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
-
2.4.1.18
-
biloba
-
ginkgo
-
amylopectin
-
endosperm
-
maize
-
grain
-
pyrophosphorylase
-
phosphorylase
-
granule-bound
-
glucans
-
potato
-
debranching
-
polysaccharide
-
polyglucosan
-
herbal
-
ssiia
-
ginkgolide
-
kernel
-
gelatin
-
waxy
-
glycogenosis
-
amyloplasts
-
pullulanase
-
andersen
-
dextrin
-
isoamylase
-
bilobalide
-
agpase
-
high-amylose
-
amylolytic
-
chain-length
-
lafora
-
rhodothermus
-
biotechnology
-
medicine
-
adpglucose
-
glycogenin
-
food industry
-
nutrition
-
diastase-resistant
-
alpha-glucans
-
drug development
-
pas-positive
-
isorhamnetin
- 2.4.1.18
- biloba
- ginkgo
- amylopectin
- endosperm
- maize
- grain
-
pyrophosphorylase
- phosphorylase
-
granule-bound
- glucans
- potato
-
debranching
- polysaccharide
-
polyglucosan
-
herbal
- ssiia
-
ginkgolide
- kernel
- gelatin
-
waxy
- glycogenosis
- amyloplasts
- pullulanase
- andersen
- dextrin
- isoamylase
- bilobalide
- agpase
-
high-amylose
-
amylolytic
-
chain-length
-
lafora
-
rhodothermus
- biotechnology
- medicine
- adpglucose
- glycogenin
- food industry
- nutrition
-
diastase-resistant
- alpha-glucans
- drug development
-
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 (Substrates Products
Substrates Products on EC 2.4.1.18 - 1,4-alpha-glucan branching enzyme
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
amylose
branched polyglucan
using linear amylose synthesized in a tandem reaction by potato phosphorylase
-
-
?
beta-cyclodextrin
?
22.82% activity compared to amylose
-
-
?
high-amylose corn starch
high-amylose corn starch containing alpha-1,6-glucosidic linkages
pea starch
pea starch containing alpha-1,6-glucosidic linkages
28.55% activity compared to amylose
-
-
?
potato amylopectin type III
potato amylopectin type III containing alpha-1,6-glucosidic linkages
wheat starch
wheat starch containing alpha-1,6-glucosidic linkages
30.56% activity compared to amylose
-
-
?
amylopectin
?
-
-
the amount of short chains with a degree of polymerization of 6-8 is significantly increased in the product of Bacillus cereus
-
?
amylopectin
?
-
-
enzyme efficiently cyclizes the inner chain of amylopectin to degrade the molecule. The degradation stopps when the molecular mass of the product reaches about 150 kDa
-
?
amylopectin
?
assay at 30°C, reaction terminated by heating at 95°C for 5 min
-
-
?
amylopectin
?
-
-
enzyme catalyzes cyclization of amylopectin, the amount of short chains with a degree of polymerization of 6-8 is significantly increased compared to reaction products of Bacillus stearothermophilus enzyme
-
?
amylopectin
amylopectin containing alpha-1,6-glucosidic linkages
-
-
-
?
amylopectin
amylopectin containing alpha-1,6-glucosidic linkages
-
-
-
?
amylopectin
amylopectin containing alpha-1,6-glucosidic linkages
-
-
-
?
amylopectin
amylopectin containing alpha-1,6-glucosidic linkages
61.16% activity compared to amylose
-
-
?
amylopectin
amylopectin containing alpha-1,6-glucosidic linkages
-
-
-
?
amylopectin
amylopectin containing alpha-1,6-glucosidic linkages
-
-
-
-
?
amylopectin
amylopectin containing alpha-1,6-glucosidic linkages
-
-
-
?
amylopectin
amylopectin containing alpha-1,6-glucosidic linkages
-
-
-
?
amylopectin
amylopectin containing alpha-1,6-glucosidic linkages
-
-
-
?
amylopectin
amylopectin with additional alpha-1,6-glucosidic linkages
-
the enzyme cyclizes the B-chain which connects the cluster structures of amylopectin. The product, highly branched cyclic dextrin, has a ring structure with DPw 50 and non-cyclic chains with an average unit chain length of 16 connected to the ring
-
-
?
