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
-
maltogenic
- amylopectin
-
transglycosylation
- amylose
-
alpha-1,4
- amylopullulanase
-
debranching
- oligo-1,6-glucosidase
-
glucanotransferase
-
thermoactinomyces
-
alpha-1,6-glucosidic
- isopanose
-
cdase
-
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
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Subunits
Subunits on EC 3.2.1.135 - neopullulanase
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dimer
monomer
additional information
dimer
the active enzyme forms a dimer in the crystalline states and in solution
dimer
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the active enzyme forms a dimer in the crystalline states and in solution
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analysis of conserved regions in the enzyme primary structure, overview
additional information
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analysis of conserved regions in the enzyme primary structure, overview
additional information
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analysis of conserved regions in the enzyme primary structure, overview
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additional information
enzyme likely to be present in monomer-dimer equilibrium with a molecular ratio of 1:9 in 50 mM sodium acetate buffer, pH 6.0, x * 65000, SDS-PAGE, x * 70156, MALDI-TOF MS analyzis
additional information
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enzyme likely to be present in monomer-dimer equilibrium with a molecular ratio of 1:9 in 50 mM sodium acetate buffer, pH 6.0, x * 65000, SDS-PAGE, x * 70156, MALDI-TOF MS analyzis
additional information
-
analysis of conserved regions in the enzyme primary sequence, overview
additional information
-
enzyme likely to be present in monomer-dimer equilibrium with a molecular ratio of 1:9 in 50 mM sodium acetate buffer, pH 6.0, x * 65000, SDS-PAGE, x * 70156, MALDI-TOF MS analyzis
-
additional information
-
analysis of conserved regions in the enzyme primary structure, overview
additional information
-
analysis of conserved regions in the enzyme primary sequence, overview
additional information
-
analysis of conserved regions in the enzyme primary sequence, overview
-