Peptidyl-dipeptidase Dcp
id:
peptidyl-dipeptidase-dcp-292-12064734
title:
Peptidyl-dipeptidase Dcp
text:
Peptidyl-dipeptidase Dcp (EC 3.4.15.5, dipeptidyl carboxypeptidase (Dcp), dipeptidyl carboxypeptidase) is a metalloenzyme found in the cytoplasm of bacterium E. Coli responsible for the C-terminal cleavage of a variety of dipeptides and unprotected larger peptide chains. The enzyme does not hydrolyze bonds in which P1' is Proline, or both P1 and P1' are Glycine. Dcp consists of 680 amino acid residues that form into a single active monomer which aids in the intracellular degradation of peptides.
brand slug:
wiki
category slug:
encyclopedia
description:
Class of enzymes
original url:
https://en.wikipedia.org/wiki/Peptidyl-dipeptidase_Dcp
date created:
date modified:
2023-08-26T15:19:33Z
main entity:
{"identifier":"Q12270377","url":"https://www.wikidata.org/entity/Q12270377"}
image:
{"content_url":"https://upload.wikimedia.org/wikipedia/commons/7/75/Peptidyl-Dipeptidase_Dcp.png","width":846,"height":550}
fields total:
13
integrity:
15