peptidase


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Related to peptidase: signal peptidase

peptidase

 [pep´tĭ-dās]
any of a subclass of proteolytic enzymes that catalyze the hydrolysis of peptide linkages.

pep·ti·dase

(pep'ti-dās),
Any enzyme capable of hydrolyzing a peptide bond of a peptide, for example, carboxypeptidases, aminopeptidases.
Synonym(s): peptide hydrolase

peptidase

/pep·ti·dase/ (pep´tĭ-dās) any of a subclass of proteolytic enzymes that catalyze the hydrolysis of peptide linkages; it comprises the exopeptidases and endopeptidases.

peptidase

(pĕp′tĭ-dās′, -dāz′)
n.

peptidase

[pep′tidās]
Etymology: Gk, peptein, to digest, ase, enzyme suffix
a protein-splitting enzyme that breaks peptides into amino acids. It occurs naturally in plants, yeasts, certain microorganisms, and digestive juices.

pep·ti·dase

(pep'ti-dās)
Any enzyme capable of hydrolyzing one of the peptide links of a peptide (e.g., carboxypeptidases, aminopeptidases).

peptidase

An enzyme that hydrolyses (see HYDROLYSIS) protein fragments (PEPTIDES), breaking them down to AMINO ACIDS.

peptidase

an enzyme present in PANCREATIC JUICE that releases free AMINO ACIDS from POLYPEPTIDE CHAINS. EXOPEPTIDASES split off terminal amino acids, whereas ENDOPEPTIDASES split links within the chain.

peptidase

any of a subclass of proteolytic enzymes that catalyze the hydrolysis of peptide linkages.
References in periodicals archive ?
All levels of hainanmycin addition had no effect on peptidase activities, which indicated that hainanmycin supplementation failed to affect degradation of peptides to amino acids.
Serine and Threonine Peptidases Introduction / Clan PA subclan S
These genes code for peptidases, which normally chew up proteins (polypeptides) and lack the ability to recognize anything else.
The KLK8 peptidase is present in numerous human tissues (10) and is involved in several physiological and pathologic processes (11, 12).
In experiments in rats' small intestines, the scientists determined that a peptidase enzyme from the bacterium Flavobacterium meningosepticum rapidly breaks down the peptide.
Without this pretreatment, inhibitor preparations had substantial endogenous peptidase activity for trypsin and thrombin substrates.
The active comparators in the studies were insulin, a sulphonylurea (SU), a thiazolidinedione (TZD), and a dipeptidyl peptidase four inhibitor (DPP-4).
Cyt-1010 is a chemically stabilized and peptidase resistant analog of endomorphin-1, is highly mu-selective, showing very poor affinity for delta and kappa opioid receptors.
The recent realization that the CLN2 protein is identical to the lysosomal enzyme tripeptidyl peptidase I (TPP-I) (10-12) should simplify detection of CLN2 deficiencies because this assay is simpler and uses a commercially available substrate.