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3.4.14.1: dipeptidyl-peptidase I

This is an abbreviated version!
For detailed information about dipeptidyl-peptidase I, go to the full flat file.

Word Map on EC 3.4.14.1

Reaction

Release of an N-terminal dipeptide, Xaa-Yaa-/-Zaa-, except when Xaa is Arg or Lys, or Yaa or Zaa is Pro =

Synonyms

Cat C, CATC, cathepsin C, cathepsin J, CTSC, DAP I, DDPI, dipeptide arylamidase I, dipeptidyl aminopeptidase I, dipeptidyl peptidase I, dipeptidyl peptidase I/cathepsin C, dipeptidyl transferase, DPAP1, DPAP2, DPP I, DPP-I, DPPI, EC 3.4.4.9, hDPPI, PBANKA_146070, PFL2290w

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.14 Dipeptidyl-peptidases and tripeptidyl-peptidases
                3.4.14.1 dipeptidyl-peptidase I

Crystallization

Crystallization on EC 3.4.14.1 - dipeptidyl-peptidase I

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
molecular modeling of inhibitor docking. Esters of dehydropeptides containing C-terminal (Z)-dehydrophenylalanine and dehydroalanine appear to be moderate or weak inhibitors of cathepsin C, with some of them exhibiting slow-binding behavior. They are rather bind at the surface of the enzyme and are not submersed in its binding cavities
molecular docking of substrate beta-(2-thienyl)Ala-beta-(7-methoxycoumarin-4-yl)Ala-Ser-Gly-Tyr(3-NO2). The interactions between the amino-terminal group of the substrate and the Asp1 and Gly277 of Cat C are responsible for the substrate N-terminus docking and are crucial for proteolytic activity