Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
amylopectin
amylopectin containing alpha-1,6-glucosidic linkages
amylopectin
amylopectin with additional alpha-1,6-glucosidic linkages
amylopectin
highly branched cyclic dextrin
amylose
amylose containing alpha-1,6-glucosidic linkages
amylose
branched polyglucan
using linear amylose synthesized in a tandem reaction by potato phosphorylase
-
-
?
beta-cyclodextrin
?
22.82% activity compared to amylose
-
-
?
corn starch
corn starch 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
Maltohexaose
?
-
dinitrosalicylate method, assay at pH 6.0, 70°C
-
-
?
maltopentaose
?
-
dinitrosalicylate method, assay at pH 6.0, 70°C
-
-
?
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
potato amylose
potato amylose 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
soluble starch
soluble starch containing alpha-1,6-glucosidic linkages
starch
?
assay at pH 5.0, 37°C
-
-
?
starch
starch containing alpha-1,6-glucosidic linkages
tapioca starch
tapioca starch containing alpha-1,6-glucosidic linkages
waxy corn starch
waxy corn starch containing alpha-1,6-glucosidic linkages
waxy maize starch
?
-
-
-
-
?
wheat starch
wheat starch containing alpha-1,6-glucosidic linkages
30.56% activity compared to amylose
-
-
?
additional information
?
-
amylopectin
?
-
-
the amount of short chains with a degree of polymerization of 6-8 is significantly increased in the product of Bacillus cereus
-
?
amylopectin
?
-
assay at 30°C, 20 min
-
-
?
amylopectin
?
iodine assay
-
-
?
amylopectin
?
iodine assay
-
-
?
amylopectin
?
iodine assay
-
-
?
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
?
-
assay at pH 7.5
-
-
?
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
-
-
-
?
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 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
-
-
-
-
?
amylopectin
amylopectin with additional alpha-1,6-glucosidic linkages
-
-
-
-
?
amylopectin
highly branched cyclic dextrin
-
-
-
-
?
amylopectin
highly branched cyclic dextrin
-
-
-
-
?
amylopectin
highly branched cyclic dextrin
-
-
-
-
?
amylose
?
-
assay at 30°C, 20 min
-
-
?
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
?
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
?
-
assay at pH 7.5
-
-
?
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
?
-
dinitrosalicylate method, assay at pH 6.0, 70°C
-
-
?
amylose
?
assay at pH 5.0, 37°C
-
-
?
amylose
?
-
assay at pH 30°C, pH 8.0
-
-
?
amylose
?
assay at pH 7.0, 30°C for 90 min
-
-
?
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
-
-
-
-
?
amylose
amylose containing alpha-1,6-glucosidic linkages
-
-
-
-
?
amylose
amylose containing alpha-1,6-glucosidic linkages
-
potato amylose
-
-
?
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
-
-
-
-
?
amylose
amylose containing alpha-1,6-glucosidic linkages
-
-
-
?
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
-
-
-
-
?
amylose
amylose containing alpha-1,6-glucosidic linkages
-
-
-
-
?
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
-
-
-
?
corn starch
corn starch containing alpha-1,6-glucosidic linkages
-
-
-
-
?
Glycogen
?
-
from E. coli and rabbit liver, little activity
-
-
?
Glycogen
?
37.06% activity compared to amylose
-
-
?
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
-
-
-
-
?
potato amylopectin type III
potato amylopectin type III containing alpha-1,6-glucosidic linkages
-
100% activity
-
-
?
potato amylose
potato amylose containing alpha-1,6-glucosidic linkages
-
-
-
?
potato amylose
potato amylose containing alpha-1,6-glucosidic linkages
-
-
-
?
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
-
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
-
-
-
?
Pullulan
?
11.21% activity compared to amylose
-
-
?
Pullulan
?
-
dinitrosalicylate method, assay at pH 6.0, 70°C
-
-
?
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
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
-
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
-
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
-
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
?
-
-
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
-
-
?
additional information
?
-
-
interactions between rice SS isozymes and BE isozymes in the synthesis of unprimed glucan, overview
-
-
?
additional information
?
-
interactions between rice SS isozymes and BE isozymes in the synthesis of unprimed glucan, overview
-
-
?
additional information
?
-
-
interactions between rice starch synthase isozymes and branching enzyme isozymes in the synthesis of unprimed glucan, overview
-
-
?
additional information
?
-
interactions between rice starch synthase isozymes and branching enzyme isozymes in the synthesis of unprimed glucan, overview
-
-
?
additional information
?
-
-
differences in properties between isoforms of SBE are not the main factors that determine the polymodal distribution of branch lengths in amylopectin
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
the enzyme forms SBE I and SBE II mainly branch the dextrins by intrachain branching
-
-
?
additional information
?
-
-
each branching enzyme isoform is involved in a different phase of glycogen synthesis
-
-
?
additional information
?
-
-
each branching enzyme isoform is involved in a different phase of glycogen synthesis
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
Multiple isoforms of starch branching enzyme-I exist in wheat. Lack of the major SBE-I isoform does not alter starch phenotype
-
-
?
additional information
?
-
-
no major difference in the amylose/amylopectin ratio is detectected by reducing the expression of SBE-I using antisense constructs
-
-
?
additional information
?
-
starch structure in the two accessions, overview
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
the catalytic center is exclusively located in the central position of the enzyme
-
-
?
additional information
?
-
-
chain-length distribution and branch linkage frequence of the 3 isoenymes
-
-
?
additional information
?
-
-
the conserved Arg residue 384 plays an important role in the catalytic function but may not be directly involved in substrate binding
-
-
?
additional information
?
-
-
starch-branching enzyme and glycogen synthase work in a cyclically interdependent fashion
-
-
?
additional information
?
