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

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Release 2023.1 (January 2023)