Information on EC 2.4.1.18 - 1,4-alpha-glucan branching enzyme

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY
2.4.1.18
-
RECOMMENDED NAME
GeneOntology No.
1,4-alpha-glucan branching enzyme
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Transfers a segment of a (1->4)-alpha-D-glucan chain to a primary hydroxy group in a similar glucan chain
show the reaction diagram
-
-
-
-
Transfers a segment of a (1->4)-alpha-D-glucan chain to a primary hydroxy group in a similar glucan chain
show the reaction diagram
interchain mechanism
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
glycosyl group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
glycogen biosynthesis I (from ADP-D-Glucose)
-
glycogen biosynthesis II (from UDP-D-Glucose)
-
Metabolic pathways
-
Starch and sucrose metabolism
-
starch biosynthesis
-
SYSTEMATIC NAME
IUBMB Comments
(1->4)-alpha-D-glucan:(1->4)-alpha-D-glucan 6-alpha-D-[(1->4)-alpha-D-glucano]-transferase
Converts amylose into amylopectin. The accepted name requires a qualification depending on the product, glycogen or amylopectin, e.g. glycogen branching enzyme, amylopectin branching enzyme. The latter has frequently been termed Q-enzyme.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
(1-4)-alpha-D-glucan:(1-4)-alpha-D-glucan 6-alpha-D-[(1-4)-alpha-D-glucano]-transferase
-
-
1,4-alpha-glucan branching enzyme
O66936
-
1,4-alpha-glucan branching enzyme
Q1IZQ3
-
1,4-alpha-glucan branching enzyme
Q9RTB7
-
1,4-alpha-glucan branching enzyme
Q9RTB7
-
-
1,4-alpha-glucan branching enzyme
-
-
1,4-alpha-glucan branching enzyme
P30538
-
1,4-alpha-glucan branching enzyme
Geobacillus stearothermophilus TRBE14
-
-
-
1,4-alpha-glucan branching enzyme 1
-
-
alpha-1,4-glucan branching enzyme
Q8DT52
-
alpha-1,4-glucan:alpha-1,4-glucan 6-glycosyltransferase
-
-
-
-
alpha-1,4-glucan:alpha-1,4-glucan-6-glycosyltransferase
-
-
-
-
alpha-glucan-branching glycosyltransferase
-
-
-
-
amylo-(1,4-1,6)-transglycosylase
-
-
-
-
amylose isomerase
-
-
-
-
BBE
Bacillus subtilis 168
-
-
-
BE
-
-
-
-
BE-01
Geobacillus stearothermophilus TRBE14
-
-
-
BE-02
O66936
-
BE1
-
a gene putatively encoding an isoform of a starch-branching enzyme in Arabidopsis thaliana genome. AGI Gene Identification: At3g20440. The protein corresponding to the BE1 gene contains a predicted chloroplast-targeting peptide of 49 amino acids. The sequence homology between BE1 and both BE2 and BE3 is 28% and 27% amino acid identity, respectively.
BE2
-
a gene putatively encoding an isoform of a starch-branching enzyme in Arabidopsis thaliana genome. AGI Gene Identification: At5g03650. The protein corresponding to the BE2 gene contains a predicted chloroplast-targeting peptide of 61 amino acids. BE2 and BE3 are two highly conserved proteins with over 75% amino acid identity.
BE3
-
a gene putatively encoding an isoform of a starch-branching enzyme in Arabidopsis thaliana genome. AGI Gene Identification: At2g36390. The protein corresponding to the BE3 gene contains a predicted chloroplast-targeting peptide of 37 amino acids. BE2 and BE3 are two highly conserved proteins with over 75% amino acid identity.
BEI
Q01401
-
BEIIa
-
-
BEIIb
-
-
branching factor, enzymatic
-
-
-
-
branching glycosyltransferase
-
-
-
-
Dr GBE
Q9RTB7
-
-
enzyme Q
-
-
-
-
full-length starch branching enzyme II
Q4VUI1
-
GBE
-
-
-
-
GBE
Q4F8A2, Q962G8
-
GBE1
-
-
GBE1 enzyme
Q6EAS5
-
GH13 GBE
Q1IZQ3
-
GH13 GBE
Q9RTB7
-
GH13 GBE
Q9RTB7
-
-
GlgB
Q10625
glycogen branching enzyme
glucosan transglycosylase
-
-
-
-
glycogen branching enzyme
-
-
-
-
glycogen branching enzyme
Q4F8A2, Q962G8
-
glycogen branching enzyme
Q1IZQ3
-
glycogen branching enzyme
Q9RTB7
-
glycogen branching enzyme
Q9RTB7
-
-
glycogen branching enzyme
-
-
glycogen branching enzyme
Q8DT52
-
glycogen branching enzyme
-
-
glycogen branching enzyme GBE1
Q6EAS5
-
glycosyltransferase, alpha-glucan-branching
-
-
-
-
IbSBEI
Q18PQ3
sweet potato SBEI gene.
mSBEIIa
O24421
-
ORF Rv1326c
Q10625
in Mycobacterium tuberculosis H37Rv codes for a enzymatically active protein that utilizes amylose as the substrate
PvSBE1
Q9XIS4
-
PvSBE2
Q9XIS5
-
Q-enzyme
-
-
-
-
Q-enzyme
-
-
QE
-
-
-
-
rBEI
-
-
rice branching enzyme I
-
-
SBE
-
-
-
-
SBE
-
starch-branching enzyme
SBE
Q18PQ3
starch-branching enzyme
SBE
-
starch-branching enzyme
SBE
Sorghum sp.
-
-
SBE
Q4VUI1
-
SBE IIa
Q9ZTB7
-
SBE Iib
Q7G0S2
-
SBE Iib
Q9ZTB6
-
SBE Iib
-
-
SBE1
Q01401
gene name
SBEI
Sorghum sp.
-
-
SBEIIA
Sorghum sp.
-
-
SBEIIB
Sorghum sp.
-
-
SmGBE
Q8DT52
-
starch branching enzyme
-
-
-
-
starch branching enzyme
-
-
starch branching enzyme
Q9ZTB6, Q9ZTB7
-
starch branching enzyme
-
-
starch branching enzyme
Sorghum sp.
-
-
starch branching enzyme
-
-
starch branching enzyme I
Q01401
-
starch branching enzyme I
-
-
starch branching enzyme II
-
-
starch branching enzyme II
A9ZPD1
-
starch branching enzyme IIa
-
-
starch branching enzyme IIb
Q24M29
-
starch branching enzyme IIb
-
-
starch branching enzyme SBE I
Q7XZK6
-
starch branching enzyme SBE IIb
Q7XZK7
-
starch branching enzyme-I
-
-
starch-branching enzyme
-
-
starch-branching enzyme Ia
O24421
-
starch-branching enzyme IIa
O24421
-
starch-branching enzyme IIb
O81387
-
starch-branching enzymes IIa
Q9ZTB7
-
starch-branching enzymes IIa
-
-
starch-branching enzymes IIb
Q7G0S2
-
starch-branching enzymes IIb
-
-
TK1436
Q5JDJ7
encodes a branching enzyme from Thermococcus kodakaraensis belonging to the GH-57 family. The TK1436 protein contains neither alpha-galactosidase nor pullulanase activity.
