Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.4.17.10 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
Search for more literature for 3.4.17.10

Inhibitors

Inhibitors Comment Organism Structure
Guanidinoethylmercaptosuccinic acid
-
 Sus scrofa

Localization

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
hypophysis
-
 Sus scrofa
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(Met)enkephalin-Arg + H2O
-
 Sus scrofa Tyr-Gly-Gly-Phe-Met + Arg
-
 ?
(Met)enkephalin-Lys + H2O
-
 Sus scrofa Tyr-Gly-Gly-Phe-Met + Lys
-
 ?
D-Tyr-Ala-His-Lys-Lys + H2O
-
 Sus scrofa D-Tyr-Ala-His-Lys + Lys
-
 ?
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 ?
-
 ?
additional information C-terminal histidine is removed at a very slow rate Sus scrofa ?
-
 ?