-
in absence of starch-branching enzyme IIb, the further absence of starch-branching enzyme Ia leads to increased branching
-
-
?
additional information
?
-
in absence of starch-branching enzyme IIb, the further absence of starch-branching enzyme Ia leads to increased branching
-
-
?
additional information
?
-
-
in absence of starch-branching enzyme IIb, the further absence of starch-branching enzyme Ia leads to increased branching
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
phosphorylated alpha-1,4-glucan
additional information
-
-
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
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(2R)-2-[(4-methoxyphenyl)methyl]-3,3-dimethylpiperidin-4-one
-
40.5% inhibition at 2 mM
(3R)-N-[(2S)-1-hydroxypropan-2-yl]-5-oxo-1-(propan-2-yl)pyrrolidine-3-carboxamide
-
-
(3S,5S)-5-[hydroxy(methoxy)methyl]pyrrolidin-3-ol
-
35.2% inhibition at 3 mM
(4R)-4-(azepan-1-yl)-1-[(1H-benzimidazol-2-yl)methyl]piperidin-3-ol
-
-
1'-(propan-2-yl)-3,3a,5,6,7,7a-hexahydrospiro[imidazo[4,5-c]pyridine-4,4'-piperidine]
-
-
1'H-spiro[piperidine-4,2'-quinazolin]-4'(3'H)-one
-
37.5% inhibition at 1 mM
1-(1H-benzimidazol-2-yl)ethan-1-amine
-
36.5% inhibition at 3 mM
1-(1H-benzimidazol-6-yl)-2-methylpropan-2-amine
-
36.5% inhibition at 2 mM
1-(2,4-dihydroxyquinolin-3-yl)ethan-1-one
-
-
1-(3-methoxyphenyl)-2-[[(pyridin-3-yl)methyl]amino]ethan-1-ol
-
-
1-(4,5-dimethyl-1H-benzimidazol-2-yl)methanamine
-
-
1-(5-methyl-1H-benzimidazol-2-yl)ethan-1-amine
-
-
1-acetyl-2-hydroxy-4-methyl-2,5-dihydro-1H-pyrrole-3-carbonitrile
-
-
1-benzyl-5-oxopyrrolidine-3-carboxylic acid
-
37.6% inhibition at 2 mM
1H-benzimidazol-2-amine
-
34.8% inhibition at 3 mM
2-(5-methyl-1H-benzimidazol-2-yl)ethan-1-amine
-
-
2-([[5-hydroxy-4-(hydroxymethyl)-6-methylpyridin-3-yl]methyl]sulfanyl)pyrimidin-4(1H)-one
-
-
2-mercaptoethanol
29.65% residual activity at 1 mM
2-oxopiperidine-3-carbohydrazide
-
-
3-chloro-4-[4-[(pyridin-3-yl)methyl]piperazin-1-yl]aniline
-
-
4,6-dihydroxy-5-nitropyridine-3-carboxylic acid
-
-
5-(piperazin-1-yl)[1,2]thiazolo[2,3-c]pyrimidin-8-ium
-
34.2% inhibition at 3 mM
5-oxo-1-(propan-2-yl)pyrrolidine-3-carboxylic acid
-
40.2% inhibition at 3 mM
Al3+
the wild type enzyme shows bout 75% residual activity at 10 mM. The C-terminally truncated enzyme shows about 95% residual activity at 10 mM
Cr2+
the wild type enzyme shows about 75% residual activity at 10 mM. The C-terminally truncated enzyme shows about 94% residual activity at 10 mM
CuSO4
-
1 mM, complete inactivation
DMSO
-
about 22.9% decreased enzyme activity, 10%
ethanol
-
about 57.2% decreased enzyme activity, 10%
ethyl 4,6-dihydroxypyridine-3-carboxylate
-
-
glycerol
high concentration of glycerol decreases the branching activity of the enzyme (97.9% residual activity at 30% (v/v)
isoniazid
-
32.5% inhibition at 1 mM
maltoheptaose
-
40% inhibition at 15 mM
methanol
-
about 45.2% decreased enzyme activity, 10%
methyl (6S)-5-methyl-4,5,6,7-tetrahydro-1H-imidazo[4,5-c]pyridine-6-carboxylate
-
-
N'-[imino(pyridin-2-yl)methyl]furan-2-carbohydrazide
-
-
N-[2-chloro-5-(trifluoromethyl)phenyl]triimidodicarbonic diamide
-
-
NaCl
-
concetration of 2-4 M NaCl
Pb2+
26.26% residual activity at 1 mM
phenylmethylsulfonyl fluoride
70.88% residual activity at 1 mM
ZnCl2
-
1 mM, complete inactivation
Ba2+
84.11% residual activity at 1 mM
Ba2+
-
1 mM slightly reduces the enzyme activity (by approximately 10%)
Ca2+
the additon of 2.5 mM of Ca2+ slightly inhibits the enzyme
Ca2+
enzyme activity is lowered to 73% at 5 mM Ca2+
Ca2+
the wild type enzyme shows about 90% residual activity at 10 mM. The C-terminally truncated enzyme shows about 97% residual activity at 10 mM
Ca2+
-
1 mM slightly reduces the enzyme activity (by approximately 10%)
CaCl2
-
0.06 M, 14% inhibition
CaCl2
-
10 mM, 50% inhibition. 100 mM, complete inactivation
Co2+
the additon of 2.5 mM of Co2+ slightly inhibits the enzyme
Co2+
42.7% residual activity at 1 mM
Co2+
the wild type enzyme shows complete inhibition at 3 mM. The C-terminally truncated enzyme shows about 28% residual activity at 10 mM
Cu2+
the enzyme has about 25% residual activity at 5 mM
Cu2+
0.25% residual activity at 1 mM
Cu2+
the wild type enzyme shows about 10% residual activity at 10 mM. The C-terminally truncated enzyme shows about 51% residual activity at 10 mM
Cu2+
-
36.54% inhibition at 1 mM
EDTA
enzymatic activity is abolished in the presence of EDTA
EDTA
-
about 44.2% decreased enzyme activity, 5 mM
EDTA
-
