protease

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endopeptidase

 [en″do-pep´tĭ-dās]
any peptidase that catalyzes the cleavage of internal bonds in a polypeptide or protein. Inhibition of the action of endopeptidases (proteases) in viruses causes formation of noninfectious particles; certain antiviral drugs work in this way (see protease inhibitors). Called also protease and proteinase.

pro·te·ase

(prō'tē-āz),
Descriptive term for proteolytic enzymes, both endopeptidases and exopeptidases; enzymes that hydrolyze (break) polypeptide chains.

protease

(prō′tē-ās′, -āz′)
n.
Any of various enzymes, including the endopeptidases and exopeptidases, that catalyze the hydrolytic breakdown of proteins. Also called peptidase.

pro·te·ase

(prō'tē-ās)
Descriptive term for proteolytic enzymes, both endopeptidases and exopeptidases; enzymes that hydrolyze (i.e., break) polypeptide chains.

protease

One of a range of protein-splitting enzymes. One focus of current interest in proteases is in their role in breaking down tissue barriers in the spread of cancer. High concentrations of the activator of one of these proteases has been found to be associated with a poor outlook in cancers of the colon and rectum.

protease

any enzyme that splits proteins, such as PEPSIN, TRYPSIN, EREPSIN or RENNIN.
References in periodicals archive ?
However, DDI family proteins contain a retroviral protease-like (RVP) domain that exhibits a structure that closely resembles that of HIV protease-1, suggesting that DDI proteins are aspartic proteases. (59-61) In fact, a mutation in the protease active site of DDI2 decreased the production of the ~110 kDa processed form of Nrf1, whereas the ~120 kDa full-length form of Nrf1 accumulated.
Aspartic protease is found in molds and yeasts, but rarely in bacteria [6].
glabrata pathogenesis, showing that aspartic protease, esterase, phytase, hemolysin, and catalase are present in strains from clinical origin.
Substrate and inhibitor profile of BACE (R-secretase) and comparison with other mammalian aspartic proteases. J Biol Chem 2002;277:4687-93.
(2003) Two distinct types of aspartic proteases from the filarial parasite Brugia malayi: molecular cloning and tissue distribution.
Cloning of cDNA for mosquito lysosomal aspartic protease. Sequence analysis of an insect lysosomal enzyme similar to cathepsins D and E.
In the case of insects, the most common digestive proteases have been classified based on their specificity, catalytic mechanism, optimum pH and sensitivity to chemical inhibitors, defining several groups that include serine proteases, cysteine proteases, aspartic proteases and metalloproteases which are widely distributed amongst insects (Terra 1990; Terra and Ferreira 1994).
Secreted aspartic proteases of Candida albicans, Candida tropicalis, Candida parapsilosis and Candida lusitaniae.
The digestive fluid of the coffee berry borer, Hypothenemus hampei, larvae contains aspartic proteases, which show greatest activity at pH 3.0 and a temperature of 40[degrees]C.