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Literature summary for 3.4.17.15 extracted from

  • Jimenez, M.A.; Villegas, V.; Santoro, J.; Serrano, L.; Vendrell, J.; Aviles, F.X.; Rico, M.
    NMR solution structure of the activation domain of human procarboxypeptidase A2 (2003), Protein Sci., 12, 296-305.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
additional information structure of the activation domain of the procarboxypeptidase A2, activation mechanism, overview Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification the proCPA2 is activated by proteoltyic cleavage Homo sapiens

Reaction

Reaction Comment Organism Reaction ID
Similar to that of carboxypeptidase A (EC 3.4.17.1), but with a preference for bulkier C-terminal residues structure-function relationship, activation mechanism Homo sapiens

Subunits

Subunits Comment Organism
More structure-function relationship, three-dimensional structure, secondary structure, NMR analysis at pH 7.0, 25°C, hydrogen exchange analysis in unfolding, overview Homo sapiens

Synonyms

Synonyms Comment Organism
ADA2
-
Homo sapiens