the enzyme retains 73.39%, 39.01%, 19.06%, 7.64%, and 3.30% of its activity in the presence of 1, 2, 4, 8, and 10 mM EDTA, respectively
Fe2+
5 mM Fe2+ inhibits the enzyme by 60%
Fe2+
the wild type enzyme shows about 85% residual activity at 10 mM. The C-terminally truncated enzyme shows about 97% residual activity at 10 mM
Fe3+
enzymatic activity is abolished in the presence of Fe3+
Fe3+
the wild type enzyme shows about 78% residual activity at 10 mM. The C-terminally truncated enzyme shows about 95% residual activity at 10 mM
Fe3+
-
17.33% inhibition at 1 mM
HgCl2
-
1 mM, complete inactivation
Mg2+
the additon of 2.5 mM of Mg2+ slightly inhibits the enzyme
Mg2+
-
1 mM slightly reduces the enzyme activity (by approximately 10%)
MgCl2
-
0.08 M, 41% inhibition
MgCl2
-
1 mM, complete inactivation
Mn2+
the additon of 2.5 mM of Mn2+ slightly inhibits the enzyme
Mn2+
enzyme activity is lowered to 86% at 5 mM Ca2+
Mn2+
80.46% residual activity at 1 mM
Mn2+
the wild type enzyme shows about 35% residual activity at 10 mM. The C-terminally truncated enzyme shows about 69% residual activity at 10 mM
MnCl2
-
-
MnCl2
-
1 mM, complete inactivation
Ni2+
4.24% residual activity at 1 mM
Ni2+
the wild type enzyme shows about 2% residual activity at 10 mM. The C-terminally truncated enzyme shows about 25% residual activity at 10 mM
Urea
-
50% inhibition at 0.4 M, complete inhibition at 2 M. Up to 2 M, reversible inhibition
Urea
92.02% residual activity at 1 mM
Zn2+
enzymatic activity is abolished in the presence of Zn2+
Zn2+
the enzyme has about 35% residual activity at 5 mM Zn2+
Zn2+
0.8% residual activity at 1 mM
Zn2+
the wild type enzyme shows about 18% residual activity at 10 mM. The C-terminally truncated enzyme shows about 58% residual activity at 10 mM
Zn2+
-
1 mM slightly reduces the enzyme activity (by approximately 10%)
additional information
not inhibitory: ADP, ADP glucose, tunicamycin, castenospermine, nojirimycin, or acarbose
-
additional information
-
not inhibitory: ADP, ADP glucose, tunicamycin, castenospermine, nojirimycin, or acarbose
-
additional information
-
small molecule inhibitor identification, high throughput virtual screening and molecular docking
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.051
-
be1-1 be3-2, T-DNA insertion double mutant in enzyme BE1 and BE3, in vitro assay of starch-branching enzyme activity
0.082
-
be3-1 (N548089), T-DNA insertion mutant line for BE3, in vitro assay of starch-branching enzyme activity
0.096
-
be1-1 (DYK140), T-DNA insertion mutant line for BE1, in vitro assay of starch-branching enzyme activity
0.102
-
be3-2 (EQJ13), T-DNA insertion mutant line for BE3, in vitro assay of starch-branching enzyme activity
0.13
-
be1-2 (N637880), T-DNA insertion mutant line for BE1, in vitro assay of starch-branching enzyme activity
0.281
mutant enzyme I571D, pH and temperature not specified in the publication
0.282
wild type enzyme, pH and temperature not specified in the publication
0.293
mutant enzyme T339E, pH and temperature not specified in the publication
0.295
mutant enzyme Q231R, pH and temperature not specified in the publication
0.296
mutant enzyme T339D, pH and temperature not specified in the publication
0.298
mutant enzyme Q231K, pH and temperature not specified in the publication
10.7
purified recombinant enzyme, pH 7.5, 25°C, substrate amylose
26
mutant enzyme A310G, using potato amylopectin type III as substrate, at pH 7.5 and 37°C
28.5
-
mutant enzyme DELTA1-63, micromol Glc incorporated into alpha-D-glucan per min at 30°C
30
mutant enzyme A310I, using potato amylopectin type III as substrate, at pH 7.5 and 37°C
384
wild type enzyme, using potato amylopectin type III as substrate, at pH 7.5 and 37°C
4.7
wild-type enzyme, branching assay
42
mutant lacking the N1 domain, i.e. lacking N-terminal residues 1-108, pH 7.0, 25°C
47.3
Cyanobacterium sp.
purified recombinant His-tagged isozyme BE1, pH 7.0, 30°C
535.4
-
mutant enzyme DELTA1-83, micromol Glc incorporated into alpha-D-glucan per min at 30°C
54
mutant enzyme A310N, using potato amylose type III as substrate, at pH 7.5 and 37°C
58
mutant enzyme A310G, using potato amylose type III as substrate, at pH 7.5 and 37°C
63.75
wild-type, pH 7.0, 25°C
67
mutant enzyme A310E, using potato amylose type III as substrate, at pH 7.5 and 37°C
7.2
wild-type enzyme, branching assay
70
mutant enzyme A310D, using potato amylose type III as substrate, at pH 7.5 and 37°C
90.28
-
purified recombinnat enzyme, pH 8.5, 55°C, substrate amylose
951.4
Cyanobacterium sp.
purified recombinant His-tagged isozyme BE1, pH 7.0, 30°C
988.8
Cyanobacterium sp.
