2.4.1.18: 1,4-alpha-glucan branching enzyme
This is an abbreviated version!
For detailed information about 1,4-alpha-glucan branching enzyme, go to the full flat file.
Word Map on EC 2.4.1.18
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2.4.1.18
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biloba
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ginkgo
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amylopectin
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endosperm
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maize
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grain
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pyrophosphorylase
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phosphorylase
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granule-bound
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glucans
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potato
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debranching
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polysaccharide
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polyglucosan
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herbal
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ssiia
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ginkgolide
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kernel
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gelatin
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waxy
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glycogenosis
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amyloplasts
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pullulanase
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andersen
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dextrin
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isoamylase
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bilobalide
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agpase
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high-amylose
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amylolytic
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chain-length
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lafora
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rhodothermus
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biotechnology
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medicine
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adpglucose
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glycogenin
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food industry
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nutrition
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diastase-resistant
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alpha-glucans
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drug development
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pas-positive
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isorhamnetin
- 2.4.1.18
- biloba
- ginkgo
- amylopectin
- endosperm
- maize
- grain
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pyrophosphorylase
- phosphorylase
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granule-bound
- glucans
- potato
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debranching
- polysaccharide
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polyglucosan
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herbal
- ssiia
-
ginkgolide
- kernel
- gelatin
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waxy
- glycogenosis
- amyloplasts
- pullulanase
- andersen
- dextrin
- isoamylase
- bilobalide
- agpase
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high-amylose
-
amylolytic
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chain-length
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lafora
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rhodothermus
- biotechnology
- medicine
- adpglucose
- glycogenin
- food industry
- nutrition
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diastase-resistant
- alpha-glucans
- drug development
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pas-positive
- isorhamnetin
Reaction
2 1,4-alpha-D-glucan
=
Synonyms
(1-4)-alpha-D-glucan:(1-4)-alpha-D-glucan 6-alpha-D-[(1-4)-alpha-D-glucano]-transferase, 1,4-alpha-glucan branching enzyme, 1,4-alpha-glucan branching enzyme 1, AGBE, alpha-1,4->alpha-1,6-glycosyltransferase, alpha-1,4-glucan branching enzyme, alpha-1,4-glucan:alpha-1,4-glucan 6-glycosyltransferase, alpha-1,4-glucan:alpha-1,4-glucan-6-glycosyltransferase, alpha-glucan branching enzyme, alpha-glucan-branching glycosyltransferase, amylo-(1,4-1,6)-transglycosylase, amylo-(1,4->1,6)-transglycosylase, amylose isomerase, BBE, BE, BE-01, BE-02, BE-II, BE1, BE2, BE3, BEI, BEII, BEIIa, BEIIb, BGE, branching enzyme, branching factor, enzymatic, branching glycosyltransferase, ChlBE, Dg GBE, Dr GBE, enzyme Q, full-length starch branching enzyme II, GBE, GBE1, GBE1 enzyme, GH13 GBE, GH57-type glycogen branching enzyme, GlgB, glucan transferase, glucosan transglycosylase, glycogen branching enzyme, glycogen branching enzyme GBE1, glycosyltransferase, alpha-glucan-branching, HosBE, IbSBEI, mSBEIIa, ORF Rv1326c, PH1386, PhGBE, PvSBE1, PvSBE2, Q-enzyme, QE, rBEI, rice branching enzyme I, RMEBE, RoBE, SBE, SBE A, SBE B, SBE I, SBE IIa, SBE Iib, SBE-I, SBE1, SBEI, SBEII, SBEIIA, SBEIIB, ScoBE, SmGBE, starch branching enzyme, starch branching enzyme I, starch branching enzyme II, starch branching enzyme IIa, starch branching enzyme IIb, starch branching enzyme SBE I, starch branching enzyme SBE IIb, starch branching enzyme-I, starch-branching enzyme, starch-branching enzyme Ia, starch-branching enzyme IIa, starch-branching enzyme IIb, starch-branching enzymes IIa, starch-branching enzymes IIb, starch-branching-enzyme, TK1436, VsbeII
ECTree
2.4.1.18 1,4-alpha-glucan branching enzymeAdvanced search results
results (
results (Engineering
Engineering on EC 2.4.1.18 - 1,4-alpha-glucan branching enzyme
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
DELTA1-112
DELTA1-63
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the wild-type enzyme transfers mainly chains with a degree of polymerization of 8-14, mutant enzyme has a pattern of transferred chains, 10-20
DELTA1-83
