Information om | Engelska ordet HYDROLASE

Exempel på hur man kan använda HYDROLASE i en mening

• GTPases are a large family of hydrolase enzymes that bind to the nucleotide guanosine triphosphate (GTP) and hydrolyze it to guanosine diphosphate (GDP).
• They are a type of G-protein found in the cytosol that are homologous to the alpha subunit of heterotrimeric G-proteins, but unlike the alpha subunit of G proteins, a small GTPase can function independently as a hydrolase enzyme to bind to and hydrolyze a guanosine triphosphate (GTP) to form guanosine diphosphate (GDP).
• C-type lysozymes are closely related to α-lactalbumin in sequence and structure, making them part of the same glycoside hydrolase family 22.
• Some common examples of hydrolase enzymes are esterases including lipases, phosphatases, glycosidases, peptidases, and nucleosidases.
• Dipeptides are produced from polypeptides by the action of the hydrolase enzyme dipeptidyl peptidase.
• A heterozygous microdeletion in the FAAH-OUT pseudogene of the fatty acid amide hydrolase (FAAH) chromosomal region that is expressed in the brain and dorsal root ganglia together with a common hypomorphic single nucleotide polymorphism in the FAAH gene was identified as the presumptive cause of congenital analgesia in a woman named Jo Cameron.
• The catalytic triad of UCH-L1 contains a cysteine at position 90, an aspartate at position 176, and a histidine at position 161 that are responsible for its hydrolase activity.
• In more general terms, phosphorylases are enzymes that catalyze the addition of a phosphate group from an inorganic phosphate (phosphate + hydrogen) to an acceptor, not to be confused with a phosphatase (a hydrolase) or a kinase (a phosphotransferase).
• Microsomal epoxide hydrolase (epoxide hydrolase 1, EH1, or mEH), soluble epoxide hydrolase (sEH, epoxide hydrolase 2, EH2, or cytoplasmic epoxide hydrolase), and the more recently discovered but not as yet well defined functionally, epoxide hydrolase 3 (EH3) and epoxide hydrolase 4 (EH4) are structurally closely related isozymes.
• Like allolactose, IPTG binds to the lac repressor and releases the tetrameric repressor from the lac operator in an allosteric manner, thereby allowing the transcription of genes in the lac operon, such as the gene coding for beta-galactosidase, a hydrolase enzyme that catalyzes the hydrolysis of β-galactosides into monosaccharides.
• Members of the papain family are widespread, found in baculoviruses, The proteins are typically lysosomal or secreted, and proteolytic cleavage of the propeptide is required for enzyme activation, although bleomycin hydrolase is cytosolic in fungi and mammals.
• The prominent hydrolase subclass used in dephosphorylation is phosphatase, which removes phosphate groups by hydrolysing phosphoric acid monoesters into a phosphate ion and a molecule with a free hydroxyl (–OH) group.
• Toxicity of mercaptopurine can be linked to genetic polymorphisms in thiopurine S-methyltransferase (TPMT), nudix hydrolase 15 (NUDT15), and inosine triphosphate pyrophosphatase (ITPA).
• The enzyme Trehalase is a glycoside hydrolase, produced by cells in the brush border of the small intestine, which catalyzes the conversion of trehalose to glucose.
• Beside the CYP family NNK can also be activated by metabolic genes, like myeloperoxidase (MPO) and epoxide hydrolase (EPHX1).
• These contain structures from different enzyme classes, including hydrolase, transferases, kinases, reductase, oxidoreductase, lyases, and G protein-coupled receptors (GPCRs).
• His early contributions to the cannabinoid field include identification and characterization of the endocannabinoid-terminating enzyme fatty acid amide hydrolase (FAAH), as well as the isolation of the novel soporific compound oleamide from cerebrospinal fluid.
• Based on its 1,3-disubstituted urea structure, sorafenib is also a potent soluble epoxide hydrolase inhibitor and this activity likely reduces the severity of its adverse effects.
• EDP and EEQ metabolites are short-lived, being inactivated within seconds or minutes of formation by epoxide hydrolases, particularly soluble epoxide hydrolase, and therefore act locally.
• EETs are generally short-lived, being rapidly converted from epoxides to less active or inactive dihydroxy-eicosatrienoic acids (diHETrEs) by a widely distributed cellular enzyme, soluble epoxide hydrolase (sEH), also termed epoxide hydrolase 2.

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