purified recombinant His-tagged isozyme BE1, pH 7.0, 30°C
0.001
-
be1-1 be2-1, T-DNA insertion double mutant in enzyme BE1 and BE2, in vitro assay of starch-branching enzyme activity
0.001
-
be2-2 (DSA16), T-DNA insertion mutant line for BE2, in vitro assay of starch-branching enzyme activity
0.002
-
be2-1 (EFH20), T-DNA insertion mutant line for BE2, in vitro assay of starch-branching enzyme activity
0.002
-
be2-1 be3-2, T-DNA insertion double mutant in enzyme BE2 and BE3, in vitro assay of starch-branching enzyme activity
0.107
-
wild type enzyme, Col-0
0.107
-
wild type enzyme, Wassilewskija genetic background
27
mutant enzyme A310N, using potato amylopectin type III as substrate, at pH 7.5 and 37°C
27
mutant enzyme A310Q, using potato amylopectin type III as substrate, at pH 7.5 and 37°C
299
-
branching enzyme II
299
wild type enzyme, using potato amylose type III as substrate, at pH 7.5 and 37°C
32
mutant enzyme A310D, using potato amylopectin type III as substrate, at pH 7.5 and 37°C
32
mutant enzyme A310E, using potato amylopectin type III as substrate, at pH 7.5 and 37°C
62
mutant enzyme A310I, using potato amylose type III as substrate, at pH 7.5 and 37°C
62
mutant enzyme A310Q, using potato amylose type III as substrate, at pH 7.5 and 37°C
additional information
the branching enzyme has a spesific activity of 0.4 U/mg. Amylose is used as substrate. The methods defines one unit of branching enzyme activity as 1 micromol of alpha-1,6 linkages synthesized per minute.
additional information
-
the branching enzyme has a spesific activity of 0.4 U/mg. Amylose is used as substrate. The methods defines one unit of branching enzyme activity as 1 micromol of alpha-1,6 linkages synthesized per minute.
additional information
-
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
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 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
-
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 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 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 538.0 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 538.0 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 556.5 U/mg, 1 U = decrease in absorbance of 1.0 per min at 530 nm, mutant CTT Dr, iodine assay
additional information
-
specific activity on amylopectin 556.5 U/mg, 1 U = decrease in absorbance of 1.0 per min at 530 nm, mutant CTT Dr, 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
-
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 404.2 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 404.2 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 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 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 442.3 U/mg, 1 U = decrease in absorbance of 1.0 per min at 660 nm, mutant CTT Dr, iodine assay
additional information
-
specific activity on amylose 442.3 U/mg, 1 U = decrease in absorbance of 1.0 per min at 660 nm, mutant CTT Dr, 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
-
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 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 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
-
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
-
-
additional information
-
-
additional information
-
assay method
additional information
-
1.229 U/mg for amylopectin, 1 U = 1% decrease of the absorbance/min
additional information
-
12.258 U/mg for amylose, 1 U = 1% decrease of the absorbance/min
additional information
2.5 U/mg for amylopectin, 1 U = decrease of one absorbance unit at 660 nm at 30°C
additional information
-
2.5 U/mg for amylopectin, 1 U = decrease of one absorbance unit at 660 nm at 30°C
additional information
20.8 U/mg for amylose, 1 U = decrease of one absorbance unit at 660 nm at 30°C
additional information
-
20.8 U/mg for amylose, 1 U = decrease of one absorbance unit at 660 nm at 30°C
additional information
-
the chimeric (1Na/2Nb)II enzyme has a specific activity of 13 U/mg in the presence of 0.1 M citrate or 6.1 U/mg in the absence of citrate. The iodine-staining assay is performed by monitoring the decrease in absorbance at 660 nm for amylose, one unit of enzyme activity is defined as the amount of enzyme yielding a decrease in A660 of 0.1 per minute at 30°C.
additional information
-
0.29 U/mg for the crude cell extract, 1 U = change in the absorbance of 1 unit
additional information
-
1.00 U/mg for the purified enzyme , 1 U = change in the absorbance of 1 unit
additional information
0.252 U/mg for the crude enzyme, 1 U = decrease of 1.0 units of absorbance per minute
additional information
-
0.252 U/mg for the crude enzyme, 1 U = decrease of 1.0 units of absorbance per minute
additional information
-
186 U/mg after ammonium sulfate fractionation, 1 unit = incorporation of 1 nmol glucose into the ethanol-insoluble glucan polymer per minute
additional information
-
39 U/mg for crude extract, 1 unit = incorporation of 1 nmol glucose into the ethanol-insoluble glucan polymer per minute
additional information
-
483 U/mg after DEAE fast flow, 1 unit = incorporation of 1 nmol glucose into the ethanol-insoluble glucan polymer per minute
additional information
6.402 U/mg for the purified enzyme, 1 U = decrease of 1.0 units of absorbance per minute
additional information
-
6.402 U/mg for the purified enzyme, 1 U = decrease of 1.0 units of absorbance per minute
additional information
-
744 to 4001 U/mg for enzyme after purification, 1 unit = incorporation of 1 nmol glucose into the ethanol-insoluble glucan polymer per minute
additional information
-
assay method
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
evolution
Cyanobacterium sp.
Cyanobacterium sp. NBRC 102756 belongs to the cyanobacteria that accumulate water-insoluble alpha-glucan similar to amylopectin rather than glycogen, the latter of which is more commonly produced in these organisms. The amylopectin-producing species invariably have three branching enzyme (BE) homologues, BE1, BE2, and BE3, all belonging to the glycoside hydrolase family 13, GH13, phylogenetic tree. The specific activity of BE3 is much lower than those of BE1 and BE2. Isozymes BE1 and BE2 show similar chain-length preference to BEIIb isoform of Oryza sativa, while the catalytic specificity of BE3 is similar to that of Oryza sativa BEI. These results indicate that starch-producing cyanobacteria have both type-I BE (BE3) and type-II BEs (BE1 and BE2) in terms of chain-length preferences, as is the case of plants
evolution
Cyanobacterium sp.
