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3.2.1.96: mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase

This is an abbreviated version!
For detailed information about mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase, go to the full flat file.

Word Map on EC 3.2.1.96

Reaction

(Man)3(GlcNAc)2Asn
+
H2O
=
(Man)3GlcNAc
 +
GlcNAc-Asn

Synonyms

acetylglucosaminidase, endo-beta, beta-N-acetylglucosaminidase, CBM32, di-N-acetylchitobiosyl beta-N-acetylglucosaminidase, DI-N-acetylchitobiosyl beta-N-acetylglucosaminidase F1, DI-N-acetylchitobiosyl beta-N-acetylglucosaminidase F2, DI-N-acetylchitobiosyl beta-N-acetylglucosaminidase F3, endo, Endo D, Endo H, Endo M, Endo-A, endo-beta-(1->4)-N-acetylglucosaminidase, endo-beta-1,4-N-acetylglucosamidase, endo-beta-acetylglucosaminidase, endo-beta-GlcNAc-ase, endo-beta-N-acetylglucosaminidase, endo-beta-N-acetylglucosaminidase A, endo-beta-N-acetylglucosaminidase D, endo-beta-N-acetylglucosaminidase F, endo-beta-N-acetylglucosaminidase H, endo-beta-N-acetylglucosaminidase HS, endo-beta-N-acetylglucosaminidase L, endo-beta-N-acetylglucosaminidase M, Endo-BH, endo-BII, Endo-CC1, Endo-CC2, Endo-D, Endo-Fsp, endo-GM, Endo-HO, endo-LE, endo-M, endo-N-acetyl-beta-D-glucosaminidase, endo-N-acetyl-beta-glucosaminidase, Endo-Om, EndoBB, EndoBI-1, EndoBI-2, EndoD, endoE, EndoF1, endoglycosidase F1, endoglycosidase F2, endoglycosidase F3, endoglycosidase S, endohexosaminidase, EndoS2, ENGase, ENGase A, ENGase CI, ENGase CII, ENGase D, ENGase F, ENGase F1, ENGase F2, ENGase F3, ENGase Fsp, ENGase H, ENGase L, ENGase Mx, ENGase PI, ENGase PII, ENGase St, Engase1p, ENGase85A, ENGase85B, mannosyl-glycoprotein 1,4-N-acetamidodeoxy-beta-D-glycohydrolase, Mannosyl-glycoprotein endo-beta-N-acetyl-glucosaminidase, Mannosyl-glycoprotein endo-beta-N-acetyl-glucosaminidase F1, Mannosyl-glycoprotein endo-beta-N-acetyl-glucosaminidase F2, Mannosyl-glycoprotein endo-beta-N-acetyl-glucosaminidase F3, More, murein hydrolase, NAGase

ECTree

     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.96 mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase

Engineering

Engineering on EC 3.2.1.96 - mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D184N
D184N b1
-
the mutated enzyme specifically binds to the core of N-glycans, Man3GlcNAc2
N180A
0.5% of the activity compared to wild-type enzyme
N180C
2.1% of the activity compared to wild-type enzyme
N180D
5.8% of the activity compared to wild-type enzyme
N180E
3.3% of the activity compared to wild-type enzyme
N180F
0.1% of the activity compared to wild-type enzyme
N180G
0.4% of the activity compared to wild-type enzyme
N180H
8.7% of the activity compared to wild-type enzyme. Wild-type Endo-CC1 can not transfer the complex type sialobiantennary oligosaccharide onto the GlcNAc-RNase B. The mutant enzyme transfers the oligosaccharide onto the GlcNAc-RNase B. This protein is named Neo-RNase B. The N180H mutant does not cleave the oligosaccharide off the Neo-RNase B
N180I
4.0% of the activity compared to wild-type enzyme
N180K
0.2% of the activity compared to wild-type enzyme
N180L
0.6% of the activity compared to wild-type enzyme
N180M
12.0% of the activity compared to wild-type enzyme
N180P
0.8% of the activity compared to wild-type enzyme
N180Q
16.9% of the activity compared to wild-type enzyme. Wild-type Endo-CC1 can not transfer the complex type sialobiantennary oligosaccharide onto the GlcNAc-RNase B. The mutant enzyme transfers the oligosaccharide onto the GlcNAc-RNase B. This protein is named Neo-RNase B. The N180Q mutant cleaves the oligosaccharide off the Neo-RNase B
N180S
1.0% of the activity compared to wild-type enzyme
N180T
1.0% of the activity compared to wild-type enzyme
N180V
3.4% of the activity compared to wild-type enzyme
N180A
-
0.5% of the activity compared to wild-type enzyme
-
N180C
-
2.1% of the activity compared to wild-type enzyme
-
N180D
-
5.8% of the activity compared to wild-type enzyme
-
N180E
-
3.3% of the activity compared to wild-type enzyme
-
N180H
-
8.7% of the activity compared to wild-type enzyme. Wild-type Endo-CC1 can not transfer the complex type sialobiantennary oligosaccharide onto the GlcNAc-RNase B. The mutant enzyme transfers the oligosaccharide onto the GlcNAc-RNase B. This protein is named Neo-RNase B. The N180H mutant does not cleave the oligosaccharide off the Neo-RNase B
-
E186Q
-
the mutant has an active beta domain but inactive alpha domain and shows no activity with lactoferrin
E662Q
-
the mutant has N active alpha domain but inactive beta domain and shows activity towards lactoferrin
E186Q
-
the mutant has an active beta domain but inactive alpha domain and shows no activity with lactoferrin
-
E662Q
-
the mutant has N active alpha domain but inactive beta domain and shows activity towards lactoferrin
-
D121N
-
mutant has no enzymatic activity
D124N
-
mutant has 35% of the wild-type activity
D126E
-
mutant has 0.1% of the wild-type activity
D126N
-
mutant has 2% of the wild-type activity
D127A
-
mutant has 1.8% of the wild-type activity
D127E
-
mutant has 7.2% of the wild-type activity
D127N
-
mutant has 6% of the wild-type activity
E128A
-
mutant has no enzymatic activity
F42G
-
mutant has 30% of the wild-type activity
G122L
-
mutant has 4.4% of the wild-type activity
N17A
-
mutant has 80% of the wild-type activity
N45A
-
mutant has 70% of the wild-type activity
N58A
-
mutant has 100% of the wild-type activity
N60A
-
mutant has 100% of the wild-type activity
N89S
-
mutant has 100% of the wild-type activity
Q91A
-
mutant has 100% of the wild-type activity
V16A
-
mutant has 70% of the wild-type activity
Y129A
-
mutant has 70% of the wild-type activity
Y13A
-
mutant has 0.1% of the wild-type activity
Y164A
-
mutant has 70% of the wild-type activity
Y191A
-
mutant has 0.2% of the wild-type activity
Y241A
-
mutant has 20% of the wild-type activity
Y56A
-
mutant has 100% of the wild-type activity
E173A
-
mutation in catalytically essential residue. Partial rescue of activity by addition of sodium azide or sodium formate, the produced beta-glycosyl azide retaines the anomeric configuration
E173Q
site-directed mutagenesis, the mutant shows increased transglycosylation activity compared to the wild-type enzyme, three-dimensional structure determination and analysis, overview
N171A
completely abolishes enzymatic activity
Y205F
exhibits reduced hydrolysis activity with an increase in transglycosylation yields
Y299F
3fold increase in the transglycosylation activity, while the hydrolysis activity remains unchanged
E172Q
Halalkalibacterium halodurans
-
mutant has no enzymatic activity
W215R
Halalkalibacterium halodurans
-
enzyme has lower transglycosylation activity
E172Q
Halalkalibacterium halodurans C-125
-
mutant has no enzymatic activity
-
W215R
Halalkalibacterium halodurans C-125
-
enzyme has lower transglycosylation activity
-
D147A
-
site-directed mutagenesis, the mutant show 19% reduced activity compared to the wild-type enzyme
D158A
-
site-directed mutagenesis, the mutant show 88% reduced activity compared to the wild-type enzyme
D170A
-
site-directed mutagenesis, the mutant show 98.8% reduced activity compared to the wild-type enzyme
D218A
-
site-directed mutagenesis, the mutant shows only residual hydrolytic activity
D279A
-
site-directed mutagenesis, the mutant shows only residual hydrolytic activity
E177A
E177H
-
site-directed mutagenesis, the mutant shows only residual hydrolytic activity
E177Q
-
site-directed mutagenesis, the mutant shows only residual hydrolytic activity
N175A
N175D
-
site-directed mutagenesis, the mutant shows only residual hydrolytic activity
N175H
-
site-directed mutagenesis, the mutant shows only residual hydrolytic activity
N175M
-
site-directed mutagenesis, the mutant shows only residual hydrolytic activity
N175Q
N175Q/Y217F
-
site-directed mutagenesis, the double mutant is a glycosynthase, but the additional mutation at Tyr217 does not further enhance the activity
N175S
-
site-directed mutagenesis, the mutant shows only residual hydrolytic activity
N175T
-
site-directed mutagenesis, the mutant shows only residual hydrolytic activity
N230S
-
reduction in transglycosylation activity
N249S
-
almost complete loss of transglycosylation activity
W228F
-
reduction in transglycosylation activity
W251N
-
almost complete loss of transglycosylation activity
Y217F
-
enhanced transglycosylation activity and diminished hydrolytic activity
Y217F/W228F
-
reduction in transglycosylation activity
Y250N
-
almost complete loss of transglycosylation activity
W295A
no endo-beta-N-acetylglucosaminidase activity
W295E
no endo-beta-N-acetylglucosaminidase activity
W295F
increased activity toward the agalacto-biantennary oligosaccharide compared with the wild-type enzyme, but decreased activities toward the trimannosyl core and high-mannose oligosaccharides
W295Y
increased endo-beta-N-acetylglucosaminidase activity
del316/delY319/E320
-
mutation completely removes the activity for (Man)5(GlcNAc)2Asn, a low level of activity towards (Man)3(GlcNAc)2Asn remains
delE324
-
loss of activity
delW359/delY360
-
loss of activity
H371W
the mutant shows increased hydrolytic activity compared to the wild type
N322A
N322Q
the mutant demonstrates remarkable transglycosylation activity with only marginal hydrolysis activity, having much higher catalytic efficiency for glycosylating the nonfucosylated GlcNAc acceptor
Y360F
the mutant shows slightly reduced hydrolytic activity compared to the wild type
D130
-
1.25-3.14% of the activity of the wild-type enzyme, depending on assay method
D130A
-
0.04-0.1% of the activity of the wild-type enzyme
D130N
-
0.1-0.21% of the activity of the wild-type enzyme, depending on assay method
D130N/E132Q
-
no activity
E132A
-
no activity
E132D
-
0.03-0.05% of the activity of the wild-type enzyme
E132Q
-
less than 0.05% of the activity of the wild-type enzyme
additional information