VsbeII
Q4VUI1
-
CAS REGISTRY NUMBER
COMMENTARY
9001-97-2
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
the protein consists of 613 amino acids. The branching enzyme of Anaerobranca gottschalkii lacks the N-terminal extension of approximately 100 amino acids found in the branching enzymes of Escherichia coli and its close phylogenetic relatives. The absence of a signal sequence indicates that the branching enzyme is an intracellular enzyme.
Swissprot
Manually annotated by BRENDA team
strain VF5
UniProt
Manually annotated by BRENDA team
two isoforms
-
-
Manually annotated by BRENDA team
strain 168
-
-
Manually annotated by BRENDA team
Bacillus subtilis 168
strain 168
-
-
Manually annotated by BRENDA team
deltamethrin resistance
Q4F8A2
UniProt
Manually annotated by BRENDA team
strain DSM 11300
UniProt
Manually annotated by BRENDA team
Norwegian Forest Cat
-
-
Manually annotated by BRENDA team
Geobacillus stearothermophilus TRBE14
strain TRBE14
-
-
Manually annotated by BRENDA team
Gossypium sp.
-
-
-
Manually annotated by BRENDA team
Golf cultivar
SwissProt
Manually annotated by BRENDA team
multiple isoforms: starch-branching enzymes IIa and starch-branching enzymes IIb
SwissProt
Manually annotated by BRENDA team
sweet potato IbSBEI gene. Full-length cDNA is 2870 bp long, this cDNA is closest to that of potato gene (StSBEI), they are 80.1% identical.; sweet potato, Kokei 14
Swissprot
Manually annotated by BRENDA team
the primary amino acid sequence has four cysteine residues at position: 95, 193, 617 and 658, therefore there is a possibility of forming intramoleculare disulfide bonds. The two closely migrating bands of purified protein on a non-reducing SDS-PAGE might be due to the presence of two populations of different confomations of the same protein: the oxidized and the reduced.; H37Rv
Swissprot
Manually annotated by BRENDA team
isoform branching enzyme I
UniProt
Manually annotated by BRENDA team
multiple isoforms
-
-
Manually annotated by BRENDA team
-
A9ZPD1
UniProt
Manually annotated by BRENDA team
L. Toramame
-
-
Manually annotated by BRENDA team
3 enzyme form: 80000 Da, 97000 Da, 103000 Da
-
-
Manually annotated by BRENDA team
two isoforms
-
-
Manually annotated by BRENDA team
Kari-Mtama1 cultivar
SwissProt
Manually annotated by BRENDA team
Sorghum sp.
-
-
-
Manually annotated by BRENDA team
member of family GH57
Swissprot
Manually annotated by BRENDA team
TK1436 encodes a protein of 675 aa; hyperthermophilic archaeon
Swissprot
Manually annotated by BRENDA team
cultivar BY535 with a high starch content and culitvar JM20 with a low starch content
-
-
Manually annotated by BRENDA team
cultivar Chinese Spring
SwissProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
2 isoforms: starch branching enzyme I, starch branching enzyme IIb
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
metabolism
-, O66936
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
Geobacillus stearothermophilus TRBE14
-
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
amylopectin
amylopectin with additional alpha-1,6-glucosidic linkages
show the reaction diagram
-
-
-
-
?
amylopectin
amylopectin with additional alpha-1,6-glucosidic linkages
show the reaction diagram
-
-
-
?
amylopectin
amylopectin with additional alpha-1,6-glucosidic linkages
show the reaction diagram
-
-
-
-
?
amylopectin
amylopectin with additional alpha-1,6-glucosidic linkages
show the reaction diagram
-
-
-
-
?
amylopectin
amylopectin with additional alpha-1,6-glucosidic linkages
show the reaction diagram
-
-
-
-
?
amylopectin
amylopectin with additional alpha-1,6-glucosidic linkages
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
Q9XIS4, Q9XIS5
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
show the reaction diagram
-
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
?
show the reaction diagram
-
-
-
-
?
amylopectin
?
show the reaction diagram
Q9ZTB6, Q9ZTB7
-
-
-
?
amylopectin
?
show the reaction diagram
-
-
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
?
show the reaction diagram
-
-
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
?
show the reaction diagram
-
-
the amount of short chains with a degree of polymerization of 6-8 is significantly increased in the product of Bacillus cereus
-
?
amylopectin
?
show the reaction diagram
-
assay at 30C, 20 min
-
-
?
amylopectin
?
show the reaction diagram
Q01401
assay at 30C, reaction terminated by heating at 95C for 5 min
-
-
?
amylopectin
?
show the reaction diagram
-
assay at pH 7.5
-
-
?
amylopectin
?
show the reaction diagram
-, Q1IZQ3
iodine assay
-
-
?
amylopectin
?
show the reaction diagram
-, Q9RTB7
iodine assay
-
-
?
amylopectin
?
show the reaction diagram
Q9RTB7
iodine assay
-
-
?
amylopectin
highly branched cyclic dextrin
show the reaction diagram
-
-
-
-
?
amylopectin
amylopectin containing alpha-1,6-glucosidic linkages
show the reaction diagram
-
-
-
-
?
amylose
amylose containing alpha-1,6-glucosidic linkages
show the reaction diagram
-
-
-
-
?
amylose
amylose containing alpha-1,6-glucosidic linkages
show the reaction diagram
-
-
-
-
?
amylose
amylose containing alpha-1,6-glucosidic linkages
show the reaction diagram
-
-
-
-
-
amylose
amylose containing alpha-1,6-glucosidic linkages
show the reaction diagram
-
-
-
-
?
amylose
amylose containing alpha-1,6-glucosidic linkages
show the reaction diagram
-
-
-
?
amylose
amylose containing alpha-1,6-glucosidic linkages
show the reaction diagram
-
-
-
-
?
amylose
amylose containing alpha-1,6-glucosidic linkages
show the reaction diagram
-
-
-
-
?
amylose
amylose containing alpha-1,6-glucosidic linkages
show the reaction diagram
-, Q10625
-
-
-
?
amylose
amylose containing alpha-1,6-glucosidic linkages
show the reaction diagram
-
-
characterization of products, smallest chains transferred contain 5-7 glucose units
?
amylose
amylose containing alpha-1,6-glucosidic linkages
show the reaction diagram
-
potato amylose
-
-
?
amylose
amylose containing alpha-1,6-glucosidic linkages
show the reaction diagram
-
at 35C the enzyme does not act rapidly on such chains unless they are about 40 glucose units or more in length, at 4C the minimum length falls to about 10
-
?