Cyanobacterium sp. NBRC 102756 belongs to the cyanobacteria that accumulate water-insoluble alpha-glucan similar to amylopectin rather than glycogen, the latter ofwhich is more commonly produced in these organisms. The amylopectin-producing species invariably have three branching enzyme (BE) homologues, BE1, BE2, and BE3, all belonging to the glycoside hydrolase family 13, GH13, phylogenetic tree. The specific activity of BE3 is much lower than those of BE1 and BE2. Isozymes BE1 and BE2 show similar chain-length preference to BEIIb isoform of Oryza sativa, while the catalytic specificity of BE3 is similar to that of Oryza sativa BEI. These results indicate that starch-producing cyanobacteria have both type-I BE (BE3) and type-II BEs (BE1 and BE2) in terms of chain-length preferences, as is the case of plants
evolution
-
great variation exists as to the preference of branching enzymes of diffeent species for their acceptor chain, either A-chain or B-chain. Phylogenetic tree of alpha-glucan branching enzymes
evolution
great variation exists as to the preference of branching enzymes of diffeent species for their acceptor chain, either A-chain or B-chain. Phylogenetic tree of alpha-glucan branching enzymes
evolution
great variation exists as to the preference of branching enzymes of diffeent species for their acceptor chain, either A-chain or B-chain. Phylogenetic tree of alpha-glucan branching enzymes
evolution
great variation exists as to the preference of branching enzymes of diffeent species for their acceptor chain, either A-chain or B-chain. Phylogenetic tree of alpha-glucan branching enzymes
evolution
great variation exists as to the preference of branching enzymes of diffeent species for their acceptor chain, either A-chain or B-chain. Phylogenetic tree of alpha-glucan branching enzymes
evolution
-
great variation exists as to the preference of branching enzymes of different species for their acceptor chain, either A-chain or B-chain. Phylogenetic tree of alpha-glucan branching enzymes
evolution
the branching enzyme is an unusual member of the alpha-amylase family because it has both alpha-1,4-amylase activity and alpha-1,6-transferase activity
evolution
-
the enzyme belongs to the glycoside hydrolase family 13, GH13. Phylogenetic analysis groups VvGBE with other Vibrio GBEs and closely related to GBEs of enteric bacteria. VvGBE and Escherichia coli GBE are type I bacterial GBEs and share 57% sequence similarity
evolution
the enzyme belongs to the glycoside hydrolase family GH13
evolution
-
Cyanobacterium sp. NBRC 102756 belongs to the cyanobacteria that accumulate water-insoluble alpha-glucan similar to amylopectin rather than glycogen, the latter ofwhich is more commonly produced in these organisms. The amylopectin-producing species invariably have three branching enzyme (BE) homologues, BE1, BE2, and BE3, all belonging to the glycoside hydrolase family 13, GH13, phylogenetic tree. The specific activity of BE3 is much lower than those of BE1 and BE2. Isozymes BE1 and BE2 show similar chain-length preference to BEIIb isoform of Oryza sativa, while the catalytic specificity of BE3 is similar to that of Oryza sativa BEI. These results indicate that starch-producing cyanobacteria have both type-I BE (BE3) and type-II BEs (BE1 and BE2) in terms of chain-length preferences, as is the case of plants
-
evolution
-
Cyanobacterium sp. NBRC 102756 belongs to the cyanobacteria that accumulate water-insoluble alpha-glucan similar to amylopectin rather than glycogen, the latter of which is more commonly produced in these organisms. The amylopectin-producing species invariably have three branching enzyme (BE) homologues, BE1, BE2, and BE3, all belonging to the glycoside hydrolase family 13, GH13, phylogenetic tree. The specific activity of BE3 is much lower than those of BE1 and BE2. Isozymes BE1 and BE2 show similar chain-length preference to BEIIb isoform of Oryza sativa, while the catalytic specificity of BE3 is similar to that of Oryza sativa BEI. These results indicate that starch-producing cyanobacteria have both type-I BE (BE3) and type-II BEs (BE1 and BE2) in terms of chain-length preferences, as is the case of plants
-
evolution
-
great variation exists as to the preference of branching enzymes of diffeent species for their acceptor chain, either A-chain or B-chain. Phylogenetic tree of alpha-glucan branching enzymes
-
malfunction
inhibitory effects of these hpSBEIIRNA constructs on the expression of SBEIIa and SBEIIb in maize endosperm, levels of ZmSBEII transcription and SBE activity in kernels of transgenic plants, overview. The transgenic maize lines show increased content of amylopectin chains with high-molecular weight compared to decreased low-molecular weight chains
malfunction
mutations of conserved residues in binding sites I and VI have a debilitating effect on the activity of the enzyme
malfunction
-
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
malfunction
-
enzyme mutations cause porphyria
metabolism
-
key biocatalyst in synthesis of polysaccharides
metabolism
key biocatalyst in synthesis of polysaccharides
metabolism
-
starch synthesis
metabolism
-
granule-bound proteins involved in amylopectin synthesis are partitioned into the starch granule as a result of their association within protein complexes, and strach synthase IIa plays a crucial role in trafficking starch synthase I and starch branching enzyme IIb into the granule matrix. A mutant starch synthase IIa that has lost catalytic activity and is inable to bind to starch additionally leads to greatly reduced activities of starch synthase I and starch branching enzyme IIb
metabolism
glycogen and starch branching enzymes catalyze the formation of alpha(1->6) linkages in storage polysaccharides by rearrangement of preexisting alpha-glucans. This reaction occurs through the cleavage of alpha(1->4) linkage and transfer in alpha(1->6) of the fragment in non-reducing position. These enzymes define major elements that control the structure of both glycogen and starch
metabolism
-
starch synthase and branching enzyme establish the two glycosidic linkages existing in starch. Both enzymes exist as several isoforms. 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. All starch synthase isoforms I-IV are able to interact with branching enzymes and form branched glucans
metabolism
the balance between branching and debranching is crucial for the synthesis of starch, as an excess of branching activity results in the formation of highly branched, water-soluble, poorly crystalline polyglucan
metabolism
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
metabolism
-
the following assembly mechanism is proposed. Polymer synthesis starts with GlgE and its donor substrate, alpha-maltose 1-phosphate, yielding a linear oligomer with a degree of polymerization (of about 16) sufficient for GlgB to introduce a branch. Branching involves strictly intrachain transfer to generate a C chain (the only constituent chain to retain its reducing end), which now bears an A chain (a nonreducing end terminal branch that does not itself bear a branch). GlgE preferentially extends A chains allowing GlgB to act iteratively to generate new A chains emanating from B chains (nonterminal branches that themselves bear a branch). Although extension and branching occur primarily with A chains, the other chain types are sometimes extended and branched such that some B chains (and possibly C chains) bear more than one branch