amylopectin
amylopectin with additional alpha-1,6-glucosidic linkages
-
-
-
-
?
amylopectin
amylopectin with additional alpha-1,6-glucosidic linkages
-
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. Mutant DELTA1-63 and mutant DELTA1-83 have an intermediate pattern of transferred chains, 10-20. A progressive shortening of the N-terminus leads to a gradual increase in the length of the transferred chains
-
-
?
amylopectin
amylopectin with additional alpha-1,6-glucosidic linkages
-
-
-
?
amylopectin
amylopectin with additional alpha-1,6-glucosidic linkages
the C-terminal regions of isoenzyme PvSBE1 and PvSBE2 have different roles in branching enzyme activity. The C-terminal region of PvSBE1 confers specificity to amylose while that of PvSBE2 confers specificity to the transfer of short chains
-
-
?
amylopectin
amylopectin with additional alpha-1,6-glucosidic linkages
-
-
-
-
?
amylopectin
amylopectin with additional alpha-1,6-glucosidic linkages
-
enzyme form SBE II is more active than enzyme form SBE I. The enzyme forms SBE I and SBE II mainly branch the dextrins by intrachain branching.The products of SBE I show distinct populations at DP11-12 and DP29-30. The products of enzyme form SBE II habe one, broader, population with a peak at DP13-14. An accumulation of 6-7 chains is seen with both isoforms
-
-
?
amylopectin
amylopectin with additional alpha-1,6-glucosidic linkages
-
-
-
-
?
amylose
?
branching assay, at pH 8.0, reaction stopped by boiling for 5 min
-
-
?
amylose
?
branching assay, at pH 8.0, reaction stopped by boiling for 5 min
-
-
?
amylose
?
Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539
branching assay, at pH 8.0, reaction stopped by boiling for 5 min
-
-
?
amylose
?
assay at 30°C, reaction terminated by heating at 95°C for 5 min
-
-
?
amylose
?
the glycogen branching enzyme catalyzes the formation of alpha-1,6-branching points during glycogenesis by cleaving alpha-1,4 bonds and making new alpha-1,6 bonds. 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 enzyme has peaks in the range of degree of polymerization of 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
-
-
?
amylose
amylose containing alpha-1,6-glucosidic linkages
-
-
-
?
amylose
amylose containing alpha-1,6-glucosidic linkages
-
-
-
?
amylose
amylose containing alpha-1,6-glucosidic linkages
-
-
characterization of products, smallest chains transferred contain 5-7 glucose units
?
amylose
amylose containing alpha-1,6-glucosidic linkages
-
wild-type enzyme and mutant enzyme Y300F both preferentially transfer chains between DP5 and DP16, with a chain of DP11 being transferred at the highest frequency
-
-
?
amylose
amylose containing alpha-1,6-glucosidic linkages
-
the wild-type enzyme transfers mainly chains with a degree of polymerization of 8-14, the mutant enzyme DELTA1-112 transfers a greater proportion of chains with higher degree of polymerization, 15-20. Mutant DELTA1-63 and mutant DELTA1-83 have an intermediate pattern of transferred chains, 10-20. A progressive shortening of the N-terminus leads to a gradual increase in the length of the transferred chains
-
-
?
amylose
amylose containing alpha-1,6-glucosidic linkages
-
-
-
?
amylose
amylose containing alpha-1,6-glucosidic linkages
-
-
-
?
amylose
amylose containing alpha-1,6-glucosidic linkages
100% activity
-
-
?
amylose
amylose containing alpha-1,6-glucosidic linkages
-
-
-
?
amylose
amylose containing alpha-1,6-glucosidic linkages
-
-
-
-
?
amylose
amylose containing alpha-1,6-glucosidic linkages
-
-
-
?
amylose
amylose containing alpha-1,6-glucosidic linkages
-
-
-
-
?
amylose
amylose containing alpha-1,6-glucosidic linkages
-
-
-
?
amylose
amylose containing alpha-1,6-glucosidic linkages
the C-terminal regions of isoenzyme PvSBE1 and PvSBE2 have different roles in branching enzyme activity. The C-terminal region of PvSBE1 confers specificity to amylose while that of PvSBE2 confers specificity to the transfer of short chains
-
-
?