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the wild-type enzyme transfers mainly chains with a degree of polymerization of 8-14, mutant enzyme has a pattern of transferred chains, 10-20
truncated enzyme form missing the first 107 amino-
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the purified full-length enzyme is poorly soluble and forms aggregates, which are inactive, at concentrations above 1 mg/ml. In contrast, the truncated form can be concentrated to 6 mg/ml without a visible signs of aggregation or loss of activity on concentration
Y300F
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mutant enzyme shows 25% of the wild-type activity, no effect on Km-value, heat stability is lowered significantly compared to that of the wild-type enzyme, lower relative activity at elevated temperatures compared to wild-type enzyme
D270A
mutant with about 10% relative enzyme activity compared to wild-type enzyme
E399A
mutant with about 5% relative enzyme activity compared to wild-type enzyme
G468D
mutant with about 95% relative enzyme activity compared to wild-type enzyme
R342A
mutant with about 15% relative enzyme activity compared to wild-type enzyme
Y235A
mutant with about 15% relative enzyme activity compared to wild-type enzyme
A310D
the mutant shows strongly reduced activity compared to the wild type enzyme
A310E
the mutant shows strongly reduced activity compared to the wild type enzyme
A310G
the mutant shows strongly reduced activity compared to the wild type enzyme
A310I
the mutant shows strongly reduced activity compared to the wild type enzyme
A310N
the mutant shows strongly reduced activity compared to the wild type enzyme
A310Q
the mutant shows strongly reduced activity compared to the wild type enzyme
I571D
the mutant shows increased thermostability and activity nearly identical to that of the wild type enzyme
M349H
the mutant shows a slight decrease in specific activity compared with that of wild type enzyme
M349S
the mutant shows 21.1% increase in specific activity compared with that of wild type enzyme. The mutant displays 24.2% enhancement in the alpha-1,6-glycosidic linkage ratio of potato starch samples
M349T
the mutant shows 24.5% increase in specific activity compared with that of wild type enzyme. The mutant displays 24.2% enhancement in the alpha-1,6-glycosidic linkage ratio of potato starch samples
M349Y
the mutant displays a significant (33.9%) reduction in specific activity compared with that of wild type enzyme
Q231K
the mutant shows increased thermostability and activity nearly identical to that of the wild type enzyme
Q231R
the mutant shows increased thermostability and activity nearly identical to that of the wild type enzyme
T339D
the mutant shows increased thermostability and activity nearly identical to that of the wild type enzyme
T339E
the mutant shows increased thermostability and activity nearly identical to that of the wild type enzyme
A310D
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the mutant shows strongly reduced activity compared to the wild type enzyme
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A310E
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the mutant shows strongly reduced activity compared to the wild type enzyme
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A310G
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the mutant shows strongly reduced activity compared to the wild type enzyme
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A310N
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the mutant shows strongly reduced activity compared to the wild type enzyme
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A310Q
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the mutant shows strongly reduced activity compared to the wild type enzyme
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I571D
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the mutant shows increased thermostability and activity nearly identical to that of the wild type enzyme
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M349H
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the mutant shows a slight decrease in specific activity compared with that of wild type enzyme
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M349S
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the mutant shows 21.1% increase in specific activity compared with that of wild type enzyme. The mutant displays 24.2% enhancement in the alpha-1,6-glycosidic linkage ratio of potato starch samples
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M349T
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the mutant shows 24.5% increase in specific activity compared with that of wild type enzyme. The mutant displays 24.2% enhancement in the alpha-1,6-glycosidic linkage ratio of potato starch samples
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M349Y
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the mutant displays a significant (33.9%) reduction in specific activity compared with that of wild type enzyme
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Q231K
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the mutant shows increased thermostability and activity nearly identical to that of the wild type enzyme
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Q231R
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the mutant shows increased thermostability and activity nearly identical to that of the wild type enzyme
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T339D
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the mutant shows increased thermostability and activity nearly identical to that of the wild type enzyme
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T339E
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the mutant shows increased thermostability and activity nearly identical to that of the wild type enzyme
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D15A
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D15A-PvSBE2 enzyme shows 13.1% of the specific activity of the wild type enzyme. The large decrease in the specific activities of the mutant is predominatly attributed to the reduced Vmax value.
D15E
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D15E-PvSBE2 enzyme shows 31.3% of the specific activity of the wild type enzyme. The large decrease in the specific activities of the mutant is predominatly attributed to the reduced Vmax value.