amylose
amylose containing alpha-1,6-glucosidic linkages
show the reaction diagram
-
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
-
-
-
amylose
amylose containing alpha-1,6-glucosidic linkages
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
Q9XIS4, Q9XIS5
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
show the reaction diagram
-
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
show the reaction diagram
Q93HU3
potato type III amylose
-
-
?
amylose
?
show the reaction diagram
-
-
-
-
?
amylose
?
show the reaction diagram
Q9ZTB6, Q9ZTB7
-
-
-
?
amylose
?
show the reaction diagram
A9ZPD1
-
-
-
?
amylose
?
show the reaction diagram
-
assay at 30C, 20 min
-
-
?
amylose
?
show the reaction diagram
Q01401
assay at 30C, reaction terminated by heating at 95C for 5 min
-
-
?
amylose
?
show the reaction diagram
-
assay at pH 30C, pH 8.0
-
-
?
amylose
?
show the reaction diagram
Q8DT52
assay at pH 5.0, 37C
-
-
?
amylose
?
show the reaction diagram
Q4VUI1, -
assay at pH 7.0, 30C for 90 min
-
-
?
amylose
?
show the reaction diagram
-
assay at pH 7.5
-
-
?
amylose
?
show the reaction diagram
-, Q1IZQ3
branching assay, at pH 8.0, reaction stopped by boiling for 5 min
-
-
?
amylose
?
show the reaction diagram
-, Q9RTB7
branching assay, at pH 8.0, reaction stopped by boiling for 5 min
-
-
?
amylose
?
show the reaction diagram
-
dinitrosalicylate method, assay at pH 6.0, 70C
-
-
?
amylose
?
show the reaction diagram
Q9RTB7
branching assay, at pH 8.0, reaction stopped by boiling for 5 min
-
-
?
amylose
branched polyglucan
show the reaction diagram
Q1IZQ3
using linear amylose synthesized in a tandem reaction by potato phosphorylase
-
-
?
Glycogen
?
show the reaction diagram
-
from E. coli and rabbit liver, little activity
-
-
?
Maltohexaose
?
show the reaction diagram
-
dinitrosalicylate method, assay at pH 6.0, 70C
-
-
?
Pullulan
?
show the reaction diagram
-
dinitrosalicylate method, assay at pH 6.0, 70C
-
-
?
starch
?
show the reaction diagram
Q8DT52
assay at pH 5.0, 37C
-
-
?
starch
starch containing alpha-1,6-glucosidic linkages
show the reaction diagram
-, Q10625
-
-
-
?
waxy maize starch
?
show the reaction diagram
-
-
-
-
?
maltopentaose
?
show the reaction diagram
-
dinitrosalicylate method, assay at pH 6.0, 70C
-
-
?
additional information
?
-
-
the enzyme forms SBE I and SBE II mainly branch the dextrins by intrachain branching
-
-
-
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
?
-
-
each isoform of the Q-enzyme plays a distinct role in starch biosynthesis
-
-
-
additional information
?
-
-
starch-branching enzyme and glycogen synthase work in a cyclically interdependent fashion
-
-
-
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
?
-
-
each branching enzyme isoform is involved in a different phase of glycogen synthesis
-
-
-
additional information
?
-
-
the enzyme is responsible for the formation of the alpha-1,6 linkages in the glycogen molecule
-
-
-
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
?
-
Q6EAS5
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
?
-
O24421, O81387
in absence of starch-branching enzyme IIb, the further absence of starch-branching enzyme Ia leads to increased branching
-
-
-
additional information
?
-
O04074
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
?
-
Q3BJY5
cyclodextrins neither serve as donors nor as acceptors
-
-
-
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 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
?
-
Q93HU3
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
?
-
Q5JDJ7, -
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
?
-
-
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
?
-
-, Q10625
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
?
-
Bacillus subtilis 168
-
the enzyme performs branching of amylose from Oryza sative starch, product identification and determination, overview
-
-
-
pea starch
?
show the reaction diagram
-
-
-
-
?
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
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
each isoform of the Q-enzyme plays a distinct role in starch biosynthesis
-
-
-
additional information
?
-
-
starch-branching enzyme and glycogen synthase work in a cyclically interdependent fashion
-
-
-
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
?
-
-
each branching enzyme isoform is involved in a different phase of glycogen synthesis
-
-
-
additional information
?
-
-
the enzyme is responsible for the formation of the alpha-1,6 linkages in the glycogen molecule
-
-
-
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
?
-
Q6EAS5
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
?
-
O24421, O81387
in absence of starch-branching enzyme IIb, the further absence of starch-branching enzyme Ia leads to increased branching
-
-
-
additional information
?
-
O04074
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
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ba2+
-
about 2.5% decreased enzyme activity, 5 mM
Ca2+
-, Q10625
the cation has no effect on the activity. The reaction mixture is incubated in the presence of 10 mM of the cation for 30 min
Ca2+
-
about 3.6% decreased enzyme activity, 5 mM
Co2+
-
upregulates GBE1 gene transcription
Cu2+
-, Q10625
maximum inhibition is observed, where about 40% of the activity is retained. The reaction mixture is incubated in the presence of 10 mM of the cation for 30 min
Cu2+
-
about 16.4% decreased enzyme activity, 5 mM
Fe2+
-
about 58.3% decreased enzyme activity, 5 mM
Mg2+
-, Q10625
the cation has no effect on the activity. The reaction mixture is incubated in the presence of 10 mM of the cation for 30 min
Mg2+
-
15% increased enzyme activity, 5 mM
Mn2+
-
about 53.5% decreased enzyme activity, 5 mM
Ni2+
-
upregulates the GBE1 gene both in vitro and in vivo
Ni2+
-
upregulates the GBE1 gene both in vitro and in vivo, in PW cell line, liver, lung, kidney and spleen. Ni2+ mimics hypoxia, GBE1 is upregulated by hypoxia
Zn2+
-, Q10625
about 70% activity retained. The reaction mixture is incubated in the presence of 10 mM of the cation for 30 min
Zn2+
-
about 61.8% decreased enzyme activity, 5 mM
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Ca2+
Q3BJY5
the additon of 2.5 mM of Ca2+ slightly inhibits the enzyme
CaCl2
-
0.06 M, 14% inhibition
CaCl2
-
10 mM, 50% inhibition. 100 mM, complete inactivation
citrate
-
-
Co2+
Q3BJY5
the additon of 2.5 mM of Co2+ slightly inhibits the enzyme
CuSO4
-
1 mM, complete inactivation
DMSO
-
about 22.9% decreased enzyme activity, 10%
EDTA
Q3BJY5
enzymatic activity is abolished in the presence of EDTA
EDTA
-
about 44.2% decreased enzyme activity, 5 mM
ethanol
-
about 57.2% decreased enzyme activity, 10%
