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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 (CPA) contains a zinc (Zn 2+) metal center in a tetrahedral geometry with amino acid residues in close proximity around zinc to facilitate catalysis and binding. Out of the 307 amino acids bonded in a peptide chain, the following amino acid residues are important for catalysis and binding; Glu-270, Arg-71, Arg-127, Asn-144 ...
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 ...
DD-transpeptidase catalytic mechanism. Crosslinking of peptidyl moieties of adjacent glycan strands is a two-step reaction. The first step involves the cleavage of the D-alanyl-D-alanine bond of a peptide unit precursor acting as carbonyl donor, the release of the carboxyl-terminal D-alanine, and the formation of the acyl-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 ...
Glutamate carboxypeptidase (EC 3.4.17.11, carboxypeptidase G, carboxypeptidase G1, carboxypeptidase G2, glutamyl carboxypeptidase, N-pteroyl-L-glutamate hydrolase) is an enzyme.
Carboxypeptidase N catalytic chain is an enzyme that in humans is encoded by the CPN1 gene. [ 5 ] [ 6 ] [ 7 ] Carboxypeptidase N is a plasma metallo-protease that cleaves basic amino acids from the C terminal of peptides and proteins.
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.