H24A
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H24A-PvSBE2 enzyme shows 38.3% of the specific activity of the wild type enzyme. The large decrease in the specific activities of the mutant is predominatly attributed to the reduced Vmax value.
R28A
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R28A-PvSBE2 enzyme shows 10.7% of the specific activity of the wild type enzyme. The large decrease in the specific activities of the mutant is predominatly attributed to the reduced Vmax value.
R28K
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R28K-PvSBE2 enzyme shows 93.5% of the specific activity of the wild type enzyme.
delN238-S247
loop-truncated mutant exhibits a 2-fold increase in activity relative to the wild type enzyme. The branching activity of the deletion variant is decreased. In the wild type enzyme, the degree of polymerization of the reaction products has peaks ranging from 7 to 12, while the loop-truncated mutant has peaks in the range of degree of polymerization 10 to 13, indicating that the chain lengths of the reaction products are slightly longer than that of the wild type enzyme. The flexible loop is associated with the catalytic process of GH57 glycogen branching enzymes and plays an important role in the branching activity and the variable lengths of the branches
E513D
site-directed mutagenesis, the mutant shows a much lower activity compared to wild-type enzyme mSBEIIa
R363K
site-directed mutagenesis, the mutant shows similar activity as the wild-type enzyme mSBEIIa
R456K
site-directed mutagenesis, the mutant shows similar activity compared to wild-type enzyme mSBEIIa
S349F
site-directed mutagenesis, creates an additional binding site for glucose, the mutant shows a much lower activity compared to wild-type enzyme mSBEIIa
Y352F
site-directed mutagenesis, , the mutant shows a much lower activity compared to wild-type enzyme mSBEIIa
additional information
DELTA1-112
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the wild-type enzyme transfers mainly chains with a degree of polymerization of 8-14, the mutant enzyme DELTA1-112 transfers a greater propertion of chains with higher degree of polymerization, 15-20
DELTA1-112
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truncated enzyme transferrs a greater amount of longer chains than the wild-type enzyme
additional information
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be1-1 (DYK140), T-DNA insertion mutant line for BE1. The amount of amylose and the branching level of amylopectin are not significantly different in the mutants when compared with the wild type.
additional information
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be1-1 be2-1, T-DNA insertion double mutant in enzyme BE1 and BE2. The amount of amylose and the branching level of amylopectin are not significantly different in the mutants when compared with the wild type.
additional information
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be1-1 be3-2, T-DNA insertion double mutant in enzyme BE1 and BE3. The amount of amylose and the branching level of amylopectin are not significantly different in the mutants when compared with the wild type.
additional information
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be1-2 (N637880), T-DNA insertion mutant line for BE1. The amount of amylose and the branching level of amylopectin are not significantly different in the mutants when compared with the wild type.
additional information
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be2-1 (EFH20), T-DNA insertion mutant line for BE2. The amount of amylose and the branching level of amylopectin are not significantly different in the mutants when compared with the wild type.
additional information
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be2-1 be3-2, T-DNA insertion double mutant in enzyme BE2 and BE3. The amount of amylose and the branching level of amylopectin are not significantly different in the mutants when compared with the wild type. The be2-1 be3-2 double mutant is free of starch, coupled with an accumulation of very high levels of water-soluble glucans, that are not observable in other lines. Moreover, this double mutant displays a lower growth rate, a pale color and a general wilting of the inflorescence.
additional information
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be2-2 (DSA16), T-DNA insertion mutant line for BE2. The amount of amylose and the branching level of amylopectin are not significantly different in the mutants when compared with the wild type.
additional information
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be3-1 (N548089), T-DNA insertion mutant line for BE3. The amount of amylose and the branching level of amylopectin are not significantly different in the mutants when compared with the wild type.
additional information
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be3-2 (EQJ13), T-DNA insertion mutant line for BE3. The amount of amylose and the branching level of amylopectin are not significantly different in the mutants when compared with the wild type.
