Search results
Results from the WOW.Com Content Network
Cofactor (biochemistry) 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 biology and biochemistry, the active site is the region of an enzyme where substrate molecules bind and undergo a chemical reaction. The active site consists of amino acid residues that form temporary bonds with the substrate, the binding site, and residues that catalyse a reaction of that substrate, the catalytic site.
A biomolecule or biological molecule is loosely defined as a molecule produced by a living organism and essential to one or more typically biological processes. [1] Biomolecules include large macromolecules such as proteins, carbohydrates, lipids, and nucleic acids, as well as small molecules such as vitamins and hormones.
An example of an enzyme that contains a cofactor is carbonic anhydrase, which uses a zinc cofactor bound as part of its active site. [58] These tightly bound ions or molecules are usually found in the active site and are involved in catalysis. [1]: 8.1.1 For example, flavin and heme cofactors are often involved in redox reactions. [1]: 17
e. Illustration of an activator. In molecular biology, a transcription factor (TF) (or sequence-specific DNA-binding factor) is a protein that controls the rate of transcription of genetic information from DNA to messenger RNA, by binding to a specific DNA sequence. [1][2] The function of TFs is to regulate—turn on and off—genes in order to ...
Cytochrome. Cytochromes are redox-active proteins containing a heme, with a central iron (Fe) atom at its core, as a cofactor. They are involved in the electron transport chain and redox catalysis. They are classified according to the type of heme and its mode of binding.
Decarboxylations are pervasive in biology. They are often classified according to the cofactors that catalyze the transformations. [11] Biotin-coupled processes effect the decarboxylation of malonyl-CoA to acetyl-CoA. Thiamine (T:) is the active component for decarboxylation of alpha-ketoacids, including pyruvate: T: + RC(O)CO 2 H → T=C(OH)R ...
In molecular biology, the Cofactor transferase family is a family of protein domains that includes biotin protein ligases, lipoate-protein ligases A, octanoyl- (acyl carrier protein):protein N-octanoyltransferases, and lipoyl-protein:protein N-lipoyltransferases. [2] The metabolism of the cofactors Biotin and lipoic acid share this family.