amylose
amylose containing alpha-1,6-glucosidic linkages
the enzyme shows limited activity for substrates containing only alpha-1,4 linkages such as amylose
-
-
?
amylose
amylose containing alpha-1,6-glucosidic linkages
the enzyme shows limited activity for substrates containing only alpha-1,4 linkages such as amylose
-
-
?
amylose
amylose containing alpha-1,6-glucosidic linkages
potato type III amylose
-
-
?
amylose
amylose containing alpha-1,6-glucosidic linkages
-
at 35°C the enzyme does not act rapidly on such chains unless they are about 40 glucose units or more in length, at 4°C the minimum length falls to about 10
-
?
amylose
amylose containing alpha-1,6-glucosidic linkages
-
enzyme SBE I is more active than enzyme SBE II. The enzyme forms SBE I and SBE II mainly branch the dextrins by intrachain branching. The products of SBE I show distinct populations at DP11-12 and DP29-30. The products of enzyme form SBE II have one, broader, population with a peak at DP13-14. An accumulation of 6-7 chains is seen with both isoforms
-
-
?
amylose
amylose containing alpha-1,6-glucosidic linkages
-
the enzyme acts on native and synthetic amyloses to give products resembling amylopectin in terms of average unit chain length, degree of beta-amylolysis and iodine stain. The profiles of the unit chains of theses synthetic products are, however, different from that of native amylopectin
-
-
?
amylose
amylose containing alpha-1,6-glucosidic linkages
-
initially the three isoenzymes BE I, BE IIa and BE IIb produce chains of various sizes, DP approximately 8 to 200. Isoenzyme BE I preferentially transfers longer chains than isoenzyme IIa and IIb
-
-
?
corn starch
corn starch containing alpha-1,6-glucosidic linkages
-
-
-
?
corn starch
corn starch containing alpha-1,6-glucosidic linkages
-
-
-
?
corn starch
corn starch containing alpha-1,6-glucosidic linkages
32.16% activity compared to amylose
-
-
?
corn starch
corn starch containing alpha-1,6-glucosidic linkages
-
-
-
?
corn starch
corn starch containing alpha-1,6-glucosidic linkages
-
-
-
?
corn starch
corn starch containing alpha-1,6-glucosidic linkages
-
-
-
?
corn starch
corn starch containing alpha-1,6-glucosidic linkages
-
-
-
?
glycogen
glycogen containing alpha-1,6-glucosidic linkages
-
-
-
?
glycogen
glycogen containing alpha-1,6-glucosidic linkages
-
-
-
?
high-amylose corn starch
high-amylose corn starch containing alpha-1,6-glucosidic linkages
-
-
-
?
high-amylose corn starch
high-amylose corn starch containing alpha-1,6-glucosidic linkages
-
-
-
?
high-amylose corn starch
high-amylose corn starch containing alpha-1,6-glucosidic linkages
-
-
-
?
high-amylose corn starch
high-amylose corn starch containing alpha-1,6-glucosidic linkages
-
-
-
?
potato amylopectin type III
potato amylopectin type III containing alpha-1,6-glucosidic linkages
-
-
-
-
?
potato amylopectin type III
potato amylopectin type III containing alpha-1,6-glucosidic linkages
-
-
-
?
potato amylopectin type III
potato amylopectin type III containing alpha-1,6-glucosidic linkages
-
-
-
-
?
potato amylopectin type III
potato amylopectin type III containing alpha-1,6-glucosidic linkages
-
-
-
-
?
potato amylopectin type III
potato amylopectin type III containing alpha-1,6-glucosidic linkages
-
-
-
?
potato amylopectin type III
potato amylopectin type III containing alpha-1,6-glucosidic linkages
-
-
-
-
?
potato amylopectin type III
potato amylopectin type III containing alpha-1,6-glucosidic linkages
-
100% activity
-
-
?
potato amylopectin type III
potato amylopectin type III containing alpha-1,6-glucosidic linkages
Rhodothermus marinus STB05
-
-
-
-
?
potato amylopectin type III
potato amylopectin type III containing alpha-1,6-glucosidic linkages
Rhodothermus marinus STB05
-
100% activity
-
-
?
potato amylose
potato amylose containing alpha-1,6-glucosidic linkages
-
-
-
?