additional information
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production of highly branched amylopectin and amylose from rice starch in a multistep procedure using several different enzymes, for braching of amylose, the Bacillus subtilis 168 branching enzyme is used, analysis of the resulting structural changes, overview
additional information
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production of highly branched amylopectin and amylose from rice starch in a multistep procedure using several different enzymes, for braching of amylose, the Bacillus subtilis 168 branching enzyme is used, analysis of the resulting structural changes, overview
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additional information
enzyme overexpression results in decrease cell proliferation when treated by deltamethrin
additional information
enzyme overexpression results in decrease cell proliferation when treated by deltamethrin
additional information
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enzyme overexpression results in decrease cell proliferation when treated by deltamethrin
additional information
GGR, construction of chimeric genes, with C-domain of GBE of Deinococcus radiodurans
additional information
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GGR, construction of chimeric genes, with C-domain of GBE of Deinococcus radiodurans
additional information
GRR, construction of chimeric genes, with A-domain and C-domain of GBE of Deinococcus radiodurans
additional information
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GRR, construction of chimeric genes, with A-domain and C-domain of GBE of Deinococcus radiodurans
additional information
RGG, construction of chimeric genes, with N-domain of GBE of Deinococcus radiodurans
additional information
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RGG, construction of chimeric genes, with N-domain of GBE of Deinococcus radiodurans
additional information
RRG, construction of chimeric genes, with N-domain and A-domain of GBE of Deinococcus radiodurans
additional information
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RRG, construction of chimeric genes, with N-domain and A-domain of GBE of Deinococcus radiodurans
additional information
GGR, construction of chimeric genes, with N-domain and A-domain of GBE of Deinococcus geothermalis
additional information
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GGR, construction of chimeric genes, with N-domain and A-domain of GBE of Deinococcus geothermalis
additional information
GRR, construction of chimeric genes, with N-domain of GBE of Deinococcus geothermalis
additional information
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GRR, construction of chimeric genes, with N-domain of GBE of Deinococcus geothermalis
additional information
RGG, construction of chimeric genes, with A-domain and C-domain of GBE of Deinococcus geothermalis
additional information
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RGG, construction of chimeric genes, with A-domain and C-domain of GBE of Deinococcus geothermalis
additional information
RRG, construction of chimeric genes, with C-domain of GBE of Deinococcus geothermalis
additional information
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RRG, construction of chimeric genes, with C-domain of GBE of Deinococcus geothermalis
additional information
Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539
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CTT Dr, tuncated at 3' end
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additional information
Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539
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GGR, construction of chimeric genes, with N-domain and A-domain of GBE of Deinococcus geothermalis
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additional information
Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539
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GRR, construction of chimeric genes, with N-domain of GBE of Deinococcus geothermalis
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additional information
Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539
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RGG, construction of chimeric genes, with A-domain and C-domain of GBE of Deinococcus geothermalis
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additional information
Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539
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RRG, construction of chimeric genes, with C-domain of GBE of Deinococcus geothermalis
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additional information
concominant reduction in SBE IIb with suppression of SBE IIa
additional information
concominant reduction in SBE IIb with suppression of SBE IIa
additional information
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concominant reduction in SBE IIb with suppression of SBE IIa
additional information
SBE IIa-, transgenic line with suppressed SBE IIa
additional information
SBE IIa-, transgenic line with suppressed SBE IIa
additional information
SBE IIa-/SBE IIb-, transgenic line with suppressed SBE IIb and suppressed SBE IIa
additional information
SBE IIa-/SBE IIb-, transgenic line with suppressed SBE IIb and suppressed SBE IIa
additional information
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SBE IIa-/SBE IIb-, transgenic line with suppressed SBE IIb and suppressed SBE IIa
additional information
SBE IIb-, transgenic line with suppressed SBE IIb
additional information
SBE IIb-, transgenic line with suppressed SBE IIb
additional information
suppression of SBE IIa with concominant reduction in SBE IIb
additional information
suppression of SBE IIa with concominant reduction in SBE IIb
additional information
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suppression of SBE IIa with concominant reduction in SBE IIb
additional information
a mutant lacking the N1 domain, i.e. lacking N-terminal residues 1-108, shows about 30% decrease in specific activity
additional information
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a mutant lacking the N1 domain, i.e. lacking N-terminal residues 1-108, shows about 30% decrease in specific activity
additional information
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a mutant lacking the N1 domain, i.e. lacking N-terminal residues 1-108, shows about 30% decrease in specific activity
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additional information
compared with the wild type enzyme, a truncation mutant made by removing the last 26 residues from its C-terminal end has enhanced thermostability and recovery ability without compromising enzymatic activity
additional information
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compared with the wild type enzyme, a truncation mutant made by removing the last 26 residues from its C-terminal end has enhanced thermostability and recovery ability without compromising enzymatic activity
additional information
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compared with the wild type enzyme, a truncation mutant made by removing the last 26 residues from its C-terminal end has enhanced thermostability and recovery ability without compromising enzymatic activity
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additional information
construction of chimeric enzymes of the isoenzymes PvSBE1 and PvSBE2
additional information
construction of chimeric enzymes of the isoenzymes PvSBE1 and PvSBE2
additional information
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chimeric enzymes of PvSBE2: only one chimeric recombinant protein ((I Na/2Nb)-II) has enzyme activity. It shows 6.1% of the specific activity of the wild type enzyme.
