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Literature summary for 3.4.17.1 extracted from

  • Srivastava, A.S.; Kurokawa, T.; Suzuki, T.
    Molecular cloning and cDNA sequence analysis of carboxypeptidases A1, A2 and B from the Japanese flounder Paralichthys olivaceus (2003), Comp. Biochem. Physiol. B, 135, 593-599.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
additional information the triad for binding of the activation peptide consists of Asp, Phe, and Trp residues Paralichthys olivaceus

Cloned(Commentary)

Cloned (Comment) Organism
DNA and amino acid sequence determination and analysis of the preproenzyme, phylogenetic analysis Paralichthys olivaceus

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ zinc-metallopeptidase, binding residues are H69, E72, and H196 Paralichthys olivaceus

Organism

Organism UniProt Comment Textmining
Paralichthys olivaceus Q8AXN4 preprocarboxypeptidase A1; Japanese flounder, female
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification the proCPA1 is activated by proteoltyic cleavage Paralichthys olivaceus

Reaction

Reaction Comment Organism Reaction ID
release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro residues Glu270 and Arg127 are important for activity, the catalytic triad consists of Ile275, Tyr248, and Ala250, residues at positions 202, 254, and 268 are important for substrate specificity Paralichthys olivaceus

Source Tissue

Source Tissue Comment Organism Textmining
intestine
-
Paralichthys olivaceus
-
pancreas
-
Paralichthys olivaceus
-

Synonyms

Synonyms Comment Organism
CPA1
-
Paralichthys olivaceus

pI Value

Organism Comment pI Value Maximum pI Value
Paralichthys olivaceus sequence calculation
-
8.75