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Literature summary extracted from

  • Aviles, F.X.; Vendrell, J.
    Carboxypeptidase B (2004), Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. ) Academic Press, 2, 831-833.
No PubMed abstract available

Application

EC Number Application Comment Organism
3.4.17.2 diagnostics the enzyme is a serum marker for acute pancreatitis and pancreatic graft injection Homo sapiens

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.17.2 DNA sequence determination, phylogenetic tree Homo sapiens
3.4.17.2 DNA sequence determination, phylogenetic tree Rattus norvegicus
3.4.17.2 DNA sequence determination, phylogenetic tree Sus scrofa
3.4.17.2 DNA sequence determination, phylogenetic tree Bos taurus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.4.17.2
-
 Sus scrofa

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.17.2 2-mercaptomethyl-3-guanidinoethyl-propanoic acid
-
 Bos taurus
3.4.17.2 2-mercaptomethyl-3-guanidinoethyl-propanoic acid
-
 Homo sapiens
3.4.17.2 2-mercaptomethyl-3-guanidinoethyl-propanoic acid
-
 Rattus norvegicus
3.4.17.2 2-mercaptomethyl-3-guanidinoethyl-propanoic acid
-
 Sus scrofa
3.4.17.2 2-mercaptomethyl-5-guanidinopentanoic acid
-
 Bos taurus
3.4.17.2 2-mercaptomethyl-5-guanidinopentanoic acid
-
 Homo sapiens
3.4.17.2 2-mercaptomethyl-5-guanidinopentanoic acid
-
 Rattus norvegicus
3.4.17.2 2-mercaptomethyl-5-guanidinopentanoic acid
-
 Sus scrofa
3.4.17.2 Guanidinoethylmercaptosuccinic acid
-
 Bos taurus
3.4.17.2 Guanidinoethylmercaptosuccinic acid
-
 Homo sapiens
3.4.17.2 Guanidinoethylmercaptosuccinic acid
-
 Rattus norvegicus
3.4.17.2 Guanidinoethylmercaptosuccinic acid
-
 Sus scrofa
3.4.17.2 leech carboxypeptidase inhibitor
-
 Bos taurus
3.4.17.2 leech carboxypeptidase inhibitor
-
 Homo sapiens
3.4.17.2 leech carboxypeptidase inhibitor
-
 Rattus norvegicus
3.4.17.2 leech carboxypeptidase inhibitor
-
 Sus scrofa
3.4.17.2 potato carboxypeptidase inhibitor
-
 Bos taurus
3.4.17.2 potato carboxypeptidase inhibitor
-
 Homo sapiens
3.4.17.2 potato carboxypeptidase inhibitor
-
 Rattus norvegicus
3.4.17.2 potato carboxypeptidase inhibitor
-
 Sus scrofa

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.17.2 extracellular the enzyme is secreted from pancreas Sus scrofa
-
-
3.4.17.2 extracellular the enzyme is secreted from pancreas Bos taurus
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.17.2 Cl- required Homo sapiens
3.4.17.2 Cl- required Rattus norvegicus
3.4.17.2 Cl- required Sus scrofa
3.4.17.2 Cl- required Bos taurus
3.4.17.2 Zn2+ 1 mol Zn2+ per mol of enzyme, coordinated by the conserved residues His69, Glu72, and His196 Homo sapiens
3.4.17.2 Zn2+ 1 mol Zn2+ per mol of enzyme, coordinated by the conserved residues His69, Glu72, and His196 Rattus norvegicus
3.4.17.2 Zn2+ 1 mol Zn2+ per mol of enzyme, coordinated by the conserved residues His69, Glu72, and His196 Sus scrofa
3.4.17.2 Zn2+ 1 mol Zn2+ per mol of enzyme, coordinated by the conserved residues His69, Glu72, and His196 Bos taurus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.17.2 additional information Homo sapiens the enzyme is highly specific for excising C-terminal Lys and Arg residues from peptides and proteins with a preference for Arg, it also acts on C-terminal Val, Leu, Ile, Asn, Gly, and Gln but at a slower rate, the enzyme shows a preference for Ala in P2 position ?
-
 ?
3.4.17.2 additional information Rattus norvegicus the enzyme is highly specific for excising C-terminal Lys and Arg residues from peptides and proteins with a preference for Arg, it also acts on C-terminal Val, Leu, Ile, Asn, Gly, and Gln but at a slower rate, the enzyme shows a preference for Ala in P2 position ?
-
 ?
3.4.17.2 additional information Sus scrofa the enzyme is highly specific for excising C-terminal Lys and Arg residues from peptides and proteins with a preference for Arg, it also acts on C-terminal Val, Leu, Ile, Asn, Gly, and Gln but at a slower rate, the enzyme shows a preference for Ala in P2 position ?
-
 ?
3.4.17.2 additional information Bos taurus the enzyme is highly specific for excising C-terminal Lys and Arg residues from peptides and proteins with a preference for Arg, it also acts on C-terminal Val, Leu, Ile, Asn, Gly, and Gln but at a slower rate, the enzyme shows a preference for Ala in P2 position ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.17.2 Bos taurus
-
-
-
3.4.17.2 Homo sapiens
-
-
-
3.4.17.2 Rattus norvegicus
-
-
-
3.4.17.2 Sus scrofa
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.4.17.2 proteolytic modification the enzyme is synthesized as zymogen, cleavage and activation in vitro by trypsin Homo sapiens
3.4.17.2 proteolytic modification the enzyme is synthesized as zymogen, cleavage and activation in vitro by trypsin Rattus norvegicus
3.4.17.2 proteolytic modification the enzyme is synthesized as zymogen, cleavage and activation in vitro by trypsin Sus scrofa
3.4.17.2 proteolytic modification the enzyme is synthesized as zymogen, cleavage and activation in vitro by trypsin Bos taurus

