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Literature summary for 3.4.19.2 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
Search for more literature for 3.4.19.2

Inhibitors

Inhibitors Comment Organism Structure
diisopropyl phosphofluoridate
-
 Rhinella marina
PCMB
-
 Rhinella marina

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Rhinella marina
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein
-
 Rhinella marina

Purification (Commentary)

Purification (Comment) Organism
to homogeneity Rhinella marina

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
-
 ?
Vasopressin + H2O
-
 Rhinella marina ?
-
 ?

Subunits

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

Synonyms

Synonyms Comment Organism
carboxamidopeptidase
-
 Rhinella marina
peptidyl-glycinamidase
-
 Rhinella marina

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
-
 Rhinella marina