potato amylose
potato amylose containing alpha-1,6-glucosidic linkages
Geobacillus mahadia Geo-05
-
-
-
?
potato amylose
potato amylose containing alpha-1,6-glucosidic linkages
-
65.4% activity compared to potato amylopectin type III
-
-
?
potato amylose
potato amylose containing alpha-1,6-glucosidic linkages
Rhodothermus marinus STB05
-
65.4% activity compared to potato amylopectin type III
-
-
?
potato amylose type III
potato amylose type III containing alpha-1,6-glucosidic linkages
-
-
-
?
potato amylose type III
potato amylose type III containing alpha-1,6-glucosidic linkages
-
-
-
-
?
potato amylose type III
potato amylose type III containing alpha-1,6-glucosidic linkages
-
-
-
?
potato starch
potato starch containing alpha-1,6-glucosidic linkages
-
-
-
?
potato starch
potato starch containing alpha-1,6-glucosidic linkages
-
-
-
?
soluble starch
soluble starch containing alpha-1,6-glucosidic linkages
-
-
-
?
soluble starch
soluble starch containing alpha-1,6-glucosidic linkages
Geobacillus mahadia Geo-05
-
-
-
?
soluble starch
soluble starch containing alpha-1,6-glucosidic linkages
82.4% activity compared to amylose
-
-
?
soluble starch
soluble starch containing alpha-1,6-glucosidic linkages
-
-
-
?
soluble starch
soluble starch containing alpha-1,6-glucosidic linkages
-
-
-
?
soluble starch
soluble starch containing alpha-1,6-glucosidic linkages
-
47.3% activity compared to potato amylopectin type III
-
-
?
soluble starch
soluble starch containing alpha-1,6-glucosidic linkages
Rhodothermus marinus STB05
-
47.3% activity compared to potato amylopectin type III
-
-
?
starch
starch containing alpha-1,6-glucosidic linkages
-
-
-
?
starch
starch containing alpha-1,6-glucosidic linkages
-
-
-
?
starch
starch containing alpha-1,6-glucosidic linkages
-
-
-
?
starch
starch containing alpha-1,6-glucosidic linkages
-
-
-
?
tapioca starch
tapioca starch containing alpha-1,6-glucosidic linkages
-
46.5% activity compared to potato amylopectin type III
-
-
?
tapioca starch
tapioca starch containing alpha-1,6-glucosidic linkages
Rhodothermus marinus STB05
-
46.5% activity compared to potato amylopectin type III
-
-
?
waxy corn starch
waxy corn starch containing alpha-1,6-glucosidic linkages
-
74.7% activity compared to potato amylopectin type III
-
-
?
waxy corn starch
waxy corn starch containing alpha-1,6-glucosidic linkages
Rhodothermus marinus STB05
-
74.7% activity compared to potato amylopectin type III
-
-
?
additional information
?
-
cyclodextrins neither serve as donors nor as acceptors
-
-
?
additional information
?
-
-
cyclodextrins neither serve as donors nor as acceptors
-
-
?
additional information
?
-
-
Starch synthase I activity in native PAGE without addition of glucans is dependent on at least one of the two branching enzyme isoforms active in Arabidopsis leaves. This interaction is most likely not based on a physical association of the enzymes. Chain length distribution patterns of the formed glucans are irrespective of enzyme isoforms origin and still independent of assay conditions. All starch synthase isoforms I-IV are able to interact with branching enzymes and form branched glucans, product analysis, overview
-
-
?
additional information
?
-
-
the branching enzyme converts any sizes of amyloses to a highly branched glucan with the same molecular size
-
-
?
additional information
?
-
-
the enzyme performs branching of amylose from Oryza sative starch, product identification and determination, overview
-
-
?
additional information
?
-
-
the enzyme performs branching of amylose from Oryza sative starch, product identification and determination, overview
-
-
?
additional information
?
-
the branching activity of the enzyme contains both alpha-1,4 and alpha-1,6 linkages
-
-
-
additional information
?
-
-
the branching activity of the enzyme contains both alpha-1,4 and alpha-1,6 linkages
-
-
-
additional information
?
-
the branching activity of the enzyme contains both alpha-1,4 and alpha-1,6 linkages
-
-
-
additional information
?