Fe3+
Q3BJY5
enzymatic activity is abolished in the presence of Fe3+
-
HgCl2
-
1 mM, complete inactivation
maltoheptaose
-
40% inhibition at 15 mM
methanol
-
about 45.2% decreased enzyme activity, 10%
Mg2+
Q3BJY5
the additon of 2.5 mM of Mg2+ slightly inhibits the enzyme
MgCl2
-
0.08 M, 41% inhibition
MgCl2
-
1 mM, complete inactivation
Mn2+
Q3BJY5
the additon of 2.5 mM of Mn2+ slightly inhibits the enzyme
NaCl
-
concetration of 2-4 M NaCl
Urea
-
50% inhibition at 0.4 M, complete inhibition at 2 M. Up to 2 M, reversible inhibition
Zn2+
Q3BJY5
enzymatic activity is abolished in the presence of Zn2+
ZnCl2
-
1 mM, complete inactivation
MnCl2
-
1 mM, complete inactivation
additional information
-, Q10625
not inhibitory: ADP, ADP glucose, tunicamycin, castenospermine, nojirimycin, or acarbose
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(NH4)2SO4
-
10 mM, activates
3-hydroxy-2-oxopropyl dihydrogen phosphate
-
10 mM, activates
3-phosphoglycerate
-
10 mM, activates
acetate
-
activation
ADP
-
10 mM, activates
ADPglucose
-
10 mM, activates
AMP
-
10 mM, activates
ATP
-
10 mM, activates
Borate
-
activation
citrate
-
0.15 M sodium citrate, 2fold stimulation
citrate
-
activation
citrate
-
3.3fold activation at 0.3 M, enzyme form KBE1 and KBE2; activation
citrate
-
0.3 M, more than 3fold stimulation of activity of isoenzyme SBE2, no effect on activity of isoenzyme SBE1
citrate
-
in the presence of 0.1 M citrate, the activity of the active enzyme increases
diphosphate
-
10 mM, activates
dithiothreitol
Q3BJY5
addition of dithiothreitol results in an increase in the branching enzyme activity up to 2.4fold at concentrations greater than 1 mM. This activation is not observed if idoacetamide is simultaneously present.
fructose 1,6-diphosphate
-
10 mM, activates
fructose 6-phosphate
-
10 mM, activates
glucose 1-phosphate
-
10 mM, activates
NaCl
-
concentration of 0.5 - 1 M NaCl
NADP+
-
10 mM, activates
phosphate
-
activates
phosphate
-
activates
phosphate
-
activates
phosphoenolpyruvate
-
10 mM, activates
potassium alpha-D-glucose 1-phosphate
-
0.05 M, 2fold stimulation
potassium alpha-D-glucose 1-phosphate
-
activation
ribose 5-phosphate
-
10 mM, activates
RuBP
-
10 mM, activates
-
glucose 6-phosphate
-
10 mM, activates
additional information
-
peak of activities at the 28th day post anthesis, higher activity in the cultivar with a high starch content
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0056
-
Amylopectin
-
pH 6.4, 30C, type IV amylopectin
0.00018
-
Amylose
-
amylose AS-1160, degree of polymerization of approximately 6,510, isoform BEI, pH 7.5, 30C
0.0009
-
Amylose
-
amylose AS-1160, degree of polymerization of approximately 6,510, isoform BEI, pH 7.5, 30C
0.0012
-
Amylose
-
amylose AS-1160, degree of polymerization of approximately 6,510, isoform BEI, pH 7.5, 30C
0.0068
-
Amylose
-
pH 7.5, 30C, reduced amylose AS-320, wild-type enzyme
0.0113
-
Amylose
-
pH 7.5, 30C, reduced amylose AS-320, mutant enzyme R384K
0.0142
-
Amylose
-
amylose AS-320, pH 7.0, 30C, wild-type enzyme
0.0175
-
Amylose
-
amylose AS-320, pH 7.0, 30C, mutant enzyme Y300F
0.059
-
Amylose
-
amylose AS-320, pH 7.0, 30C, enzyme forms BE I and BE II
0.083
-
Amylose
-
amylose AS-320, pH 7.0, 30C, chimeric enzyme form BE II-I BspHI
2
-
Amylose
-
reduced amylose of an average chain-length 405, enzyme isoenzyme BE I
10
-
Amylose
-
reduced amylose of an average chain-length 405, enzyme isoenzyme BE IIa
11
-
Amylose
-
reduced amylose of an average chain-length 405, enzyme isoenzyme BE IIb
additional information
-
additional information
-
amylose: 0.02 mg/ml
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
amylose: 0.018 mg/ml
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
amylose: 0.29 mg/ml
-
additional information
-
additional information
-
Km-value for amylose, enzyme form KBE1: 1.27 mg/ml. Km-value for amylose, enzyme form KBE2: 0.74 mg/ml
-
additional information
-
additional information
-
Km-value for amylose, enzyme form WBE-IB: 0.11 mg/ml, Km-value for amylose, enzyme form WBE-IAD: 0.3 mg/ml, Km-value for amylose, enzyme form WBE-II: 0.65 mg/ml
-
additional information
-
additional information
-
Km-value for amylose, isoenzyme SBE2: 1.27 mg/ml. Km-value for amylose, isoenzyme SBE1: 0.46 mg/ml
-
additional information
-
additional information
-
Km value of the chimeric enzyme (1Na/2Nb)-II is 0.63 mg/ml. The Km value of D15A-PvSBE2 is 1.3 mg/ml, 1.52 mg/ml for D15E-PvSBE2, 1.57 mg/ml for R28A-PvSBE2, 1.55 mg/ml for R28K-PvSBE2 and 1.59 mg/ml for H24A-PvSBE2.
-
additional information
-
additional information
Q93HU3
Km-value for amylose is 0.7 mg/ml, 30C, pH 7.0
-
additional information
-
additional information
-, Q10625
Km-value for amylose is 0.56 mg/ml, wild-type, 25C, pH 7.0. Km value for mutant lacking N1 domain is 0.33 mg/ml
-
additional information
-
additional information
-
Km-value for amylopectin is 3.0 mg/ml for isoform BEI, 2.7 mg/ml for isoform BEIIa, and 0.9 mg/ml for isoform BEIIb, 30C, pH 7.0
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.068
-
Amylose
-, Q10625
mutant lacking N1 domain, pH 7.0, 25C
0.15
-
Amylose
-, Q10625
wild-type, pH 7.0, 25C
1000
-
Amylose
-
potato amylose
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.001
-
-
be1-1 be2-1, T-DNA insertion double mutant in enzyme BE1 and BE2, in vitro assay of starch-branching enzyme activity; be2-2 (DSA16), 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; be2-1 (EFH20), T-DNA insertion mutant line for BE2, in vitro assay of starch-branching enzyme activity
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
0.107
-
-
wild type enzyme, Col-0; wild type enzyme, Wassilewskija genetic background
0.13
-
-
be1-2 (N637880), T-DNA insertion mutant line for BE1, in vitro assay of starch-branching enzyme activity
4.7
-
-, Q9RTB7
wild-type enzyme, branching assay
7.2
-
-, Q1IZQ3
wild-type enzyme, branching assay
28.5
-
-
mutant enzyme DELTA1-63, micromol Glc incorporated into alpha-D-glucan per min at 30C
42
-
-, Q10625
mutant lacking the N1 domain, i.e. lacking N-terminal residues 1-108, pH 7.0, 25C
63.75
-
-, Q10625
wild-type, pH 7.0, 25C
108
-
Q93HU3
30C, pH 7.0
299
-
-
branching enzyme II
460
-
-
branching enzyme I
535.4
-
-
mutant enzyme DELTA1-83, micromol Glc incorporated into alpha-D-glucan per min at 30C
1000000
-
-
-
additional information
-
-
assay method
additional information
-
-
-
additional information
-
-
-
additional information
-
-
assay method
additional information
-
Q9RQI5
-
additional information
-
Q3BJY5
the branching enzyme has a spesific actvity 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 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 30C.
