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Phosphatases are a class of enzymes that play a key role in the dephosphorylation of organic compounds. Using water as a reactant, phosphatase enzymes catalyze the hydrolysis of various monophosphate esters into phosphoric acid and alcohol. These enzymes are present in both prokaryotes and eukaryotes alike, and are typically classified as either acid phosphatase or alkaline phosphatase. Acidic phosphatases function optimally in acidic pH environments, whereas alkaline phosphatases are optimally active at alkaline pH environments. Together with kinases (enzymes that catalyze the addition of phosphate groups onto molecules), phosphatase enzymes direct a form a post-translational modification that is essential for normal cell biology and pathogenesis.
Dehydrogenases are family of enzymes belonging to the group oxidoreductase. These enzymes catalyze the oxidation of a substrate by transferring one or more hydrides to an electron acceptor or coenzyme. Common electron acceptors, being considered as oxidizers of the substrate are usually nicotinamide adenine dinucleotide (NAD+/NADH), nicotinamide adenine dinucleotide phosphate (NADP+/NADPH), flavin adenine dinucleotide (FAD) or flavin mononucleotide (FMN).
Horseradish peroxidase (HRP) is a popular enzyme used extensively in molecular biology for the detection of immune complexes and targets such as proteins, carbohydrates or nucleic acids. This enzyme, which is typically conjugated to antibodies, streptavidin or other proteins, functions as a reporter system for probe-based immunoassay applications including, immunohistochemistry (IHC), Western blot (WB), and enzyme-linked immunosorbent assays (ELISAs).
Kinases are a family of enzymes that catalyze the transfer of a phosphate moiety from a high-energy, phosphate-donating molecule, such as ATP, to its specific substrate. This process is referred to as phosphorylation, where the high-energy ATP molecule donates a phosphate group to the substrate, producing a phosphorylated substrate and ADP (Figure 1). Because of the high levels of energy released during the breakage of phosphoanhydride bonds, kinases are necessary to stablize this reaction.
The most versatile and common reporter gene is the luciferase of the North American firefly photinus pyralis. The protein requires no posttranslational modification for enzyme activity. It is not even toxic in high concentration (in vivo) and can be used in pro- and eukaryotic cells.
A protease is an enzyme that conducts proteolysis, i.e., the protein catabolism by hydrolysis of the peptide bonds that link amino acids together in the polypeptide chain which form the protein. Proteases, also known as peptidases or proteolytic enzymes, are a large group of enzymes. They belong to the class of enzymes known as hydrolases, which catalyse the reaction of hydrolysis of various bonds with the participation of a water molecule.
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