-
Cyanobacterium sp.
the recombinant isozyme is active with amylose or amylopectin, and is active against phosphorylase limit dextrin, in which outer branches are uniformly diminished to 4 glucose residues. Chain-length preference of reaction product of the recombinant isozymes, overview
-
-
?
additional information
?
-
Cyanobacterium sp.
the recombinant isozyme is active with amylose or amylopectin, and is active against phosphorylase limit dextrin, in which outer branches are uniformly diminished to 4 glucose residues. Chain-length preference of reaction product of the recombinant isozymes, overview
-
-
?
additional information
?
-
Cyanobacterium sp.
the recombinant isozyme is active with amylose or amylopectin, and is active against phosphorylase limit dextrin, in which outer branches are uniformly diminished to 4 glucose residues. Chain-length preference of reaction product of the recombinant isozymes, overview
-
-
?
additional information
?
-
the recombinant isozyme is active with amylose or amylopectin, and is active against phosphorylase limit dextrin, in which outer branches are uniformly diminished to 4 glucose residues. Chain-length preference of reaction product of the recombinant isozymes, overview
-
-
?
additional information
?
-
the recombinant isozyme is active with amylose or amylopectin, and is active against phosphorylase limit dextrin, in which outer branches are uniformly diminished to 4 glucose residues. Chain-length preference of reaction product of the recombinant isozymes, overview
-
-
?
additional information
?
-
the recombinant isozyme is active with amylose or amylopectin, and is active against phosphorylase limit dextrin, in which outer branches are uniformly diminished to 4 glucose residues. Chain-length preference of reaction product of the recombinant isozymes, overview
-
-
?
additional information
?
-
glycogen branching enzyme GBE1 mutation causing equine glycogen storage disease IV.A C to A substitution at base 102 results in a tyrosine (Y) to stop (X) mutation in codon 34 of exon of exon 1. All 11 affected foals are homozygous for the X34 allele, all 16 control horses are homozygous for the Y34 allele. Poorly branched glycogen, abnormal polysaccharide accumulation, lack of measurable GBE1 enzyme activity and immunodetectable GBE1 protein, coupled with the present observation of abundant GBE1 mRNA in affected foals, are consistent with the nonsense mutation in the 699 amino acid GBE1 protein
-
-
?
additional information
?
-
-
glycogen branching enzyme GBE1 mutation causing equine glycogen storage disease IV.A C to A substitution at base 102 results in a tyrosine (Y) to stop (X) mutation in codon 34 of exon of exon 1. All 11 affected foals are homozygous for the X34 allele, all 16 control horses are homozygous for the Y34 allele. Poorly branched glycogen, abnormal polysaccharide accumulation, lack of measurable GBE1 enzyme activity and immunodetectable GBE1 protein, coupled with the present observation of abundant GBE1 mRNA in affected foals, are consistent with the nonsense mutation in the 699 amino acid GBE1 protein
-
-
?
additional information
?
-
-
the enzyme is responsible for the formation of the alpha-1,6 linkages in the glycogen molecule
-
-
?
additional information
?
-
the Escherichia coli enzyme specifically forms the branch linkages at the third glucose residue from the reducing end of the acceptor chain. The enzyme recognizes the location of branching points in its acceptor chain during their branching reaction
-
-
?
additional information
?
-
-
a fatal form of glycogen storage disease IV affects Norwegian Florest Cat, in which striated muscles and the nervous system are primarily affected, while the liver remains unaffected. This form of GSD IV is caused by a 6.1-kb deletion that eliminates exon 12 of the feline GBE1 gene
-
-
?
additional information
?
-
-
each isoform of the Q-enzyme plays a distinct role in starch biosynthesis
-
-
?
additional information
?
-
two-step reaction mechanism for the amylase activity, i.e. 1-4 bond breakage, and isomerization, i.e. 1-6 bond formation, which occur in the same catalytic pocket
-
-
?
additional information
?
-
-
two-step reaction mechanism for the amylase activity, i.e. 1-4 bond breakage, and isomerization, i.e. 1-6 bond formation, which occur in the same catalytic pocket
-
-
?
additional information
?
-
two-step reaction mechanism for the amylase activity, i.e. 1-4 bond breakage, and isomerization, i.e. 1-6 bond formation, which occur in the same catalytic pocket
-
-
?
additional information
?
