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Literature summary extracted from

  • Simmons, W.H.
    Peptidyl-glycinamidase (2004), Handbook of Proteolytic Enzymes (Barrett, A. J. , Rawlings, N. D. , Woessner, J. F. , eds) Academic Press, 2, 1932-1933.
No PubMed abstract available

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.19.2 diisopropyl phosphofluoridate
-
 Rhinella marina
3.4.19.2 PCMB
-
 Rhinella marina

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.19.2 48000
-
 2 * 48000, each subunit consists of two polypeptide chains of 28 kDa and 19 kDa linked via two disulfide bonds Rhinella marina

Organism

EC Number Organism UniProt Comment Textmining
3.4.19.2 Rhinella marina
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.4.19.2 glycoprotein
-
 Rhinella marina

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.19.2 to homogeneity Rhinella marina

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.19.2 oxytocin + H2O the enzyme is not a strict peptidyl-glycinamidase, but can release other amino acid amides from a variety of amidated peptide Rhinella marina ?
-
 ?
3.4.19.2 Vasopressin + H2O
-
 Rhinella marina ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.4.19.2 dimer 2 * 48000, each subunit consists of two polypeptide chains of 28 kDa and 19 kDa linked via two disulfide bonds Rhinella marina

Synonyms

EC Number Synonyms Comment Organism
3.4.19.2 carboxamidopeptidase
-
 Rhinella marina
3.4.19.2 peptidyl-glycinamidase
-
 Rhinella marina

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.19.2 7
-
-
 Rhinella marina