additional information
-
-, Q1IZQ3
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; 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; 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; 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; 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; 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; 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; 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; 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; 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
-
-, Q9RTB7
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; 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; 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; 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; 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; 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; 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; 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; 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; 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; 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; 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
-
-
20.8 U/mg for amylose, 1 U = decrease of one absorbance unit at 660 nm at 30C; 2.5 U/mg for amylopectin, 1 U = decrease of one absorbance unit at 660 nm at 30C
additional information
-
-
12.258 U/mg for amylose, 1 U = 1% decrease of the absorbance/min; 1.229 U/mg for amylopectin, 1 U = 1% decrease of the absorbance/min
additional information
-
Q4VUI1, -
0.252 U/mg for the crude enzyme, 1 U = decrease of 1.0 units of absorbance per minute; 6.402 U/mg for the purified 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; 39 U/mg for crude extract, 1 unit = incorporation of 1 nmol glucose into the ethanol-insoluble glucan polymer per minute; 483 U/mg after DEAE fast flow, 1 unit = incorporation of 1 nmol glucose into the ethanol-insoluble glucan polymer per minute; 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
-
-
0.29 U/mg for the crude cell extract, 1 U = change in the absorbance of 1 unit; 1.00 U/mg for the purified enzyme , 1 U = change in the absorbance of 1 unit
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
8
-
-
6.8
7.4
-
citrate buffer
7
-
Q3BJY5
the branching enzyme is optimally active at 50C and pH 7
7
-
Q5JDJ7, -
determined by iodine-staining assay
7
-
-, Q10625
all assays are perfomed at 30C with 0.5 microM of protein
7
-
Q4VUI1, -
assay at
7.2
7.6
-
glucose 1-phosphate buffer
7.5
8
-
soluble and insoluble enzyme form
7.5
-
-
-
7.5
-
-
the branching enzyme is most active at 30C and pH 7.5
7.5
-
-
assay at
8
-
-, Q1IZQ3
iodine assay
8
-
-, Q9RTB7
iodine assay
8
-
Q1IZQ3
tandem reaction with potato phosphorylase at pH 7.0
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.5
6
Q8DT52
-
5
9
-
pH 5.0: about 40% of maximal activity, pH 9.0: about 50% of maximal activity
7
9
-, Q1IZQ3
iodine assay
7
9
-, Q9RTB7
iodine assay
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
15
20
-
isozyme BE IIb
25
-
-
isozyme BE IIa
25
-
-
-
30
-
-
-
30
-
-
the branching enzyme is most active at 30C and pH 7.5
30
-
-, Q10625
incubated at different temperatures for 30 min at pH 7 in 50 mM citrate buffer
30
-
-
assay at
30
-
Q4VUI1, -
assay at
33
-
-
isozyme BE I
34
-
-, Q1IZQ3
iodine assay
34
-
-, Q9RTB7
iodine assay
34
-
Q1IZQ3
tandem reaction with potato phosphorylase at 38C
36
-
-
-
37
-
Q8DT52
assay at
50
-
Q3BJY5
the branching enzyme is optimally active at 50C and pH 7
70
-
Q5JDJ7, -
determined by iodine-staining assay
75
-
-
soluble and insoluble enzyme form
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
50
-
about 50% of maximal activity at 20C and at 50C
22
45
-
22C: about 50% of maximal activity, 45C: about 60% of maximal activity
30
40
-, Q1IZQ3
iodine assay
30
40
-, Q9RTB7
iodine assay
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
of transgenic rice, expression of Escherichia coli branching enzyme in caryopses of transgenic Oryza sativa
Manually annotated by BRENDA team
-
expression of starch-branching enzymes IIb
Manually annotated by BRENDA team
-
developing hexaploid. Enzyme form WBE-II is expressed at a constant level through mid and late endosperm development. Enzyme forms WBE-IAD and WBE-IB are preferentially expressed in late endosperm development
Manually annotated by BRENDA team
-
SBE IIb is the major isoform in endosperm
Manually annotated by BRENDA team
-
expression of starch-branching enzymes IIb
Manually annotated by BRENDA team
Q7G0S2, Q9ZTB7
specific expression of starch-branching enzymes IIb; specific expression of starch-branching enzymes IIb
Manually annotated by BRENDA team
Q24M29
starch branching enzyme IIb is expressed at low levels in the endosperm compared to other cereals and encoded at a non-syntenic locus
Manually annotated by BRENDA team
Q9ZTB6, Q9ZTB7
;
Manually annotated by BRENDA team
Sorghum sp.
-
-
Manually annotated by BRENDA team
-
developing
Manually annotated by BRENDA team
Gossypium sp.
-
-
Manually annotated by BRENDA team
-
isoform RBE 4
Manually annotated by BRENDA team
-
SBE A is the predominant isoform in leaf
Manually annotated by BRENDA team
-
starch-branching enzymes IIa is predominantly expressed in leaf
Manually annotated by BRENDA team
-, Q18PQ3
IbSBEI RNA is found
Manually annotated by BRENDA team
-, Q18PQ3
IbSBEI RNA is found
Manually annotated by BRENDA team
-, Q18PQ3
IbSBEI RNA is found
Manually annotated by BRENDA team
-
isoform RBE4
Manually annotated by BRENDA team
-
developing seeds contain several isoforms. The major forms are KBE1 and KBE2
Manually annotated by BRENDA team
-
immature
Manually annotated by BRENDA team
-, Q7XZK6
exclusively in endosperm
Manually annotated by BRENDA team
Q7XZK7
endosperm and embryo, activity exhibits a late onset with a peak of transcription at around 22 days after pollination
Manually annotated by BRENDA team
-
activity and expression level of branching enzyme 1 and branching enzyme 3 are lower at 29C/35C than those at 22C/28C. The decreased activity of starch branching enzyme reduces the branching frequency of the branches of amylopectin, which results in the increased amount of long chains of amylopectin of endosperm in rice grain at high temperature
Manually annotated by BRENDA team
Q9XIS4, Q9XIS5
;
Manually annotated by BRENDA team
Sorghum sp.
