carboxypeptidase


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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 ?
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.
"In this paper we link the catalytic activity of carboxypeptidase N to tumor progression in clinical samples from breast cancer patients and a breast cancer animal model," biomedical engineer Dr Tony Hu, who led the project, (http://medicalxpress.com/news/2013-11-early-stages-breast-cancer-blood.html) said in a news release.
Angiotensin-converting enzyme (ACE, EC 3.4.15.1, dipeptidyl carboxypeptidase) is associated with the regulation of blood pressure and maintenance of salt and water homeostasis of the body [5].
(8) The thiol groups of CK are susceptible to oxidation, CK may be glycated, and it can be deactivated by the plasma enzyme carboxypeptidase N (summarised in Delanghe and De Buyzere (8)).
Results of BLAST search performed with human EGF against the non redundant mycobacterial protein database at NCBI Accession Protein Name E-Value Number NP_302390 Probable multidrug resistance pump 0.022 NP_301513 GTP-binding protein LepA 0.40 NP_301554 Putative -alanyl-D-alanine carboxypeptidase 2.2 NP_302118 heat shock protein 90 2.4 NP_302586 UDP-N-acetylenolpyruvoylglucosamine reductase 4.4 NP_301491 6-phosphogluconolactonase 6.5 NP_301739 Possible ATP/GTP-binding protein 7.8 NP_301890 Mycocerosic acid synthase 8.8 Table 3.
An intramolecularly quenched fluorescent tripeptide as a fluorogenic substrate of angiotensin-I-converting enzyme and of bacterial dipeptidyl carboxypeptidase. Eur.
Carbonic anhydrase was the first discovered zinc metalloenzyme; other enzymes include: carboxypeptidase, alkaline phosphatase, DNA/RNA polymerase and superoxide dismutase.
Tomato fruit carboxypeptidase: Properties, induction upon wounding, and immunocytochemical localization.
Miami Beach -- Mast cell carboxypeptidase shows promise as a new clinical marker for anaphylaxis, Dr.
Using a pair of specific monoclonal antibodies, CA4 and CA5, British researchers have developed an enzyme-linked immunosorbent assay for carboxypeptidase, a protease that is released with tryptase by activated mast cells and is a mediator of inflammation.
Amin I, Jinap S, Jamilah B (1998) Proteolytic activity (aspartic endoproteinase and carboxypeptidase) of cocoa bean during fermentation.