carboxypeptidase

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Related to Carboxypeptidases: Carboxypeptidase B

carboxypeptidase

 [kahr-bok″se-pep´tĭ-dās]
an exopeptidase that acts only on the peptide linkage of a terminal amino acid containing a free carboxyl group.

car·box·y·pep·ti·dase

(kar-bok'sē-pep'ti-dās),
A hydrolase that removes the amino acid at the free carboxyl end of a polypeptide chain; an exopeptidase.

carboxypeptidase

/car·boxy·pep·ti·dase/ (-pep´tĭ-dās) any exopeptidase that catalyzes the hydrolytic cleavage of the terminal or penultimate bond at the end of a peptide or polypeptide where the free carboxyl group occurs.

carboxypeptidase

(kär-bŏk′sē-pĕp′tĭ-dās′, -dāz′)
n.
Any of several enzymes that catalyze the hydrolysis of the terminal amino acid of a polypeptide from the end that contains a free carboxyl group.

carboxypeptidase

Any enzyme (EC 3.4.16 to EC 3.4.18) which hydrolyses (cleaves) the peptide bond of the COOH terminal amino acid from a peptide; carboxypeptidase A removes aromatic or branched hydrocarbons, while carboxypeptidase B removes positively charged terminal lysine or arginine amino acid residues.

car·box·y·pep·ti·dase

(kahr-bok'sē-pep'ti-dās)
A hydrolase that removes the amino acid at the free carboxyl end of a polypeptide chain; an exopeptidase.

carboxypeptidase

an exopeptidase that catalyses the hydrolysis of amino acids in polypeptide chains from the C-terminal.

carboxypeptidase (kärbok´sēpep´-tidās),

n an exopeptidase that stimulates the hydrolytic cleavage of the last or second to last peptide bond at the C-terminal end of a peptide or polypeptide.

carboxypeptidase

an exopeptidase enzyme secreted by the pancreas that acts only on the peptide linkage of a terminal amino acid containing a free carboxyl group; includes carboxypeptidases A and B.
References in periodicals archive ?
Aspartic protease, [beta]-galactosidase, peroxidase and serine carboxypeptidase were detected in three Ephedra species.
beta]-D-xylosidase and [beta]-galactosidase, and a serine carboxypeptidase.
Ephedra monosperma had mostly degradome proteins (profilins, desiccation-related protein, the GTP-binding protein RAN-1, and ceramidase) and had only two secretome proteins that we could detect in this initial comparative study--serine carboxypeptidase and glucan endo-1,3-[beta]-glucosidase.
Furthermore, amidation of the C-terminus is not sufficient to suppress any carboxypeptidase activity (28).
Comparison of dipeptidyl carboxypeptidase and endopeptidase activities in the three enkephalin-hydrolysing metallopeptidases: "angiotensin-converting enzyme," thermolysin and "enkephalinase.
18 g/L bovine carboxypeptidase A (CpA) and incubated the fibrinogen solution overnight at room temperature (9).
CpA, the major carboxypeptidase produced by the pancreas, preferentially cleaves uncharged C-terminal residues (17); however, a number of CpAs with slightly different specificities have recently been identified in several mammalian species (18).
Determination of the activity of carboxypeptidase A in the blood of healthy human adults.
A kinetic spectrophotometric method for the determination of basic carboxypeptidases was described using furyl-acrolyl peptides (42).
The intrinsic threshold of the fibrinolytic system is modulated by basic carboxypeptidases, but the magnitude of the antifibrinolytic effect of activated thrombin activable fibrinolyis inhibitor is masked by its instability.
Basic carboxypeptidases are a group of enzymes that cleave a single basic amino acid, lysine or arginine, from the COOH terminus of peptides and proteins.
Plasma carboxypeptidases as regulators of the plasminogen system.