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Literature summary extracted from

  • Darby, N.J.; Fricker, L.D.; Maruthainar, K.; Smyth, D.G.
    A study of the substrate specificity of carboxypeptidase H (1988), Pept. Chem. Biol. (Proc. Am. Pept. Symp. ,10th Meeting Date 1987, Marshall, G. R. , ed. ), , 613-614.
No PubMed abstract available

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.17.10 Guanidinoethylmercaptosuccinic acid
-
 Sus scrofa

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.17.10 secretory granule
-
 Sus scrofa 30141
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.17.10 additional information Sus scrofa C-terminal histidine is removed at a very slow rate ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.17.10 Sus scrofa
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.17.10 hypophysis
-
 Sus scrofa
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.17.10 (Met)enkephalin-Arg + H2O
-
 Sus scrofa Tyr-Gly-Gly-Phe-Met + Arg
-
 ?
3.4.17.10 (Met)enkephalin-Lys + H2O
-
 Sus scrofa Tyr-Gly-Gly-Phe-Met + Lys
-
 ?
3.4.17.10 D-Tyr-Ala-His-Lys-Lys + H2O
-
 Sus scrofa D-Tyr-Ala-His-Lys + Lys
-
 ?
3.4.17.10 additional information releases C-terminal arginine or lysine residues from the hexapeptide precursor of [Met]enkephalin and [Leu]enkephalin, forming the pentapeptide enkephalin Sus scrofa ?
-
 ?
3.4.17.10 additional information C-terminal histidine is removed at a very slow rate Sus scrofa ?
-
 ?