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EC Tree
IUBMB Comments Converts amylose into amylopectin. The accepted name requires a qualification depending on the product, glycogen or amylopectin, e.g. glycogen branching enzyme, amylopectin branching enzyme. The latter has frequently been termed Q-enzyme.
The taxonomic range for the selected organisms is: Deinococcus geothermalis The enzyme appears in selected viruses and cellular organisms
Synonyms
gbe, branching enzyme, sbeiib, glycogen branching enzyme, starch branching enzyme, sbeiia, beiib, sbeii, starch-branching enzyme, beiia,
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1,4-alpha-glucan branching enzyme
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glycogen branching enzyme
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alpha-1,4-glucan:alpha-1,4-glucan 6-glycosyltransferase
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alpha-1,4-glucan:alpha-1,4-glucan-6-glycosyltransferase
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alpha-glucan-branching glycosyltransferase
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amylo-(1,4-1,6)-transglycosylase
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amylose isomerase
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branching factor, enzymatic
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branching glycosyltransferase
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glucosan transglycosylase
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glycogen branching enzyme
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glycosyltransferase, alpha-glucan-branching
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starch branching enzyme
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glycosyl group transfer
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(1->4)-alpha-D-glucan:(1->4)-alpha-D-glucan 6-alpha-D-[(1->4)-alpha-D-glucano]-transferase
Converts amylose into amylopectin. The accepted name requires a qualification depending on the product, glycogen or amylopectin, e.g. glycogen branching enzyme, amylopectin branching enzyme. The latter has frequently been termed Q-enzyme.
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amylopectin
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iodine assay
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amylose
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branching assay, at pH 8.0, reaction stopped by boiling for 5 min
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amylose
branched polyglucan
using linear amylose synthesized in a tandem reaction by potato phosphorylase
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?
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7.2
wild-type enzyme, branching assay
additional information
specific activity on amylopectin 342.3 U/mg, 1 U = decrease in absorbance of 1.0 per min at 530 nm, mutant RGG, iodine assay
additional information
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specific activity on amylopectin 342.3 U/mg, 1 U = decrease in absorbance of 1.0 per min at 530 nm, mutant RGG, iodine assay
additional information
specific activity on amylopectin 359.2 U/mg, 1 U = decrease in absorbance of 1.0 per min at 530 nm, mutant GGR, iodine assay
additional information
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specific activity on amylopectin 359.2 U/mg, 1 U = decrease in absorbance of 1.0 per min at 530 nm, mutant GGR, iodine assay
additional information
specific activity on amylopectin 474.3 U/mg, 1 U = decrease in absorbance of 1.0 per min at 530 nm, wild-type enzyme, iodine assay
additional information
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specific activity on amylopectin 474.3 U/mg, 1 U = decrease in absorbance of 1.0 per min at 530 nm, wild-type enzyme, iodine assay
additional information
specific activity on amylopectin 505.6 U/mg, 1 U = decrease in absorbance of 1.0 per min at 530 nm, mutant RRG, iodine assay
additional information
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specific activity on amylopectin 505.6 U/mg, 1 U = decrease in absorbance of 1.0 per min at 530 nm, mutant RRG, iodine assay
additional information
specific activity on amylopectin less than 0.5 U/mg, 1 U = decrease in absorbance of 1.0 per min at 530 nm, mutant GRR, iodine assay
additional information
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specific activity on amylopectin less than 0.5 U/mg, 1 U = decrease in absorbance of 1.0 per min at 530 nm, mutant GRR, iodine assay
additional information
specific activity on amylose 411.7 U/mg, 1 U = decrease in absorbance of 1.0 per min at 660 nm, mutant RRG, iodine assay
additional information
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specific activity on amylose 411.7 U/mg, 1 U = decrease in absorbance of 1.0 per min at 660 nm, mutant RRG, iodine assay
additional information
specific activity on amylose 468.8 U/mg, 1 U = decrease in absorbance of 1.0 per min at 660 nm, mutant GGR, iodine assay
additional information
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specific activity on amylose 468.8 U/mg, 1 U = decrease in absorbance of 1.0 per min at 660 nm, mutant GGR, iodine assay
additional information
specific activity on amylose 621.3 U/mg, 1 U = decrease in absorbance of 1.0 per min at 660 nm, wild-type enzyme, iodine assay
additional information
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specific activity on amylose 621.3 U/mg, 1 U = decrease in absorbance of 1.0 per min at 660 nm, wild-type enzyme, iodine assay
additional information
specific activity on amylose 624.1 U/mg, 1 U = decrease in absorbance of 1.0 per min at 660 nm, mutant RGG, iodine assay
additional information
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specific activity on amylose 624.1 U/mg, 1 U = decrease in absorbance of 1.0 per min at 660 nm, mutant RGG, iodine assay
additional information
specific activity on amylose less than 0.5 U/mg, 1 U = decrease in absorbance of 1.0 per min at 660 nm, mutant GRR, iodine assay
additional information
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specific activity on amylose less than 0.5 U/mg, 1 U = decrease in absorbance of 1.0 per min at 660 nm, mutant GRR, iodine assay
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8
iodine assay
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tandem reaction with potato phosphorylase at pH 7.0
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34
iodine assay
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tandem reaction with potato phosphorylase at 38°C
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UniProt
brenda
strain DSM 11300
UniProt
brenda
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brenda
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additional information
CT Dg, truncated at 3' end
additional information
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CT Dg, truncated at 3' end
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
NT Dg, tuncated at 5' end
additional information
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NT Dg, tuncated at 5' end
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
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60 - 65
after 1 h incubation at 60°C fully active, after 1 h incubation at 65°C only 80% residual activity
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His tag affinity chromatography
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expression in Escherichia coli BL21
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Palomo, M.; Kralj, S.; van der Maarel, M.J.; Dijkhuizen, L.
The unique branching patterns of Deinococcus glycogen branching enzymes are determined by their N-terminal domains
Appl. Environ. Microbiol.
75
1355-1362
2009
Deinococcus geothermalis (Q1IZQ3), Deinococcus geothermalis, Deinococcus radiodurans (Q9RTB7), Deinococcus radiodurans, Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539 (Q9RTB7)
brenda
Van Der Vlist, J.; Reixach, M.; Van Der Maarel, M.; Dijkhuizen, L.; Schouten, A.; Loos, K.
Synthesis of branched polyglucans by the tandem action of potato phosphorylase and deinococcus geothermalis glycogen branching enzyme
Macromol. Rapid Commun.
29
1293-1297
2008
Deinococcus geothermalis (Q1IZQ3)
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brenda