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Enzyme induction is a process in which a molecule (e.g., a drug) induces (i.e., initiates or enhances) the expression of an enzyme. The induction of heat shock proteins in the fruit fly Drosophila melanogaster. The Lac operon is an interesting example of how gene expression can be regulated.
Recent studies [citation needed] have shown that the manipulation of pectinesterase expression can influence numerous physiological processes. In plants, pectinesterase plays a role in the modulation of cell wall mechanical stability during fruit ripening, cell wall extension during pollen germination and pollen tube growth, abscission, stem elongation, tuber yield and root development.
In prokaryotes, the term corepressor is used to denote the activating ligand of a repressor protein. For example, the E. coli tryptophan repressor (TrpR) is only able to bind to DNA and repress transcription of the trp operon when its corepressor tryptophan is bound to it.
Some examples of this include producing the mRNA that encode enzymes to adapt to a change in a food source, producing the gene products involved in cell cycle specific activities, and producing the gene products responsible for cellular differentiation in multicellular eukaryotes, as studied in evolutionary developmental biology.
The L-arabinose operon houses genes coding for arabinose-digesting enzymes. These function to break down arabinose as an alternative source for energy when glucose is low or absent. [ 4 ] The operon consists of a regulatory repressor gene (araC), three control sites (ara02, ara01, araI1, and araI2), two promoters (Parac/ParaBAD) and three ...
Pectinase enzymes used today are naturally produced by fungi and yeasts (50%), insects, bacteria and microbes (35%) and various plants (15%), [4] but cannot be synthesized by animal or human cells. [5] In plants, pectinase enzymes hydrolyze pectin that is found in the cell wall, allowing for new growth and changes to be made.
The first plant phytase was found in 1907 from rice bran [3] [4] and in 1908 from an animal (calf's liver and blood). [4] [5] In 1962 began the first attempt at commercializing phytases for animal feed nutrition enhancing purposes when International Minerals & Chemicals (IMC) studied over 2000 microorganisms to find the most suitable ones for phytase production.
The enzyme's reaction pathway contains binding to the substrate and active site, splitting of glycosidic bonds, unsaturated products forming, and product release. Pectin lyase is crucial to decaying plant materials and is commonly used in the food industry and biotechnology.