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.

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 ?
Research findings demonstrated that carboxypeptidase A gene is responsible to hydrolyze OTA to non toxic metabolite (Pitout, 1969; Abrunhosa et al.
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).
Determination of the activity of carboxypeptidase A in the blood of healthy human adults.
Another important advantage of activity assays compared with antigen assays is that the 2 described polymorphisms in the coding region of proCPU (Thr147A1a and Thr325I1e) have similar activation kinetics and the activated enzymes have similar carboxypeptidase B-like activity toward small synthetic substrates (26, 28).
Carboxypeptidase O (CPO) is a member of the M14 family of proteolytic enzymes.
6) catalyzes the hydrolysis of an amide bond (N-CO) in the [beta]-lactam ring of the antibiotics of the penicillin/cephalosporin family contributing to the most common mechanism of bacterial resistance to [beta]-lactam antibiotics, while penicillin-binding proteins encompass transpeptidase, carboxypeptidase, and transglycosylase activities and have a part in the biosynthesis of the bacterial cell wall.
Rigat B, Hubert C, Corvol P, Soubrier F (1992) PCR detection of the insertion/deletion polymorphism of the human angiotensin converting enzyme gene (DCP1) (dipeptidyl carboxypeptidase 1).
Hydrolysis of biological peptides by human angiotensin-converting enzyme-related carboxypeptidase," Journal of Biological Chemistry, vol.
1%) in any traits were phosphodiesterase 4B (PDE4B), serine/threonine kinase 40 (STK40), collagen, type XI, alpha 1 (COL11A1), ephrin-A1 (EFNA1), netrin 4 (NTN4), neuron specific gene family member 1 (NSG1), estrogen receptor 1 (ESR1), neurexin 3 (NRXN3), spectrin, beta, non-erythrocytic 1 (SPTBN1), ADP-ribosylation factor interacting protein 1 (ARFIP1), mutL homolog 1 (MLH1), transmembrane channel-like 7 (TMC7), carboxypeptidase X, member 2 (CPXM2), and ADAM metallopeptidase domain 12 (ADAM12).