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Polyphenol oxidase is an enzyme found throughout the plant and animal kingdoms, [31] including most fruits and vegetables. [32] PPO has importance to the food industry because it catalyzes enzymatic browning when tissue is damaged from bruising, compression or indentations, making the produce less marketable and causing economic loss.
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.
Central dogma depicting transcription from DNA code to RNA code to the proteins in the second step covering the production of protein. Protein production is the biotechnological process of generating a specific protein. It is typically achieved by the manipulation of gene expression in an organism such that it expresses large amounts of a ...
Protein Kinase C (PKC) is a class of enzymes that phosphorylates proteins. Its substrates are typically on the membrane surface where the enzyme is recruited by the lipid diacylglycerol. Thus a portion of PKC activation is through substrate presentation, i.e., by localization with its substrate on the membrane.
This may happen for various reasons, for example when the plant contains low amounts of cellular water due to drought. [51] The gating of an aquaporin is carried out by an interaction between a gating mechanism and the aquaporin, which causes a 3D change in the protein so that it blocks the pore and, thus, disallows the flow of water through ...
Signaling peptides include members of the following protein families. Systemin — is a small polypeptide functioning as a long-distance signal to activate chemical defenses against herbivores. It was the first plant hormone proven to be a peptide. Systemin induces the production of protein defense compound called protease inhibitors.
A protein phosphatase is an enzyme that dephosphorylates an amino acid residue of its protein substrate. Whereas protein kinases act as signaling molecules by phosphorylating proteins, phosphatases remove the phosphate group, which is essential if the system of intracellular signaling is to be able to reset for future use.
A particular example of this process is the scaffold, A-kinase anchor proteins (AKAPs), which target cyclic AMP-dependent protein kinase to various sites in the cell. [7] This localization is able to locally regulate PKA and results in the local phosphorylation by PKA of its substrates.