-
-
two-step reaction mechanism for the amylase activity, i.e. 1-4 bond breakage, and isomerization, i.e. 1-6 bond formation, which occur in the same catalytic pocket
-
-
?
additional information
?
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The activities of the isozymes BEi, BEIIa and BEIIb with a linear glucan amylose decrease with a decrease in the molar size of amylose, and no activities of BEIIa and BEIIb are found when the degree of polymerization of amylose is lower than at least 80, whereas BEI had an activity with amylose of a degree of polymerization higher than approximately 50. Isoform BEIIb almost exclusively transfers chains with degree of polymerization of 7 and 6 while isoform BEIIa forms a wide range of short chains with degree of polymerization of 6 to around 15 from outer chains of amylopectin and amylose. Isoform BEI forms a variety of short chains and intermediate chains of a degree of polymerization below 40 by attacking not only outer chains but also inner chains of branched glucan. Isoforms BEIIa or BEIIb can only scarcely or can not attack inner chains, respectively
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interactions between rice SS isozymes and BE isozymes in the synthesis of unprimed glucan, overview
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interactions between rice SS isozymes and BE isozymes in the synthesis of unprimed glucan, overview
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interactions between rice starch synthase isozymes and branching enzyme isozymes in the synthesis of unprimed glucan, overview
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interactions between rice starch synthase isozymes and branching enzyme isozymes in the synthesis of unprimed glucan, overview
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differences in properties between isoforms of SBE are not the main factors that determine the polymodal distribution of branch lengths in amylopectin
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a minimal chain length of ten glucosyl units is required for the donor substrate to be recognized by Rhodothermus marinus branching enzyme that essentially produces branches with a degree of polymerization of 3-8. The enzyme preferentially creates new branches by intermolecular mechanism. Branched glucans define better substrates for the enzyme leading to the formation of hyper-branched particles of 30-70 nm in diameter, dextrins. The enzyme catalyzes an additional alpha-4-glucanotransferase activity
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a minimal chain length of ten glucosyl units is required for the donor substrate to be recognized by Rhodothermus marinus branching enzyme that essentially produces branches with a degree of polymerization of 3-8. The enzyme preferentially creates new branches by intermolecular mechanism. Branched glucans define better substrates for the enzyme leading to the formation of hyper-branched particles of 30-70 nm in diameter, dextrins. The enzyme catalyzes an additional alpha-4-glucanotransferase activity
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the enzyme catalyzes starch branching by the cleavage of alpha(1->4) linkage and transfer in alpha(1->6) of the fragment in non-reducing position, but the enzyme also shows an additional alpha-4-glucanotransferase activity not described so far for a member of the GH13 family. The enzyme is able to transfer alpha(1->4)-linked-glucan in C4 position (instead of C6 position for the branching activity) of a glucan to create new alpha(1->4) linkages yielding to the elongation of linear chains subsequently used for further branching, overview
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the enzyme catalyzes starch branching by the cleavage of alpha(1->4) linkage and transfer in alpha(1->6) of the fragment in non-reducing position, but the enzyme also shows an additional alpha-4-glucanotransferase activity not described so far for a member of the GH13 family. The enzyme is able to transfer alpha(1->4)-linked-glucan in C4 position (instead of C6 position for the branching activity) of a glucan to create new alpha(1->4) linkages yielding to the elongation of linear chains subsequently used for further branching, overview
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increased branching of the starch from maize and potato following BE treatment, short chains increase whereas the number of long chains decrease after BE treatment, molecular size distribution of branching enzyme-treated and control starch, granular structure, NMR analysis, overview
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the enzyme forms SBE I and SBE II mainly branch the dextrins by intrachain branching
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each branching enzyme isoform is involved in a different phase of glycogen synthesis
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each branching enzyme isoform is involved in a different phase of glycogen synthesis
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the Synechococcus elongatus enzyme specifically forms the branch linkages at the third glucose residue from the reducing end of the acceptor chain. The enzyme recognizes the location of branching points in its acceptor chain during their branching reaction
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the Synechococcus elongatus enzyme specifically forms the branch linkages at the third glucose residue from the reducing end of the acceptor chain. The enzyme recognizes the location of branching points in its acceptor chain during their branching reaction
