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.
Miller-Keane Encyclopedia and Dictionary of Medicine, Nursing, and Allied Health, Seventh Edition. © 2003 by Saunders, an imprint of Elsevier, Inc. All rights reserved.

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.
Farlex Partner Medical Dictionary © Farlex 2012

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.
The American Heritage® Medical Dictionary Copyright © 2007, 2004 by Houghton Mifflin Company. Published by Houghton Mifflin Company. All rights reserved.

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.
Segen's Medical Dictionary. © 2012 Farlex, Inc. All rights reserved.

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.
Medical Dictionary for the Health Professions and Nursing © Farlex 2012

carboxypeptidase

an exopeptidase that catalyses the hydrolysis of amino acids in polypeptide chains from the C-terminal.
Collins Dictionary of Biology, 3rd ed. © W. G. Hale, V. A. Saunders, J. P. Margham 2005
References in periodicals archive ?
Pshezhetsky, "Lysosomal carboxypeptidase A," in Handbook of Proteolytic Enzymes, vol.
Ephedra foeminea drops had a probable defense protein (chitinase), two carbohydrate-modifying enzymes ([beta]-xylosidase, glycosyl-hydrolase-like protein), and proteases (aspartic protease, serine carboxypeptidase).
The inactive forms of chymotrypsin, carboxypeptidases, and other peptidases are activated by trypsin.
The use of a non-specific technique (Walter, 1984) at a neutral and basic pH enables the quantification of activities of different proteases, such as trypsin, chymotrypsin, carboxypeptidases, aminopeptidases, elastases and collagenases as the main proteases that acts together as reported in several fish species (Torrissen, 1987; Klomklao, 2008; Unajak et al, 2012).
Many preformed mediators are involved in an anaphylactic reaction, including histamine, tryptase, chymase, mast cell carboxypeptidases, platelet activating factor and others.
The amidation of the carboxy terminus has been reported to protect against carboxypeptidases (26), and exoprotease resistance was characteristic to designated "second-generation" reporter peptides (Table 1).
Carboxypeptidases from A to Z: implications in embryonic development and Wnt binding.
The proteolytic processing of peptides in the circulation by amino- and carboxypeptidases is well known, and it should not be surprising that the identified molecules represent modified and/or truncated forms of C3a.
A kinetic spectrophotometric method for the determination of basic carboxypeptidases was described using furyl-acrolyl peptides (42).
C3a is very short lived and in serum is cleaved immediately into the more stable [C3a.sub.desArg] (8.9 kDa) by carboxypeptidases (9).
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.