metabolism
the following assembly mechanism is proposed. Polymer synthesis starts with GlgE and its donor substrate, alpha-maltose 1-phosphate, yielding a linear oligomer with a degree of polymerization (of about 16) sufficient for GlgB to introduce a branch. Branching involves strictly intrachain transfer to generate a C chain (the only constituent chain to retain its reducing end), which now bears an A chain (a nonreducing end terminal branch that does not itself bear a branch). GlgE preferentially extends A chains allowing GlgB to act iteratively to generate new A chains emanating from B chains (nonterminal branches that themselves bear a branch). Although extension and branching occur primarily with A chains, the other chain types are sometimes extended and branched such that some B chains (and possibly C chains) bear more than one branch
metabolism
-
the following assembly mechanism is proposed. Polymer synthesis starts with GlgE and its donor substrate, alpha-maltose 1-phosphate, yielding a linear oligomer with a degree of polymerization (of about 16) sufficient for GlgB to introduce a branch. Branching involves strictly intrachain transfer to generate a C chain (the only constituent chain to retain its reducing end), which now bears an A chain (a nonreducing end terminal branch that does not itself bear a branch). GlgE preferentially extends A chains allowing GlgB to act iteratively to generate new A chains emanating from B chains (nonterminal branches that themselves bear a branch). Although extension and branching occur primarily with A chains, the other chain types are sometimes extended and branched such that some B chains (and possibly C chains) bear more than one branch
-
metabolism
-
the following assembly mechanism is proposed. Polymer synthesis starts with GlgE and its donor substrate, alpha-maltose 1-phosphate, yielding a linear oligomer with a degree of polymerization (of about 16) sufficient for GlgB to introduce a branch. Branching involves strictly intrachain transfer to generate a C chain (the only constituent chain to retain its reducing end), which now bears an A chain (a nonreducing end terminal branch that does not itself bear a branch). GlgE preferentially extends A chains allowing GlgB to act iteratively to generate new A chains emanating from B chains (nonterminal branches that themselves bear a branch). Although extension and branching occur primarily with A chains, the other chain types are sometimes extended and branched such that some B chains (and possibly C chains) bear more than one branch
-
metabolism
-
key biocatalyst in synthesis of polysaccharides
-
physiological function
-
the synthesis of maltodextrins by alpha-glucan phosphorylase Pho1 is markedly accelerated by branching enzyme isozymes, with the greatest effect being exhibited by the presence of branching isozyme BEI rather than by isozyme BEIIa or isozyme BEIIb. The enhancement of the activity of Pho1 by branching enzymes is not merely due to the supply of a non-reducing ends. At the same time, Pho1 greatly enhances the branching enzyme activity, possibly by generating a branched carbohydrate substrate which is used by branching enzyme with a higher affinity. The interaction between Pho1 and branching enzyme is not merely due to chain-elongating and chain-branching reactions, but occurs in a physically and catalytically synergistic manner by each activating the mutual capacity of the other, presumably forming a physical association of Pho1, isoform BEI and branched maltodextrins
physiological function
-
glycogen is a major polysaccharide of energy reservoir in animals and microorganisms. It is a highly branched polysaccharide, in which glucose residues are linked by alpha-1,4 glycosidic bonds to from linear chains and at every 10 residues, other linear chains are linked by alpha-1,6-glycosidic bonds to form side chains. Formation of side chains in glycogen is catalyzed by glycogen branching enzyme (GBE) or branching enzyme (BE). GBE catalyzes formation of alpha-1,6-glycosidic linkage by cleaving alpha-1,4 linkages of substrate and transferring the non-reducing end of the chain to an acceptor
physiological function
rice branching enzyme isozymes BEI, BEIIa, or BEIIb accelerate the reaction velocity of starch synthase SSI, but not of SSIIa or SSIIIa, in rice. The interaction between starch synthase I (SSI) and branching enzyme (BE) is established by stimulation of SSI activity with BE and by activation of the BE activity by SSI
physiological function
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
physiological function
starch branching enzyme IIb plays a crucial role in amylopectin biosynthesis in maize endosperm by defining the structural and functional properties of storage starch and is regulated by protein phosphorylation
physiological function
starch synthesis requires several enzymatic activities including branching enzymes (BEs) responsible for the formation of alpha(1->6) linkages. Distribution and number of these linkages are further controlled by debranching enzymes that cleave some of them, rendering the polyglucan water-insoluble and semi-crystalline. The activity of BEs and debranching enzymes is mandatory to sustain normal starch synthesis
physiological function
the branching enzyme is responsible for all branching of glycogen and starch. It has both alpha-1,4-amylase activity and alpha-1,6-transferase activity
physiological function
-
the enzyme GlgB is essential for the biosynthesis of branched glucan and modulates pathogenesis and survival, it is the key enzyme involved in the biosynthesis of alpha-glucan, which plays a significant role in the virulence and pathogenesis of Mycobacterium tuberculosis
physiological function
-
the enzyme is a regulator of iron homeostasis. The enzyme interacts physically with the holoform of iron regulatory protein 1A (IRP1A) and Cisd2, an ortholog of vertebrate mitoNEET. This synergistic interaction ensures that holo-IRP1A remains functional
physiological function
-
starch branching enzyme IIb plays a crucial role in amylopectin biosynthesis in maize endosperm by defining the structural and functional properties of storage starch and is regulated by protein phosphorylation
-
additional information
-
branching patterns of the truncation mutants and the swapping mutant. Branching patterns of VvGBE wild-type
additional information
molecular dynamics simulation and modeling of phosphorylation of enzyme mutants
additional information
-
molecular dynamics simulation and modeling of phosphorylation of enzyme mutants
additional information