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the Synechococcus elongatus enzyme specifically forms the branch linkages at the third glucose residue from the reducing end of the acceptor chain. The enzyme recognizes the location of branching points in its acceptor chain during their branching reaction
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loop 220-245, named as catalytic loop, acts as a lid retaining the intermediate reaction product for subsequent transfer to a new a-1,6 position. The active site comprises two acidic catalytic residues, Glu183 and Asp354, the polarizer His10, aromatic gate-keepers Trp28, Trp270, Trp407, and Trp416 and the residue Tyr233
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szubstrates are 0.5%, w/v of amylose, corn starch, potato starch, wheat starch and waxy corn starch, all gelatinized by a high temperature (121°C) and pressure (100 KPa) prior treatment. The recombinant enzyme shows the highest specificity to amylose. The recombinant enzyme can act on maize starch, and starch treated with TcGBE is observed to have a lower amylose content and molecular weight. Chain length distribution of amylopectin products by anion exchange chromatography
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szubstrates are 0.5%, w/v of amylose, corn starch, potato starch, wheat starch and waxy corn starch, all gelatinized by a high temperature (121°C) and pressure (100 KPa) prior treatment. The recombinant enzyme shows the highest specificity to amylose. The recombinant enzyme can act on maize starch, and starch treated with TcGBE is observed to have a lower amylose content and molecular weight. Chain length distribution of amylopectin products by anion exchange chromatography
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Multiple isoforms of starch branching enzyme-I exist in wheat. Lack of the major SBE-I isoform does not alter starch phenotype
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no major difference in the amylose/amylopectin ratio is detectected by reducing the expression of SBE-I using antisense constructs
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starch structure in the two accessions, overview
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the glycogen branching enzyme from Vibrio vulnificus transfers short side chains (DP 3-5) significantly greater than any other bacterial glycogen branching enzyme. The N1-domain of the enzyme has a crucial role in the determination of the branching pattern of glycogen, degrees of polymerization in enzyme reaction products compared to enzymes from other origin, overview
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the glycogen branching enzyme from Vibrio vulnificus transfers short side chains (DP 3-5) significantly greater than any other bacterial glycogen branching enzyme. The N1-domain of the enzyme has a crucial role in the determination of the branching pattern of glycogen, degrees of polymerization in enzyme reaction products compared to enzymes from other origin, overview
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the catalytic center is exclusively located in the central position of the enzyme
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chain-length distribution and branch linkage frequence of the 3 isoenymes
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the conserved Arg residue 384 plays an important role in the catalytic function but may not be directly involved in substrate binding
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starch-branching enzyme and glycogen synthase work in a cyclically interdependent fashion
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in absence of starch-branching enzyme IIb, the further absence of starch-branching enzyme Ia leads to increased branching
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in absence of starch-branching enzyme IIb, the further absence of starch-branching enzyme Ia leads to increased branching
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in absence of starch-branching enzyme IIb, the further absence of starch-branching enzyme Ia leads to increased branching
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the enzyme performs branching of two linear alpha-(1,4)-D-glucans substrates of degrees of polymerization about 150 and 6000, product identification by NMR and gel filtration, determination of chain-length distributions and hydrodynamic volume distributions, interchain mechanism, overview
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the enzyme performs branching of two linear alpha-(1,4)-D-glucans substrates of degrees of polymerization about 150 and 6000, product identification by NMR and gel filtration, determination of chain-length distributions and hydrodynamic volume distributions, interchain mechanism, overview
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molecular weight distribution of starch, amylose and amylopectin, overview. SBE is the only enzyme that generates glucan branches, i.e. it is the only chain-stopping substance for branch growth, and as a consequence SBE has a significant effect on the final structure of the resulting starch
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molecular weight distribution of starch, amylose and amylopectin, overview. SBE is the only enzyme that generates glucan branches, i.e. it is the only chain-stopping substance for branch growth, and as a consequence SBE has a significant effect on the final structure of the resulting starch
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phosphorylated alpha-1,4-glucan
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33P-labeled phosphorylated and 3H-end-labeled nonphosphorylated
formation of dual-labeled phosphorylated branched polysaccharides with an average degree of polymerization of 80 to 85
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