-
-
Manually annotated by BRENDA team
-, Q18PQ3
IbSBEI RNA is found
Manually annotated by BRENDA team
-
isoform SBE A mRNA is expressed at very low levels in tubers. Expression of isoform SBE B increases with tuber size and is greatest in the largest tubers
Manually annotated by BRENDA team
additional information
-
organ specificity of isoforms
Manually annotated by BRENDA team
additional information
Q7G0S2, Q9ZTB7
the two genes encoding starch-branching enzymes IIa and IIb are differentially expressed; the two genes encoding starch-branching enzymes IIa and IIb are differentially expressed
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
isoform SBE A is found predominantly in the soluble phase of the tuber extracts, indicating a stromal location within the plastid
Manually annotated by BRENDA team
-
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 sign of aggregation or loss of activity on concentration
-
Manually annotated by BRENDA team
-
SBE2 is present in the soluble fraction, SBE1 is associated with the starch granule fraction
-
Manually annotated by BRENDA team
Q24M29
in the soluble fraction, the amount of SBE IIa protein is two to three fold higher than SBIIb
-
Manually annotated by BRENDA team
-
SBE2 is present in the soluble fraction, SBE1 is associated with the starch granule fraction
Manually annotated by BRENDA team
-
soluble isoforms of starch synthase and starch-branching enzyme also occur within starch granules in developing pea embryos
Manually annotated by BRENDA team
Q24M29
two to three fold more SBE IIb protein amount than SBE IIa
Manually annotated by BRENDA team
additional information
-
more than 95% of the recombinant enzyme is present within the cells as insoluble but catalytically active aggregate. Heat treatment of the aggregate suspension at 70C results in about 30% solubilization of the enzyme activity
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Escherichia coli (strain K12)
Oryza sativa subsp. japonica
Oryza sativa subsp. japonica
Oryza sativa subsp. japonica
Thermococcus kodakaraensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
Thermococcus kodakaraensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
Thermococcus kodakaraensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
40000
-
-
gel filtration
52000
-
-
gel filtration
60000
-
-
gel filtration
70000
90000
-
-
72000
-
Q3BJY5
SDS-PAGE and non-denaturing PAGE
74000
-
Q8DT52
SDS-PAGE
75000
-
-, Q1IZQ3
SDS-PAGE
78550
-
Q5JDJ7, -
calculated molecular mass of the TK1436 protein
80000
-
-
isozyme QE I
80000
-
-
native PAGE
80000
-
-
gel filtration
80000
-
-, Q10625
gel filtration chromatography using Superdex 200 HR10/30 column
80000
-
-, Q9RTB7
SDS-PAGE
82000
-
Q7XZK7
calculation from nucleotide sequence
85000
-
-
isozyme QE II
85000
-
-
sucrose density gradient centrifugation
85000
-
-, Q10625
SDS-PAGE at 4C
86060
-
-, Q10625
theoretical mass of the recombinant branching enzyme with N-terminal S-tag and C-terminal His-tag
87000
-
-
branching enzyme II, sucrose density gradient centrifugation
87000
-
-, Q7XZK6
calculation from nucleotide sequence
90000
-
-
-
90700
-
-
SDS-PAGE and MALDI-TOF-MS analyses
92000
103000
-
sucrose density gradient centrifugation
93000
-
-
sucrose density gradient centrifugation
95000
-
-
branching enzyme I, sucrose density gradient centrifugation
103000
-
-
native PAGE
108000
-
Q4VUI1, -
Western blot
558000
-
Q5JDJ7, -
TK1436deltaH protein, gel filtration on a Superdex 200 HR 10/30 column
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 84000, SDS-PAGE
monomer
-
1 * 103000, SDS-PAGE
monomer
-
1 * 70000-90000, SDS-PAGE
monomer
-
1 * 80000, SDS-PAGE
monomer
-
1 * 71000, SDS-PAGE
monomer
-
1 * 71000, SDS-PAGE; 1 * 77000, SDS-PAGE
monomer
-
1 * 84000, SDS-PAGE
monomer
-
1 * 85000, SDS-PAGE
monomer
-
1 * 77000, enzyme KBE2, SDS-PAGE; 1 * 80000, enzyme KBE1, SDS-PAGE
monomer
-
1 * 100000, isoenzyme SBE1, SDS-PAGE; 1 * 81932, isoenzyme SBE2, calculation from nucleotide sequence; 1 * 82000, isoenzyme SBE2, SDS-PAGE; 1 * 88590, isoenzyme SBE1, calculation from nucleotide sequence
monomer
Q9RQI5
1 * 86313, calculation from nucleotide sequence
monomer
-
1 * 80000, SDS-PAGE
additional information
-
isoform IIb assembles to trimer with starch synthase I and starch synthase IIa. Starch synthase IIa is at the core of the complex, interacting with starch synthase I and starch branching enzyme IIb, which do not interact directly with each other
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
proteolytic modification
-, Q7XZK6
after removal of the transit peptide sequence the sbeI cDNA encodes a 762 amino acid-long mature protein
proteolytic modification
-
RBE4 is initially produced as a precursor protein of 841 amino acids, including a 53 residue transit peptide at the N-terminus
proteolytic modification
Q7XZK7
removal of the transit peptide yields a 746 amino acids-long mature protein
glycoprotein
-
enzyme contains 0.03 mg of carbohydrate in 1 mg of enzyme protein
additional information
-
no glycoprotein
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
hanging drop method, active N-terminally truncated form missing the first 107 amino acids
-
crystal structure of full-length protein at 2.33 A resolution. The enzyme contains four domains: N1 beta-sandwich, N2 beta-sandwich, a central (beta/alpha)8 domain that houses the catalytic site, and a C-terminal beta-sandwich. The N1 beta-sandwich, which is formed by the first 105 amino acids and superimposes well with the N2 beta-sandwich, has an influence in substrate binding in the amylase assay
-, Q10625
determination of the crystal structure of branching enzyme I at a resolution of 1.9 A by molecular replacement using the Escherichia coli glycogen branching enzyme as a search model. Branching enzyme I is roughly ellipsoidal in shape with two globular domains that form a prominent groove proposed to serve as the alphha-polyglucan-binding site. Amino acid residues Asp344 and Glu399, postulated to play an essential role in catalysis, are located at a central cleft in the groove
-
mutant E399Q in complex with maltopentaose at a resolution of 2.2 A. Maltopentaose binds to a hydrophobic pocket formed by the N-terminal helix, carbohydrate-binding module 48, and alpha-amylase domain. In addition, glucose moieties can be observed at molecular surfaces on the N-terminal helix alpha2 and carbohydrate-binding module 48
Q01401
sitting drop method, 20C
-
in the native state and in complex with glucose and substrate mimetics, to 2.4 A, 2.9 A, and 1.9 A resolution, respectively. The structure encompasses a distorted (beta/alpha)7-barrel juxtaposed to a C-terminal alpha-helical domain, which also participates in the formation of the active-site cleft. 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, which is fully conserved among GH13- and GH57-type branching enzymes
Q5JDJ7, -
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
8
Q8DT52
relatively stable during 1 h of incubation
5
-
-
irreversible inactivation below
7
8.5
-
4C, 16 h, less than 10% loss of activity, isoenzyme SBE1
7
9
-
4C, 16 h, less than 10% loss of activity, isoenzyme SBE2
7
9.5
-
4C, 16 h, less than 10% loss of activity, enzyme form KBE1 and KBE2; stable
7.3
8.1
-
4C, 16 h, stable
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
45
-
no apparent inactivation up to 30C, about 10% loss of activity at 35C, about 90% loss of enzyme activity at 50C
10
30
-, Q10625
pre-incubation of the enzyme for 2 h at different temperatures, following enzyme assay is conducted at 30C. About 80% activity is retained after pre-incubation at 37C and 45C
35
-
-
pH 8.0, 30 min, stable below
40
-
-
pH 8.0, 15 min, stable up to, enzyme form KBE1
40
-
Q8DT52
above 40C enzyme inactivated after incubation time of 1 h
45
-
-, Q10625
with a direct enzyme assay at 45C the enzyme retains about 45% activity
50
55
Q3BJY5
in the absence of substrates the branching enzyme is stable at 50C for more than 6 h. At 55C the half-life of the branching enzyme is 50 min.
