metalloenzymes

metalloenzymes

[mə‚tal·ō ′en‚zīmz]
(biochemistry)
Metalloproteins that catalyze important cellular reactions.
References in periodicals archive ?
(Forge), a biotechnology company developing novel medicines targeting metalloenzymes, announced today that the United States Patent and Trademark Office (USPTO) has issued a notice of allowance for its patent application directed to compositions of matter and methods of use of certain 'non-hydroxamate' inhibitors of LpxC for the treatment of Gram-negative bacterial infections.
According to Forge, its BLACKSMITH comprises a deep knowledge of metalloenzymes, bioinorganic and medicinal chemistry know-how and a focused library of proprietary metal-binding fragment pharmacophores (MBPs) that provide selective and diverse starting points for novel inhibitors.
As far as structure of alpha amylases are concerned, these metalloenzymes exhibit great structural resemblance with each other.
Most metalloenzymes are highly specific for their cognate metal, exhibiting reduced or abrogated activity when loaded with alternative metal ions.
The increased hematological indices could be due to higher ceruloplasmin and cytochrome oxidase activity, (the copper containing metalloenzymes) in bone marrow of these calves.
Metal salt is found to be inactive against these enzymes, which demonstrates the different interactions of metal and its complexes with metalloenzymes.
The element functions mainly as a divalent cation in metalloenzymes and among these functions is the linkage of these enzymes to their corresponding substrates.
Zinc is an essential trace element involved in many physiological functions, including catalytic and structural roles in metalloenzymes, as well as regulatory roles in diverse cellular processes, such as synaptic signaling and gene expression.
Nature is widely known to be a source of efficient catalysts: the enzymes and metalloenzymes, which are natural machines that can be esteemed for performing extremely difficult chemical processes with elegant selectivity, fast rates, and low activation energies.
Class A, C, and D enzymes all possess an active site serine, whereas class B [beta]-lactamases are metalloenzymes with a [Zn.sup.2+] ion(s) in the active site [26].
Keltjens, "Metal enzymes in "impossible" microorganisms catalyzing the anaerobic oxidation of ammonium and methane," in Sustaining Life on Planet Earth: Metalloenzymes Mastering Dioxygen and Other Chewy Gases, P.
Zn and Cu are required to maintain a proper immune response and antioxidant protection in the body as they are the cofactors of metalloenzymes [17, 18].