function in bacteria lab- What's Inside Centrum?
Find Out What Key Nutrients Are In
Centrum. Learn More!
- Centrum Silver on Walmart
Buy Centrum Silver for Adults
On Walmart and Support Brain Health
- Buy Men's MultiGummies
With More Vitamin D3 Than Any Other
Leading Gummy. Try It & Save Today!
- Free Menopause Guide
Take Our Quiz for Free Personalized
Menopause Advice for Your Symptoms.
- What's Inside Centrum?
Search results
Results From The WOW.Com Content Network
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.
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 .
The main alcohol dehydrogenase in yeast is larger than the human one, consisting of four rather than just two subunits. It also contains zinc at its catalytic site. Together with the zinc-containing alcohol dehydrogenases of animals and humans, these enzymes from yeasts and many bacteria form the family of "long-chain"-alcohol dehydrogenases.
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]
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.
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]