Peptidase


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peptidase

[′pep·tə‚dās]
(biochemistry)
An enzyme that catalyzes the hydrolysis of peptides to amino acids.

Peptidase

 

any one of a group of enzymes of the hydrolase class. Peptidases split off one amino acid at a time from either the carboxylic or the aminic end of protein and peptide molecules. Accordingly, they are classed as either carboxypeptidases or aminopeptidases. Dipeptidases hydrolyze dipeptides.

References in periodicals archive ?
Dipeptidyl peptidase 4 inhibitor sitagliptin protects endothelial function in hypertension through a glucagon-like peptide 1-dependent mechanism.
Kraemer-Aguiar, "Dipeptidyl peptidase 4: a new link between diabetes mellitus and atherosclerosis?" BioMed Research International, vol.
To identify the class of peptidases present in the gastric fluid of American lobster and its role in the hydrolysis of each substrate, inhibition assays were done using the specific serine, cysteine, and aspartic peptidase inhibitors (Pefabloc, E-64, and Pepstatin A, respectively) combined with the enzyme solution.
This investigation aimed to investigate the fundamental mechanism of ATP hydrolysis by Escherichia coli caseinolytic peptidase B (ClpB), an enzyme that may be capable of preventing neurodegeneration, by determining its steady-state ATP-dependent maximum initial velocity, Michaelis constant, and catalytic constant.
Demuth et al., "Long-term treatment with the dipeptidyl peptidase IV inhibitor P32/98 causes sustained improvements in glucose tolerance, insulin sensitivity, hyperinsulinemia, and [beta]-cell glucose responsiveness in VDF (fa/fa) Zucker rats," Diabetes, vol.
(v) Studies on the gene structures and function of pepsinogens: the first determination of the structure of an aspartic peptidase gene.
Proteinase, peptidase, and deaminase activities were measured by using mixed ruminal bacteria from fermentation fluid after 24 h incubation, prepared by straining and centrifuging at 200 g for 15 min in order to remove ciliate protozoa.
These nine articles describe some of the work being done to differentiate markers and use their presence to detect and treat a range of cancers, addressing the characterization of breast cancer subtypes in a large retrospective study, intraocular lymphoma markers, polymorphisms in genes associated with certain T-cell lymphomas, tumor antigens that are markers of minimal residual disease in acute myeloid leukemia, thyroid tumor markers, activity and expression of dipeptidyl peptidase IV and cathepsin H in human cutaneous melanoma compared to other common cancers, melanoma inhibitory activity as a serological marker in metastic melanoma, and the promise (or myth) of the tumor necrosis factor alpha receptors p55 and p75 in ovarian cancer detection.
Januvia does this by blocking an enzyme (dipeptidyl peptidase IV or DPP-IV) which breaks down these proteins, leading to better blood sugar control.
Both compounds inhibit an enzyme called dipeptidyl peptidase 4 (DPP-4), which usually controls the body's production of a hormone, called GLP1.