3.2.1.135: neopullulanase
This is an abbreviated version!
For detailed information about neopullulanase, go to the full flat file.
Word Map on EC 3.2.1.135
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3.2.1.135
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starch
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stearothermophilus
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amylolytic
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alpha-amylases
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cyclomaltodextrinase
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maltogenic
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amylopectin
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transglycosylation
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amylose
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alpha-1,4
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amylopullulanase
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debranching
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oligo-1,6-glucosidase
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glucanotransferase
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thermoactinomyces
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alpha-1,6-glucosidic
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isopanose
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cdase
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saccharifying
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pullulanases
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cyclodextrinase
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maltooligosaccharides
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isoamylase
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isopullulanase
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gamma-cyclodextrins
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biotechnology
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industry
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synthesis
- 3.2.1.135
- starch
- stearothermophilus
-
amylolytic
- alpha-amylases
- cyclomaltodextrinase
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maltogenic
- amylopectin
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transglycosylation
- amylose
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alpha-1,4
- amylopullulanase
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debranching
- oligo-1,6-glucosidase
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glucanotransferase
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thermoactinomyces
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alpha-1,6-glucosidic
- isopanose
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cdase
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saccharifying
- pullulanases
- cyclodextrinase
- maltooligosaccharides
- isoamylase
- isopullulanase
- gamma-cyclodextrins
- biotechnology
- industry
- synthesis
Reaction
Synonyms
Amo105, amylopullalanase, amylopullulanase, ApuA, ApuADELTA, bsNpl, cyclomaltodextrinase, Env Npu193A, More, neopullulanase-alpha-amylase, neopullulanase-like enzyme, Pul, pullulan 4-D-glucanohydrolase (6-alpha-D-glucosylmaltose), pullulan hydrolase type I, pullulanase, pullulanase II, pullulanase, neo-, Rbamy5, TetApuM955, TetApuR855, type II pullulanase, type III pullulan hydrolase
ECTree
Advanced search results
Engineering
Engineering on EC 3.2.1.135 - neopullulanase
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A416I
t1/2 of mutant enzyme at 70°C is 17 min, compared to 15 min for wild-type enzyme. Mutation does not compromise the catalytic activity
A566L
t1/2 of mutant enzyme at 70°C is 27 min, compared to 15 min for wild-type enzyme. Mutation does not compromise the catalytic activity
D46E
t1/2 of mutant enzyme at 70°C is 100 min, compared to 15 min for wild-type enzyme. Mutation does not compromise the catalytic activity
I358V
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mutation decreases the preference for alpha(1-6)-branched oligosaccharides and pullulan as substrates
I358W
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mutation reduces the acceptability of alpha(1-6)-branched oligo- and polysaccharides
M375L
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mutation increases transglycosylation activity in comparison to wild-type enzyme
N413Q
t1/2 of mutant enzyme at 70°C is 32 min, compared to 15 min for wild-type enzyme. Mutation does not compromise the catalytic activity
S407T
t1/2 of mutant enzyme at 70°C is 66 min, compared to 15 min for wild-type enzyme. Mutation does not compromise the catalytic activity
S422V
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mutation increases transglycosylation activity in comparison to wild-type enzyme
V239L
t1/2 of mutant enzyme at 70°C is 103 min, compared to 15 min for wild-type enzyme. Mutation does not compromise the catalytic activity
V374I
t1/2 of mutant enzyme at 70°C is 14 min, compared to 15 min for wild-type enzyme. Mutation does not compromise the catalytic activity
V404L
t1/2 of mutant enzyme at 70°C is 191 min, compared to 15 min for wild-type enzyme. Mutation does not compromise the catalytic activity
V533L
t1/2 of mutant enzyme at 70°C is 8 min, compared to 15 min for wild-type enzyme. Mutation does not compromise the catalytic activity
Y377D
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mutation decreases transglycosylation activity in comparison to wild-type enzyme
Y377F
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mutation increases transglycosylation activity in comparison to wild-type enzyme
Y377S
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mutation decreases transglycosylation activity in comparison to wild-type enzyme
I358V
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mutation decreases the preference for alpha(1-6)-branched oligosaccharides and pullulan as substrates
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I358W
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mutation reduces the acceptability of alpha(1-6)-branched oligo- and polysaccharides
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M375L
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mutation increases transglycosylation activity in comparison to wild-type enzyme
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S422V
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mutation increases transglycosylation activity in comparison to wild-type enzyme
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Y377F
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mutation increases transglycosylation activity in comparison to wild-type enzyme
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I358V
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site-directed mutagenesis, the mutant shows increased activity hydrolyzing alpha-1,6-glucosidic bonds, producing maltotriose, compared to the wild-type enzyme
I358W
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site-directed mutagenesis, the mutant shows decreased activity hydrolyzing alpha-1,6-glucosidic bonds, producing maltotriose, compared to the wild-type enzyme
I358V
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site-directed mutagenesis, the mutant shows increased activity hydrolyzing alpha-1,6-glucosidic bonds, producing maltotriose, compared to the wild-type enzyme
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I358W
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site-directed mutagenesis, the mutant shows decreased activity hydrolyzing alpha-1,6-glucosidic bonds, producing maltotriose, compared to the wild-type enzyme
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additional information
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diverse mutants are constructed and specific activities, sugar compositions of pullulan hydrolysate and hydrolysis activities toward alpha-(1-4) and alpha-(1-6)-glucosidic linkages analyzed
additional information
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diverse mutants are constructed and specific activities, sugar compositions of pullulan hydrolysate and hydrolysis activities toward alpha-(1-4) and alpha-(1-6)-glucosidic linkages analyzed
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additional information
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knockout variant through insertion in gene apuB that is encoding for amylopullulanase: no growth on starch, amylopectin, glycogen, or pullulan
additional information
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knockout variant through insertion in gene apuB that is encoding for amylopullulanase: no growth on starch, amylopectin, glycogen, or pullulan
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additional information
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C-terminal truncated ApuA produced with Escherichia coli plasmid, and transformed into Lactobacillus plantarum
additional information
Lactiplantibacillus plantarum ATCC BAA-793
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C-terminal truncated ApuA produced with Escherichia coli plasmid, and transformed into Lactobacillus plantarum
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additional information
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mutation of residues A357, Q359, and Y360X also leads to increased activity hydrolyzing alpha-1,6-glucosidic bonds, producing maltotriose
additional information
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mutation of residues A357, Q359, and Y360X also leads to increased activity hydrolyzing alpha-1,6-glucosidic bonds, producing maltotriose
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additional information
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R855 C-terminal truncated (100 amino acids) mutant R855 of full length TetApuM955, produced with trypsin-like proteolytic cleavage reaction
additional information
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R855 C-terminal truncated (100 amino acids) mutant R855 of full length TetApuM955, produced with trypsin-like proteolytic cleavage reaction
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