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The expected taxonomic range for this enzyme is: Tetrapoda
Reaction Schemes
cleavage of C-terminal glycinamide from polypeptides
Synonyms
carboxyamidase, carboxamidopeptidase,
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EC 3.4.15.2
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formerly
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glycinamidase, peptidyl
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peptidyl amino acid amide hydrolase
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peptidyl carboxy-amidase
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peptidyl carboxyamidase
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peptidyl-aminoacylamidase
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peptidyl-glycinamidase
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carboxamidopeptidase
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cleavage of C-terminal glycinamide from polypeptides
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hydrolysis of peptide bond
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acetyl-L-Trp ethyl ester + H2O
?
toad
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?
alpha-aminosuberic acid + H2O
?
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?
alpha-aminosuberic acid oxytocin + H2O
glycinamide + ?
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?
alpha-deamino-cystathionine + H2O
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?
alpha-deamino-cystathionine-6,1-oxytocin + H2O
glycinamide + ?
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?
antidiuretic hormone + H2O
glycinamide + ?
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release of glycinamide from the C-terminus of the hormone
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?
benzoyl-L-Arg ethyl ester + H2O
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toad
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?
beta-deamino-cystathionine-1,6-oxytocin + H2O
glycinamide + ?
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?
oxytocin + H2O
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the enzyme is not a strict peptidyl-glycinamidase, but can release other amino acid amides from a variety of amidated peptide
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oxytocin + H2O
glycinamide + ?
Vasopressin + H2O
?
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?
[Arg8]-vasopressin + H2O
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toad
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hydrolysis of the Arg8-Gly9-NH2 bond
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?
additional information
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toad
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enzyme inactivates neurophyseal hormones
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oxytocin + H2O
glycinamide + ?
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?
oxytocin + H2O
glycinamide + ?
toad
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hydrolysis of the Leu8-Gly9-NH2 bond
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additional information
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toad
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enzyme inactivates neurophyseal hormones
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?
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4-methylumbelliferyl p-guanidinobenzoate
toad
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alpha-aminosuberic acid oxytocin
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at high concentrations
beta-deamino-cystathionine-1,6-oxytocin
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at high concentrations
concanavalin A
toad
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diisopropyl phosphofluoridate
Lima bean trypsin inhibitor
toad
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p-Nitrophenyl p-guanidinobenzoate
toad
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tosyllysine chloromethyl ketone
toad
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tosylphenylalanine chloromethyl ketone
toad
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diisopropyl phosphofluoridate
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diisopropyl phosphofluoridate
toad
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PCMB
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PCMB
toad
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reversed by Cys
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0.0025 - 0.0033
alpha-aminosuberic acid
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0.0025 - 0.0033
alpha-deamino-cystathionine
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0.00625
beta-deamino-cystathionine-1,6-oxytocin
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0.0025 - 0.0033
Oxytocin
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7.5 - 8.5
toad
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hydrolysis of 8-arginine-vasopressin or benzoyl-L-Arg ethyl ester
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brenda
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brenda
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brenda
toad
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brenda
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medulla
brenda
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brenda
toad
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brenda
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brenda
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100000
toad
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gel filtration
48000
toad
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2 * 48000, each subunit consists of a heavy chain, 28000 da, and a light chain, 19000 Da joined by a disulfide bond, SDS-PAGE
48000
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2 * 48000, each subunit consists of two polypeptide chains of 28 kDa and 19 kDa linked via two disulfide bonds
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dimer
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2 * 48000, each subunit consists of two polypeptide chains of 28 kDa and 19 kDa linked via two disulfide bonds
dimer
toad
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2 * 48000, each subunit consists of a heavy chain, 28000 da, and a light chain, 19000 Da joined by a disulfide bond, SDS-PAGE
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EDTA, 0.001 mM, stabilizes during purification
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Nardacci, N.J.; Mukhopadhyay, S.; Campbell, B.J.
Partial purification and characterization of the antidiuretic hormone-inactivating enzyme from renal plasma membranes
Biochim. Biophys. Acta
377
146-157
1975
Sus scrofa
brenda
Fruhaufova, L.; Suska-Brzezinska, E.; Barth,T.; Rychlik, I.
Rat liver enzyme inactivating oxytocin and its deamino-carba analogues
Collect. Czech. Chem. Commun.
38
2793-2798
1973
Rattus norvegicus
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brenda
Simmons, W.H.; Walter, R.
Carboxamidopeptidase: purification and characterization of a neurohypophyseal hormone inactivating peptidase from toad skin
Biochemistry
19
39-48
1980
toad
brenda
Simmons, W.H.
Peptidyl-glycinamidase
Handbook of Proteolytic Enzymes (Barrett, A. J. , Rawlings, N. D. , Woessner, J. F. , eds) Academic Press
2
1932-1933
2004
Rhinella marina
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brenda
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3.4.19.2 peptidyl-glycinamidase
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