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A carboxypeptidase (EC number 3.4.16 - 3.4.18) is a protease enzyme that hydrolyzes (cleaves) a peptide bond at the carboxy-terminal (C-terminal) end of a protein or peptide. This is in contrast to an aminopeptidases , which cleave peptide bonds at the N-terminus of proteins.
Carboxypeptidase A and the target enzyme of Captopril, angiotensin-converting enzyme, have very similar structures, as they both contain a zinc ion within the active site. This allowed for a potent carboxypeptidase A inhibitor to be used to inhibit the enzyme and, thus, lower blood pressure through the renin-angiotensin-aldosterone system. [1]
Lysine carboxypeptidase's EC number is 3.4.17.3. The first number in an EC number indicates the main class that the enzyme belongs to (the options being oxidoreductases, transferases, hydrolases, lyases, isomerases, and ligases). Lysine carboxypeptidase belongs to class 3 which indicates that it is a hydrolase. Hydrolases use water to break ...
Glutamate carboxypeptidase (EC 3.4.17.11, carboxypeptidase G, carboxypeptidase G1, carboxypeptidase G2, glutamyl carboxypeptidase, N-pteroyl-L-glutamate hydrolase) is an enzyme.
53320 Ensembl ENSG00000086205 ENSMUSG00000001773 UniProt Q04609 O35409 RefSeq (mRNA) NM_001014986 NM_001193471 NM_001193472 NM_001193473 NM_004476 NM_001351236 NM_001159706 NM_016770 RefSeq (protein) NP_001014986 NP_001180400 NP_001180401 NP_001180402 NP_004467 NP_001338165 NP_001153178 NP_058050 Location (UCSC) Chr 11: 49.15 – 49.21 Mb Chr 7: 86.37 – 86.43 Mb PubMed search Wikidata View ...
Carboxypeptidase E (CPE), also known as carboxypeptidase H (CPH) and enkephalin convertase, is an enzyme that in humans is encoded by the CPE gene. [5] This enzyme catalyzes the release of C-terminal arginine or lysine residues from polypeptides. CPE is involved in the biosynthesis of most neuropeptides and peptide hormones. [6]
Carboxypeptidase M (EC 3.4.17.12, CPM) is an enzyme. [1] [2] [3] This enzyme catalyses the following chemical reaction. Cleavage of C-terminal arginine or lysine residues from polypeptides. This is a membrane-bound enzyme optimally active at neutral pH.
The carboxypeptidase A family can be divided into two subfamilies: carboxypeptidase H (regulatory) and carboxypeptidase A (digestive). [1] Members of the H family have longer C-termini than those of family A, [2] and carboxypeptidase M (a member of the H family) is bound to the membrane by a glycosylphosphatidylinositol anchor, unlike the majority of the M14 family, which are soluble.