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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

Engineering

Engineering on EC 3.5.1.52 - peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C251A
-
the mutant exhibits a defect in degrading RTADELTA-transmembrane-Leu2 protein. Expression of the catalytic mutant results in significant stabilization of RTADELTA protein by binding to N-glycans on the substrate
L66M/L75M/L87M
-
site-directed mutagenesis, the PUB domain mutant shows slightly reduced p97 binding
C306A
-
site-directed mutagenesis, inactive mutant, inhibitor Z-VAD-fmk does not bind to the mutant enzyme
G79/F80A
-
site-directed mutagenesis, the double mutation completely abolishes the interaction of PNGase with p97
N41P
-
site-directed mutagenesis, the mutation completely abolishes the interaction of PNGase with p97
N58A
-
site-directed mutagenesis, the mutation does not affect the interaction of PNGase with p97
A208C
-
inactive
A208C/Y235H
-
inactive
Y235H
-
inactive
C165T
-
inactive
C165T/N166V/R167C
-
inactive
C191A
C221T
-
mutant with more than 50% wild type activity
D179E/P180A
-
mutant with more than 50% wild type activity
D208R/V209A
-
mutant with 10-50% wild type activity
D217A
mutation in the peptide binding site
D235A
E185R
-
mutant with 10-50% wild type activity
E185R/T186V
-
mutant with 10-50% wild type activity
E193D
-
inactive
E193D/W194F
-
inactive
E222A
-
no enzymic activity
E238A
mutation in the chitobiose binding site
F224Y
-
mutant with more than 50% wild type activity
G206D/L207I
-
mutant with 10-50% wild type activity
H218A
H218F
mutation in the chitobiose binding site
H218Y
-
site-directed mutagenesis, the mutant is inactive in protein glycosylation, but interacts with protein Rad23
I181W
-
mutant with more than 50% wild type activity
I181W/K182Q
-
inactive
K182Q
-
mutant with more than 50% wild type activity
K253A
mutation in the chitobiose binding site
L198V
-
mutant with more than 50% wild type activity
L200M
-
mutant with more than 50% wild type activity
L200M/I201L
-
mutant with more than 50% wild type activity
N166V/R167C
-
the mutant shows 79% of wild type activity
N178A
mutation in the peptide binding site
N178T
-
mutant with 10-50% wild type activity
N214C/R215Q
-
mutant with 10-50% wild type activity
N266F/F227H
-
mutant with more than 50% wild type activity
Q239A
mutation near the nonreducing end of the chitobiose, possible mannose binding site
Q243A
mutation near the nonreducing end of the chitobiose, possible mannose binding site
R176A
mutation in the peptide binding site
R187K/K188R
-
mutant with more than 50% wild type activity
R210A
-
no enzymic activity
V219L
-
mutant with 1-10% wild type activity
W123A
mutation in the peptide binding site
W194F/C195A
-
mutant with 10-50% wild type activity
W220F
-
81% of activity compared to wild type
W231F
-
83% of activity compared to wild type
W251A
mutation in the chitobiose binding site
Y211W
-
mutant with more than 50% wild type activity
Y223I
-
mutant with 10-50% wild type activity
additional information