six distinct oligosaccharide binding sites on the surface of the branching enzyme, most of which surround the edge of the beta-barrel domain and are quite far from the active site. No evidence of oligosaccharide binding in the active site of the enzyme, the closest bound oligosaccharide resides almost 18 A from the active site
additional information
-
six distinct oligosaccharide binding sites on the surface of the branching enzyme, most of which surround the edge of the beta-barrel domain and are quite far from the active site. No evidence of oligosaccharide binding in the active site of the enzyme, the closest bound oligosaccharide resides almost 18 A from the active site
additional information
the branching enzyme's origin has only a limited impact on establishing essential characteristics of starch
additional information
-
the branching enzyme's origin has only a limited impact on establishing essential characteristics of starch
additional information
Tyr352, Glu513, and Ser349 are important for mSBEIIa activity while Arg456 is important for determining the position at which the linear glucan is cut, enzyme active site structure, molecular dynamics simulations and modeling, overview
additional information
-
Tyr352, Glu513, and Ser349 are important for mSBEIIa activity while Arg456 is important for determining the position at which the linear glucan is cut, enzyme active site structure, molecular dynamics simulations and modeling, overview
additional information
-
molecular dynamics simulation and modeling of phosphorylation of enzyme mutants
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DELTA1-63
-
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
-
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-
-
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
Y300A
-
mutant enzyme shows less than 1% of the wild-type activity
Y300D
-
mutant enzyme shows less than 1% of the wild-type activity
Y300F
-
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
Y300L
-
mutant enzyme shows less than 1% of the wild-type activity
Y300S
-
mutant enzyme shows less than 1% of the wild-type activity
Y300W
-
mutant enzyme shows less than 1% of the wild-type activity
D270A
mutant with about 10% relative enzyme activity compared to wild-type enzyme
D344A
mutant without enzyme activity
E399A
mutant with about 5% relative enzyme activity compared to wild-type enzyme
E399Q
supposed general acid/base residue, crystallization data
G468D
mutant with about 95% relative enzyme activity compared to wild-type enzyme
H275A
mutant without enzyme activity
H467A
mutant without enzyme activity
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
-
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
-
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
-
D15A
-
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
-
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
-
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
-
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
-
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
E185Q
enzymatic activity is abolished
W22A
complete loss of activity
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
R384A
-
mutation causes almost complete inactivation
R384E
-
mutation causes almost complete inactivation
R384K
-
residual activity of the mutant enzyme is 5% of the wild-type enzyme
R384Q
-
mutation causes almost complete inactivation
R384S
-
mutation causes almost complete inactivation
R456K
site-directed mutagenesis, the mutant shows similar activity compared to wild-type enzyme mSBEIIa
S147A
site-directed mutagenesis
S204A
site-directed mutagenesis
S286A
site-directed mutagenesis
S286A/S297A/S649A
site-directed mutagenesis
S297A
site-directed mutagenesis
S297A/S298A
site-directed mutagenesis
S298A
site-directed mutagenesis
S349F
site-directed mutagenesis, creates an additional binding site for glucose, the mutant shows a much lower activity compared to wild-type enzyme mSBEIIa
S568A
site-directed mutagenesis
S598A
site-directed mutagenesis
S649A
site-directed mutagenesis
S659A
site-directed mutagenesis
S699A
site-directed mutagenesis
S705A
site-directed mutagenesis
Y352F
site-directed mutagenesis, , the mutant shows a much lower activity compared to wild-type enzyme mSBEIIa
S204A
-
site-directed mutagenesis
-
S286A
-
site-directed mutagenesis
-
S297A
-
site-directed mutagenesis
-
S298A
-
site-directed mutagenesis
-
DELTA1-112
-
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
-
truncated enzyme transferrs a greater amount of longer chains than the wild-type enzyme
additional information
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
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
-
enzyme overexpression results in decrease cell proliferation when treated by deltamethrin
additional information
CT Dg, truncated at 3' end
additional information
-
CT Dg, truncated at 3' end
additional information
GGR, construction of chimeric genes, with C-domain of GBE of Deinococcus radiodurans
additional information
-
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
-
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
-
NT Dg, tuncated at 5' end
additional information
RGG, construction of chimeric genes, with N-domain of GBE of Deinococcus radiodurans
additional information
-
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
-
RRG, construction of chimeric genes, with N-domain and A-domain of GBE of Deinococcus radiodurans
additional information
CTT Dr, tuncated at 3' end
additional information
-
CTT Dr, tuncated at 3' end
additional information
GGR, construction of chimeric genes, with N-domain and A-domain of GBE of Deinococcus geothermalis
additional information
-
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
-
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
-
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
-
RRG, construction of chimeric genes, with C-domain of GBE of Deinococcus geothermalis
additional information
-
CTT Dr, tuncated at 3' end
-
additional information
-
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
-
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
concominant reduction in SBE IIb with suppression of SBE IIa
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
SBE IIa-, transgenic line with suppressed 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
-
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
-
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
-
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
-
a mutant lacking the N1 domain, i.e. lacking N-terminal residues 1-108, shows about 30% decrease in specific activity
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
-
ae mutant, BEIIb-deficient mutant
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
-
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
-
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
construction of chimeric enzymes of the isoenzymes PvSBE1 and PvSBE2
additional information
construction of chimeric enzymes of the isoenzymes PvSBE1 and PvSBE2
additional information
-
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
-
N-termial truncated enzyme of PvSBE2. Delta46-PvSBE2 has no branching enzyme activity.