50
-
-
pH 8.0, 15 min, stable up to, enzyme form KBE2
50
-
-, Q9RTB7
after 1 h incubation at fully active
51
-
-
partial inactivation
60
65
-, Q1IZQ3
after 1 h incubation at 60C fully active, after 1 h incubation at 65C only 80% residual activity
70
-
-
pH 7.0, 30 min, 10% loss of the soluble enzyme form, 50% loss of the insoluble enzyme form
75
-
-
fully active after 100 min incubation, half-life time at 80C 73.7 min, half-life time at 85C 16.7 min
85
-
-
soluble and insoluble enzyme form, stable up to
90
-
Q5JDJ7, -
the protein is stable up to 90C, the activity decreases gradually during the incubation at 100C
additional information
-
-
the activity is lost after incubation at 50C for 30 min
additional information
-
-
when the enzymes are maintained for 15 min at various temperatures ranging from 30C to 60C, more than 80% of the original activity was retained up to 47.5C for PvSBE2, up to 40C for D15A- and D15E-PvSBE2, up to 42.5C for R28A- and H24A-PvSBE2, and up to 45C for R28K-PvSBE2.
additional information
-
Q5JDJ7, -
high thermal tolerance even at boiling temperatures
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
unstable in diluted solutions
-
urea, 2 M irreversible denaturation
-
stable protein even at high concentrations of chaotropic agents
Q5JDJ7, -
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-85C or 4C, stable for several months
-
-20C, 50 mM glycylglycine buffer, pH 8.0, 5 mM mercaptoethanol, 1 mM EDTA, 0.02% NaN3, 25% glycerol
-
0-4C, 50 mM Tris/HCl buffer, pH 7.5, stable for at least 1 month
-
4C, 10 mM Tris/HCl buffer, pH 7.0, 15 mM mercaptoethanol, stable for several months
-
-20C, stable for 3 months
-
-80C, stable in presence of SH-group reducing agents
-
addition of 0.04% (w/v) polyvinyl alcohol 50 K and 1 mM dithiothreitol to the glycine buffer, pH 8.4, leads to long-term stability and
-
higher yields of both starch synthase and starch branching enzyme, due to activation of inactive enzymes
-
the TK1436 protein shows rapid degradation within 2 to 3 days of storage at 4C, while the TK1436deltaH protein is stable unter the same conditions
Q5JDJ7, -
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Phenyl Sepharose 6 Fast Flow column and Superdex 200 gel filtration column
Q3BJY5
His tag affinity chromatography
-, Q1IZQ3
His tag affinity chromatography
-, Q9RTB7
wild-type and truncation mutants
-
-
Gossypium sp.
-
isoform QEIIf
-
Ni2+-NTA affinity column and Q-Sepharose column
-, Q10625
2 isozymes
-
anion exchange chromatography
-
HitrapQ HP anion exchange column
-
isoform RBE 4
-
Q-sepharose chromatography
-
HitrapQ HP anion exchange column
A9ZPD1
chimeric and N-terminal truncated enzymes: DEAE-Sepharose Cl6B column, Bio-Gel P-200 and Gigapite column all at 4C and pH 7.5. Site-directed mutant enzymes: chelating Sepharose FF column and DEAE-Sepharose CL-6B column, all at 4C.
-
chimeric enzymes; chimeric enzymes
Q9XIS4, Q9XIS5
ammonium sulfate, Q-Sepharose column, ultrafiltration, gel filtration with Superdex 200 column, native polyacrylamide gel elektrophoresis
-
large scale purification from white potato tuber
-
partial, 800000 Da enzyme form
-
4 isozymes
-
His-tag affinity column chromatography
Q8DT52
3.45fold after Ni-NTA affinity chromatography
-
anion exchange column and hydrophobic column
Q5JDJ7, -
25.4fold after immobilized metal-ion affinity chromatography
Q4VUI1, -
about 19.0 to 101.9fold after Sephacryl S-200 gel filtration and Q2-sepharose anion exchange chromatography
-
2 isozymes
-
chimeric enzymes expressed in E. coli
-
wild-type and mutant enzymes R384A, R384S, R384Q, E384E and R384K
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
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
Q3BJY5
expression in Bacillus subtilis
-, O66936
expression in Escherichia coli
-
two closely related cDNAs encode starch branching enzyme from Arabidopsis thaliana
-
expressed in Escherichia coli
-
expression in Escherichia coli
Q9RQI5
expression in mosquito C6/36 cells; expression in mosquito C6/36 cells
-, Q4F8A2, Q962G8
expression in Escherichia coli BL21
-, Q1IZQ3
expression in Escherichia coli BL21
-, Q9RTB7
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
Q6EAS5
expression in Escherichia coli, glycogen branching enzyme gene existing in tandem with the glycogen debranching enzyme
-
expression in Escherichia coli, full-length enzyme and a truncated enzyme form missing the first 107 amino acids
-
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 in Bacillus subtilis
-
;
Q9ZTB6, Q9ZTB7
the barley clone encodes the complete mature SBEI but is truncated by approximately 150 bases at the 5'-end
-, Q7XZK6
expressed in Escherichia coli strain KV832
-, Q18PQ3
expressed in Escherichia coli DG5alpha
-, Q10625
expression in Escherichia coli
-, Q10625
-
Q01401
expression in Escherichia coli
-
expression in Escherichia coli AD494
-
overexpression in Escherichia coli BL21
-
transformed to Agrobacterium tumefaciens EHA 105, generation of transgenic Oryza sativa, expression in Escherichia coli AD494
A9ZPD1
expressed in Escherichia coli BL21 (DE3)
-
isoenzymes PySBE1 and PySBE2, expression in Escherichia coli
-
expression in Bacillus subtilis
Q93HU3
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 Escherichia coli BL21
Q8DT52
expression in Escherichia coli BL21
-
expressed in Escherichia coli Bl21-CodonPlus(DE3)-RIL and pET21a(+)
Q5JDJ7, -
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
Q24M29
expression in Escherichia coli BL21
Q4VUI1, -
expression in Escherichia coli
-
expression in Escherichia coli, chimeric enzymes consisting of part mBE I and mBE II
-
expression in Saccharomyces cerevisiae, each of the three isoforms is functional in yeast cells
-
expression of mSBEIIa in Escherichia coli as Strep-tagged enzyme
-
isolation and characterization of a starch-branching enzymes IIa cDNA
-
wild-type and mutant enzymes R384A, R384S, R384Q, E384E and R384K
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
in mutants with suppression of expression SBE IIa; in mutants with suppression of expression SBE IIb or with concominant reduction in SBE IIb
Q9ZTB6, Q9ZTB7
lower expression in amylose-extender mutant of rice
-
lower expression in amylose-extender mutant of rice
A9ZPD1
gene expression oscillates with a period of approximately 24 h
Sorghum sp.
