3.2.1.57: isopullulanase
This is an abbreviated version!
For detailed information about isopullulanase, go to the full flat file.
Word Map on EC 3.2.1.57
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3.2.1.57
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pullulans
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aspergillus
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niger
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ipu
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glucoamylase
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oligosaccharides
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subsite
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minioluteum
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dextranases
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penicillium
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deglycosylation
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neopullulanase
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glucosidic
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hydrolyse
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dextran
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flask
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oryzae
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polysaccharide
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melanogenum
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endoglycosidase
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aureobasidium
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peptide-n-glycosidase
- 3.2.1.57
- pullulans
- aspergillus
- niger
- ipu
- glucoamylase
- oligosaccharides
-
subsite
- minioluteum
- dextranases
-
penicillium
-
deglycosylation
- neopullulanase
-
glucosidic
-
hydrolyse
- dextran
-
flask
- oryzae
- polysaccharide
- melanogenum
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endoglycosidase
-
aureobasidium
-
peptide-n-glycosidase
Reaction
hydrolysis of pullulan to isopanose (6-alpha-maltosylglucose) =
Synonyms
IPU, More, pullulan 4-glucanohydrolase
ECTree
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Posttranslational Modification
Posttranslational Modification on EC 3.2.1.57 - isopullulanase
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glycoprotein
highly N-glycosylated enzyme with 15 potential N-glycosylation sites (Asn-X-Ser/Thr), the side chain of a glycosylated asparagine residue is important for the stability of the enzyme, enzyme deglycosylation results in a decrease in thermostability. Enzyme deglycosylated with peptide-N-glycosidase F shows virtually no enzymatic activity, while a single GlcNAc residue remains following digestion with Endo H, and the activity of the Endo H-treated wild-type enzyme is 65% compared to intact, non-deglycosylated, wild-type enzyme
glycoprotein
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highly N-glycosylated enzyme with 15 potential N-glycosylation sites (Asn-X-Ser/Thr), the side chain of a glycosylated asparagine residue is important for the stability of the enzyme, enzyme deglycosylation results in a decrease in thermostability. Enzyme deglycosylated with peptide-N-glycosidase F shows virtually no enzymatic activity, while a single GlcNAc residue remains following digestion with Endo H, and the activity of the Endo H-treated wild-type enzyme is 65% compared to intact, non-deglycosylated, wild-type enzyme
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glycoprotein
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recombinant IPU expressed in Pichia pastoris GS115 has a higher carbohydrate content, 41%, than native IPU, 12-15%, or recombinant IPU expressed in Aspergillus oryzae M-2-3, 34%
glycoprotein
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the sugar content of native IPU is 12.4-15.3%, that of recombinant IPU is 33.8%, deglycosylated enzyme by endoglycosidase H with a sugar content of 2.1% retains 65% of its original activity, kinetics of deglycosylated IPU, hybrid- and/or high-mannose types