additional information
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N-termial truncated enzyme of PvSBE2. Delta46-PvSBE2 has no branching enzyme activity.
additional information
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starch from tubers of enzyme overexpressing plants posses an increased degree of amylopectin branching, with more short chains of degree of polymerisation (DP) 6-12 and particularly of DP6. Construction of transgenic lines expressing a GRANULE-BOUND STARCH SYNTHASE (GBSS) RNAi, which exhibit post-transcriptional gene silencing of GBSS and reduced amylose content in the starch. Both transgenic modifications do not affect granule morphology but reduce starch peak viscosity. In starch from SBEII-overexpressing lines, the increased ratio of short to long amylopectin branches facilitates gelatinisation, which occurs at a reduced temperature (by up to 3°C) or lower urea concentration. In contrast, silencing of GBSS increases the gelatinisation temperature by 4°C, and starch requires a higher urea concentration for gelatinisation. In lines with a range of SBEII overexpression, the magnitude of the increase in SBEII activity, reduction in onset of gelatinisation temperature and increase in starch swollen pellet volume are highly correlated, consistent with reports that starch swelling is greatly dependent upon the amylopectin branching pattern. Amylose content in starch and thermal properties of tuber starch granules from potato tubers of a range of lines exhibiting silencing of GBSS or overexpressing SBEII, overview
additional information
recombinant TK1436 protein (amino acids [aa] 1 to 675) and a deletion derivative devoid of the C-terminal two-copy helix-hairpin-helix (HhH)2 motif (TK1436deltaH, aa 1 to 562)
additional information
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construction of domain-truncated (N1 and N) and N1-domain-swapped (with VvGBE N1 replacing the counter part of Escherichia coli GBE) mutants. The truncation mutants synthesize branched products with a greatly reduced proportion of short chains compared to the wild-type. The swapping mutant exhibit a branching pattern of the short chain region similar to that of the ewild-type enzyme
additional information
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construction of domain-truncated (N1 and N) and N1-domain-swapped (with VvGBE N1 replacing the counter part of Escherichia coli GBE) mutants. The truncation mutants synthesize branched products with a greatly reduced proportion of short chains compared to the wild-type. The swapping mutant exhibit a branching pattern of the short chain region similar to that of the ewild-type enzyme
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additional information
application of RNAi technology for improving amylose content in maize endosperm through the suppression of the ZmSBEIIa and ZmSBEIIb genes by hairpin SBEIIRNAi constructs. These SBEIIRNAi transgenes lead to the downregulation of ZmSBEII expression and SBE activity to various degrees and altered the morphology of starch granule
additional information
application of RNAi technology for improving amylose content in maize endosperm through the suppression of the ZmSBEIIa and ZmSBEIIb genes by hairpin SBEIIRNAi constructs. These SBEIIRNAi transgenes lead to the downregulation of ZmSBEII expression and SBE activity to various degrees and altered the morphology of starch granule
additional information
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application of RNAi technology for improving amylose content in maize endosperm through the suppression of the ZmSBEIIa and ZmSBEIIb genes by hairpin SBEIIRNAi constructs. These SBEIIRNAi transgenes lead to the downregulation of ZmSBEII expression and SBE activity to various degrees and altered the morphology of starch granule
additional information
construction of enzyme point mutants by site-directed mutagenesis to change the chain-length distribution CLD by changing activity of enzyme SBE. The enzyme mutants show no or only a slight change in degree of polymerization of branched glucans
additional information
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construction of enzyme point mutants by site-directed mutagenesis to change the chain-length distribution CLD by changing activity of enzyme SBE. The enzyme mutants show no or only a slight change in degree of polymerization of branched glucans
additional information
generation of N- and C-terminally truncated enzyme mutants. Activities of kinases on wild-type and enzyme mutants, overview
additional information
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generation of N- and C-terminally truncated enzyme mutants. Activities of kinases on wild-type and enzyme mutants, overview
additional information
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generation of N- and C-terminally truncated enzyme mutants. Activities of kinases on wild-type and enzyme mutants, overview
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