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3.5.1.52: peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase

This is an abbreviated version!
For detailed information about peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase, go to the full flat file.

Word Map on EC 3.5.1.52

Reaction

Manalpha(1-6)(Xylbeta(1-2))Manbeta(1-4)GlcNAcbeta(1-4)(Fucalpha(1-3))GlcNAc-Asn-Asp-Glu-Ser-Ser
+
H2O
=
Manalpha(1-6)(Xylbeta(1-2))Manbeta(1-4)GlcNAcbeta(1-4)(Fucalpha(1-3))GlcNAc
+
Asn-Asp-Glu-Ser-Ser

Synonyms

acid PNGase M, acidic peptide:N-glycanase, acidic PNGase, aPNGase, At3g14920, At5g05480, AtPNG1, DDB0189828, EC 3.2.2.18, glycoamidase, glycopeptidase, glycopeptide N-glycosidase, jackbean glycopeptidase, L-929 PNGase, MPng1, N-glycanase, N-glycosidase F, N-oligosaccharide glycopeptidase, Ncpng1, neutral PNGase M, Ngly1, peptide N-glycanase, peptide N-glycosidase, peptide N-glycosidase F, peptide N4(N-acetyl-glucosaminyl)asparagine amidase, peptide-N-(N-acetyl-beta-glucosaminyl) asparagine amidase F, peptide-N-glycanase, peptide-N-glycosidase F, peptide-N4-(N-acetyl-beta-D-glucosaminyl)asparagine amidase F, peptide-N4-(N-acetyl-beta-glucosaminyl) asparagine amidase, peptide: N-glycanase, peptide: N-glycosidase, peptide:N-glycanase, peptide:N-glycanase homolog, peptide:N-glycosidase, peptidyl N-glycanase F, PGNase, PNG-1, PNG1, Png1p, PNGase, PNGase A, PNGase A-like enzyme, PNGase At, PNGase F, PNGase F-II, PNGase H+, PNGase J, PNGase Os, PNGase Se, PNGase Yl, PNGase-A, PNGaseF, Pngl, SpPNGase, TGc domain-containing protein, yeast peptide: N-glycanase, YPng, YPng1

ECTree

     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.1 In linear amides
                3.5.1.52 peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase

Natural Substrates Products

Natural Substrates Products on EC 3.5.1.52 - peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase

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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATPase p97 + H2O
?
show the reaction diagram
a cofactor-binding motif of p97 contained within the last 10 amino acid residues of the C terminus is both necessary and sufficient to mediate interactions of p97 with PNGase. Phosphorylation of p97’s highly conserved penultimate tyrosine residue, which is the main phosphorylation site during T cell receptor stimulation, completely blocks binding of either PNGase or Ufd3 to p97. This observation suggests that phosphorylation of this residue modulates endoplasmic reticulum-associated protein degradation activity by discharging substrate-processing cofactors
-
-
?
class I MHC HC + H2O
?
show the reaction diagram
-
the enzyme is involved proteasomal degradation of glycosylated type I membrane protein class I MHC heavy chain, dislocated from ER to cytosol by cytomegalovirus-encoded glycoprotein US2 protein, overview
-
-
?
concanavalin A-precursor + H2O
?
show the reaction diagram
-
deglycosylation leads to conversion into an active lectin
-
-
?
melanopsin + H2O
?
show the reaction diagram
-
-
-
?
N-glycoprotein + H2O
?
show the reaction diagram
-
PNGase is involved in the release of N-glycans from N-glycoproteins
-
-
?
Oryzias latipes glycophosphoprotein MU-1 + H2O
?
show the reaction diagram
-
acid PNGase M from blastoderm stage 11, yolk-absorptive stage
-
-
?
Oryzias latipes glycophosphoprotein MU-2 + H2O
?
show the reaction diagram
-
acid PNGase M from blastoderm stage 11, yolk-absorptive stage
-
-
?
proton-coupled folate transporter + H2O
?
show the reaction diagram
-
-
-
-
?
tyrosinase + H2O
?
show the reaction diagram
-
the enzyme is required for processing of a class I-restricted epitope from tyrosinase together with the cooperative action of endoplasmic reticulum aminopeptidase 1 and cytosolic protease, overview
-
-
?
additional information
?
-