additional information
-
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
-
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
-
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
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
-
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
-
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
-
generation of N- and C-terminally truncated enzyme mutants. Activities of kinases on wild-type and enzyme mutants, overview
additional information
-
generation of N- and C-terminally truncated enzyme mutants. Activities of kinases on wild-type and enzyme mutants, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
complete cDNA sequence for the wild-type gene and the nonsense mutation in which 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
expressed in Escherichia coli
-
expressed in Escherichia coli BL21 (DE3)
-
expressed in Escherichia coli BL21 cells
expressed in Escherichia coli BL21 Star (DE3) cells
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli Bl21-CodonPlus(DE3)-RIL and pET21a(+)
expressed in Escherichia coli DG5alpha
expressed in Escherichia coli strain KV832
expression in Bacillus subtilis
expression in Escherichia coli
expression in Escherichia coli AD494
-
expression in Escherichia coli BL21
expression in Escherichia coli, chimeric enzymes consisting of part mBE I and mBE II
-
expression in Escherichia coli, full-length enzyme and a truncated enzyme form missing the first 107 amino acids
-
expression in Escherichia coli, glycogen branching enzyme gene existing in tandem with the glycogen debranching enzyme
-
expression in Escherichia coli. Multiple forms of the enzyme exist which differ mainly in the length of a polyglutamic acid repeat at the C-terminus of the protein, SBE A1 to SBE A-6. Expression of an antisense SBE A RNA in transgenic potato
-
expression in mosquito C6/36 cells
expression in Saccharomyces cerevisiae, each of the three isoforms is functional in yeast cells
-
expression of Escherichia coli branching enzyme in caryopses of transgenic Oryza satica results in amylopectin with an increased degree of branching. Expression of Escgerichia coli glgB in rice results in an increase in the short-chain fractions with DP between 6 and 10, which should have a significant effect on retrogradation
-
expression of mSBEIIa in Escherichia coli as Strep-tagged enzyme
gene gkgB, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
gene glgB, functional recombinant expression of the bacterial enzyme in Arabidopsis thaliana be2 be3 double mutant leaves, ecotype WS, which is devoid of BE activity and consequently free of starch. The synthesis of a water-insoluble, partly crystalline, amylose-containing starch-like polyglucan is restored in GlgB-expressing transgenic plants, morphology of purified insoluble and soluble polyglucans, phenotype, overview
gene nbrc_glgB1, functional recombinant expression of N-terminally His-tagged isozyme BE1 in Escherichia coli
Cyanobacterium sp.
gene nbrc_glgB2, functional recombinant expression of His-tagged isozyme BE2 in Escherichia coli
Cyanobacterium sp.
gene nbrc_glgB3, functional recombinant expression of His-tagged isozyme BE3 in Escherichia coli
Cyanobacterium sp.
gene RmGBE, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of N-terminally His-tagged enzyme in Escherichia coli strain BL21
gene SBE I, DNA and amino acid sequence determination and analysis of SBE I from two accessions, Y59 and Y63, genetic structure, sequence comparisons and phylogenetic analysis, enzyme expression analysis by real-time quantitative PCR
gene Sbe2a, recombinant expression of N-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)pLysS
gene TcGBE, recombinant expression in Escherichia coli strain BL21(DE3)
-
isoenzymes PySBE1 and PySBE2, expression in Escherichia coli
-
isolation and characterization of a starch-branching enzymes IIa cDNA
-
isolation of a cDNA encoding a granule-bound 152-kilodalton starch-branching enzyme, a non-full-length cDNA clone
-
isolation of wheat SBE IIb cDNA
overexpression in Escherichia coli BL21
recombinant expression of His-tagged isozymes rBE2 and rBE3 in Escherichia coli strain BL21(DE3) and in strain DELTAglgCAP with BL21(DE3) background
-
recombinant expression of wild-type and mutant enzymes
recombinant overexpression of endogenaous enzyme SBEII in Solanum tuberosum. A complete cDNA of potato SBEII is unable to be propagated in Escherichia coli, therefore a complete but hybrid SBEII intragene containing a single intron to prevent bacterial translation is assembled from cDNA and genomic DNA fragments
-
the barley clone encodes the complete mature SBEI but is truncated by approximately 150 bases at the 5'-end
the gene encoding the branching enzyme from Anaerobranca gottschalkii is fused with a twin arginine translocation protein secretory-pathway-dependent siganl sequence from Escherichia coli and expressed in Staphylococcus carnosus
transformed to Agrobacterium tumefaciens EHA 105, generation of transgenic Oryza sativa, expression in Escherichia coli AD494
two closely related cDNAs encode starch branching enzyme from Arabidopsis thaliana
-
wild-type and mutant enzymes R384A, R384S, R384Q, E384E and R384K
-
-
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells
expression in Bacillus subtilis
-
expression in Bacillus subtilis
expression in Bacillus subtilis
expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli BL21
-
expression in Escherichia coli BL21
expression in Escherichia coli BL21
expression in Escherichia coli BL21
expression in Escherichia coli BL21
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.