-
induction of gene expression with abscisic acid or sucrose as source
Sorghum sp.
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
DELTA1-112
-
truncated enzyme transferrs a greater amount of longer chains than the wild-type enzyme
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
DELTA1-63
-
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
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
Q01401
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
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
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.
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.
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
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.; 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.; 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.; 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.; 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.; 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.; 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.; 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.; 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
Bacillus subtilis 168
-
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
-, Q4F8A2, Q962G8
enzyme overexpression results in decrease cell proliferation when treated by deltamethrin
additional information
-, Q1IZQ3
CT Dg, truncated at 3' end; GGR, construction of chimeric genes, with C-domain of GBE of Deinococcus radiodurans; GRR, construction of chimeric genes, with A-domain and C-domain of GBE of Deinococcus radiodurans; NT Dg, tuncated at 5' end; RGG, construction of chimeric genes, with N-domain of GBE of Deinococcus radiodurans; RRG, construction of chimeric genes, with N-domain and A-domain of GBE of Deinococcus radiodurans
additional information
-, Q9RTB7
CTT Dr, tuncated at 3' end; GGR, construction of chimeric genes, with N-domain and A-domain of GBE of Deinococcus geothermalis; GRR, construction of chimeric genes, with N-domain of GBE of Deinococcus geothermalis; RGG, construction of chimeric genes, with A-domain and C-domain of GBE of Deinococcus geothermalis; RRG, construction of chimeric genes, with C-domain of GBE of Deinococcus geothermalis
additional information
-
CTT Dr, tuncated at 3' end; GGR, construction of chimeric genes, with N-domain and A-domain of GBE of Deinococcus geothermalis; GRR, construction of chimeric genes, with N-domain of GBE of Deinococcus geothermalis; RGG, construction of chimeric genes, with A-domain and C-domain of GBE of Deinococcus geothermalis; RRG, construction of chimeric genes, with C-domain of GBE of Deinococcus geothermalis
-
Y300W
-
mutant enzyme shows less than 1% of the wild-type activity
additional information
Q9ZTB6, Q9ZTB7
concominant reduction in SBE IIb with suppression of SBE IIa; SBE IIa-/SBE IIb-, transgenic line with suppressed SBE IIb and suppressed SBE IIa; SBE IIa-/SBE IIb-, transgenic line with suppressed SBE IIb and suppressed SBE IIa; SBE IIa-, transgenic line with suppressed SBE IIa; SBE IIb-, transgenic line with suppressed SBE IIb; suppression of SBE IIa with concominant reduction in SBE IIb
additional information
-, Q10625
a mutant lacking the N1 domain, i.e. lacking N-terminal residues 1-108, shows about 30% decrease in specific activity
H467A
-
mutant without enzyme activity
additional information
-
ae mutant, BEIIb-deficient mutant
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.
additional information
Q9XIS4, Q9XIS5
construction of chimeric enzymes of the isoenzymes PvSBE1 and PvSBE2; construction of chimeric enzymes of the isoenzymes PvSBE1 and PvSBE2
additional information
-
chimeric enzymes of PvSBE2: only one chimeric recombinat protein ((I Na/2Nb)-II) has enzyme actvity. It shows 6.1% of the specific activity of the wild type enzyme.; N-termial truncated enzyme of PvSBE2. Delta46-PvSBE2 has no branching enzyme activity.
R28K
-
R28K-PvSBE2 enzyme shows 93.5% of the specific activity of the wild type enzyme.
additional information
Q5JDJ7, -
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)
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
unfolding equilibrium is a two-state process with no intermediates
Q5JDJ7, -
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
food industry
-, O66936
production of food ingredients
food industry
-
analyzation and characterization of reaction products of branching enzymes from different sources for starch processing to synthesize the food ingredient, highly branched cyclic dextrin. The amount of short chains with a degree of polymerization of 6-8 is signifi cantly increased in the product of Bacillus cereus
medicine
Q6EAS5
defining the molecular basis of equine glycogen storage disease IV will allow for accurate DNA testing and the ability to prevent occurence of this disease affecting American Quarter Horses and related breeds. 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
nutrition
-
cooking and textural characteristics of rice depend not only on the ratio of amylose, but also on the degree of amylopectin branching. Short chains of glucose with a degree of polymerization (DP)of 69 inhibit retrogradation. In vivo modification of starches using genetic engineering holds potential for both enhancing nutritional qualities and for obviating post-harvest modifications often necessary for utilization of this complex carbohydrate
food industry
-
analyzation and characterization of reaction products of branching enzymes from different sources for starch processing to synthesize the food ingredient, highly branched cyclic dextrin; starch processiong to synthesize a food ingredient, highly branched cyclic dextrin
food industry
-
production of food ingredients
food industry
-, P30538
involved in the synthesis of highly-branched cyclic dextrin, a dextrin food ingredient
food industry
Geobacillus stearothermophilus TRBE14
-
production of food ingredients
-
food industry
-
analyzation and characterization of reaction products of branching enzymes from different sources for starch processing to synthesize the food ingredient, highly branched cyclic dextrin. The amount of short chains with a degree of polymerization of 6-8 is significantly increased in the product of Phaseolus vulgaris
nutrition
-
production of very-high-amylose potato starch by simultaneous inhibition of SBE A and SBE B to a level of less than 1% using an antisense construct