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.17.2 native enzyme from pancreatic acetine powder Bos taurus

Reaction

EC Number Reaction Comment Organism Reaction ID
3.4.17.2 preferential release of a C-terminal lysine or arginine amino acid conserved catalytic residues are Glu270 and Asp127, residues Ser207, Glu243, and Asp255 determine the substrate specificity Homo sapiens
a
3.4.17.2 preferential release of a C-terminal lysine or arginine amino acid conserved catalytic residues are Glu270 and Asp127, residues Ser207, Glu243, and Asp255 determine the substrate specificity Rattus norvegicus
a
3.4.17.2 preferential release of a C-terminal lysine or arginine amino acid conserved catalytic residues are Glu270 and Asp127, residues Ser207, Glu243, and Asp255 determine the substrate specificity Sus scrofa
a
3.4.17.2 preferential release of a C-terminal lysine or arginine amino acid conserved catalytic residues are Glu270 and Asp127, residues Ser207, Glu243, and Asp255 determine the substrate specificity Bos taurus
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.17.2 intestine
-
 Bos taurus
-
3.4.17.2 muscle longitudinal, of instestine Bos taurus
-
3.4.17.2 pancreas
-
 Homo sapiens
-
3.4.17.2 pancreas
-
 Sus scrofa
-
3.4.17.2 pancreas
-
 Bos taurus
-
3.4.17.2 serum
-
 Homo sapiens
-

Storage Stability

EC Number Storage Stability Organism
3.4.17.2 frozen or precipitated purified pancreatic enzyme is stable for years Bos taurus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.17.2 benzoyl-Gly-Arg + H2O
-
 Homo sapiens benzoyl-Gly + Arg
-
 ?
3.4.17.2 benzoyl-Gly-Arg + H2O
-
 Rattus norvegicus benzoyl-Gly + Arg
-
 ?
3.4.17.2 benzoyl-Gly-Arg + H2O
-
 Sus scrofa benzoyl-Gly + Arg
-
 ?
3.4.17.2 benzoyl-Gly-Arg + H2O
-
 Bos taurus benzoyl-Gly + Arg
-
 ?
3.4.17.2 additional information the enzyme is highly specific for excising C-terminal Lys and Arg residues from peptides and proteins with a preference for Arg, it also acts on C-terminal Val, Leu, Ile, Asn, Gly, and Gln but at a slower rate, the enzyme shows a preference for Ala in P2 position Homo sapiens ?
-
 ?
3.4.17.2 additional information the enzyme is highly specific for excising C-terminal Lys and Arg residues from peptides and proteins with a preference for Arg, it also acts on C-terminal Val, Leu, Ile, Asn, Gly, and Gln but at a slower rate, the enzyme shows a preference for Ala in P2 position Rattus norvegicus ?
-
 ?
3.4.17.2 additional information the enzyme is highly specific for excising C-terminal Lys and Arg residues from peptides and proteins with a preference for Arg, it also acts on C-terminal Val, Leu, Ile, Asn, Gly, and Gln but at a slower rate, the enzyme shows a preference for Ala in P2 position Sus scrofa ?
-
 ?
3.4.17.2 additional information the enzyme is highly specific for excising C-terminal Lys and Arg residues from peptides and proteins with a preference for Arg, it also acts on C-terminal Val, Leu, Ile, Asn, Gly, and Gln but at a slower rate, the enzyme shows a preference for Ala in P2 position Bos taurus ?
-
 ?
3.4.17.2 additional information the enzyme is highly specific for excising C-terminal Lys and Arg residues from peptides and proteins with a preference for Arg, it also acts on C-terminal Val, Leu, Ile, Asn, Gly, and Gln but at a slower rate, the enzyme shows a preference for Ala in P2 position, the enzyme shows no intrinsic carboxypeptidase and autoactivation activity Homo sapiens ?
-
 ?
3.4.17.2 additional information the enzyme is highly specific for excising C-terminal Lys and Arg residues from peptides and proteins with a preference for Arg, it also acts on C-terminal Val, Leu, Ile, Asn, Gly, and Gln but at a slower rate, the enzyme shows a preference for Ala in P2 position, the enzyme shows no intrinsic carboxypeptidase and autoactivation activity Rattus norvegicus ?
-
 ?
3.4.17.2 additional information the enzyme is highly specific for excising C-terminal Lys and Arg residues from peptides and proteins with a preference for Arg, it also acts on C-terminal Val, Leu, Ile, Asn, Gly, and Gln but at a slower rate, the enzyme shows a preference for Ala in P2 position, the enzyme shows no intrinsic carboxypeptidase and autoactivation activity Sus scrofa ?
-
 ?
3.4.17.2 additional information the enzyme is highly specific for excising C-terminal Lys and Arg residues from peptides and proteins with a preference for Arg, it also acts on C-terminal Val, Leu, Ile, Asn, Gly, and Gln but at a slower rate, the enzyme shows a preference for Ala in P2 position, the enzyme shows no intrinsic carboxypeptidase and autoactivation activity Bos taurus ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.4.17.2 More the pancreatic enzyme is divided in the activation domain and the enzyme domain linked by a connecting region Homo sapiens
3.4.17.2 More the pancreatic enzyme is divided in the activation domain and the enzyme domain linked by a connecting region Rattus norvegicus
3.4.17.2 More the pancreatic enzyme is divided in the activation domain and the enzyme domain linked by a connecting region Bos taurus
3.4.17.2 More the pancreatic enzyme is divided in the activation domain, residues 1-80, and the enzyme domain, residues 96-401, linked by a connecting region, residues 81-95 Sus scrofa

Synonyms

EC Number Synonyms Comment Organism
3.4.17.2 basic carboxypeptidase
-
 Homo sapiens
3.4.17.2 basic carboxypeptidase
-
 Rattus norvegicus
3.4.17.2 basic carboxypeptidase
-
 Sus scrofa
3.4.17.2 basic carboxypeptidase
-
 Bos taurus
3.4.17.2 CPB
-
 Homo sapiens
3.4.17.2 CPB
-
 Rattus norvegicus
3.4.17.2 CPB
-
 Sus scrofa
3.4.17.2 CPB
-
 Bos taurus
3.4.17.2 More the enzyme belongs to the M14A peptidase family Homo sapiens
3.4.17.2 More the enzyme belongs to the M14A peptidase family Rattus norvegicus
3.4.17.2 More the enzyme belongs to the M14A peptidase family Sus scrofa
3.4.17.2 More the enzyme belongs to the M14A peptidase family Bos taurus
3.4.17.2 protaminase formerly Homo sapiens
3.4.17.2 protaminase formerly Rattus norvegicus
3.4.17.2 protaminase formerly Sus scrofa
3.4.17.2 protaminase formerly Bos taurus
3.4.17.2 tissue carboxypeptidase B
-
 Homo sapiens
3.4.17.2 tissue carboxypeptidase B
-
 Rattus norvegicus
3.4.17.2 tissue carboxypeptidase B
-
 Sus scrofa
3.4.17.2 tissue carboxypeptidase B
-
 Bos taurus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.17.2 7.5 7.8 assay at Homo sapiens
3.4.17.2 7.5 7.8 assay at Rattus norvegicus
3.4.17.2 7.5 7.8 assay at Sus scrofa
3.4.17.2 7.5 7.8 assay at Bos taurus

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.4.17.2 additional information
-
 additional information the Ki values for 2-mercaptomethyl-3-guanidinoethyl-propanoic acid, potato and leech carboxypeptidase inhibitors, and 2-mercaptomethyl-5-guanidinopentanoic acid are in the nanomolar range Homo sapiens
3.4.17.2 additional information
-
 additional information the Ki values for 2-mercaptomethyl-3-guanidinoethyl-propanoic acid, potato and leech carboxypeptidase inhibitors, and 2-mercaptomethyl-5-guanidinopentanoic acid are in the nanomolar range Rattus norvegicus
3.4.17.2 additional information
-
 additional information the Ki values for 2-mercaptomethyl-3-guanidinoethyl-propanoic acid, potato and leech carboxypeptidase inhibitors, and 2-mercaptomethyl-5-guanidinopentanoic acid are in the nanomolar range Sus scrofa
3.4.17.2 additional information
-
 additional information the Ki values for 2-mercaptomethyl-3-guanidinoethyl-propanoic acid, potato and leech carboxypeptidase inhibitors, and 2-mercaptomethyl-5-guanidinopentanoic acid are in the nanomolar range Bos taurus