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 hide
2.4.1.18
-
RECOMMENDED NAME
GeneOntology No.
1,4-alpha-glucan branching enzyme
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
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
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cyclization
glycosyl group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
-
glycogen biosynthesis
-
-
glycogen biosynthesis I (from ADP-D-Glucose)
-
-
glycogen biosynthesis II (from UDP-D-Glucose)
-
-
glycogen metabolism
-
-
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.
CAS REGISTRY NUMBER
COMMENTARY hide
9001-97-2
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
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 168
-
-
Manually annotated by BRENDA team
strain 168
-
-
Manually annotated by BRENDA team
strain R1
UniProt
Manually annotated by BRENDA team
strain R1
UniProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
Norwegian Forest Cat
-
-
Manually annotated by BRENDA team
strain TRBE14
-
-
Manually annotated by BRENDA team
Gossypium sp.
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Sorghum sp.
-
-
-
Manually annotated by BRENDA team
A3(2)
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
amylopectin
?
show the reaction diagram
amylopectin
amylopectin containing alpha-1,6-glucosidic linkages
show the reaction diagram
-
-
-
-
?
amylopectin
amylopectin with additional alpha-1,6-glucosidic linkages
show the reaction diagram
amylopectin
highly branched cyclic dextrin
show the reaction diagram
amylose
?
show the reaction diagram
amylose
amylose containing alpha-1,6-glucosidic linkages
show the reaction diagram
amylose
branched polyglucan
show the reaction diagram
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
-
-
?
maltopentaose
?
show the reaction diagram
-
dinitrosalicylate method, assay at pH 6.0, 70C
-
-
?
pea starch
?
show the reaction diagram
-
-
-
-
?
Pullulan
?
show the reaction diagram
-
dinitrosalicylate method, assay at pH 6.0, 70C
-
-
?
starch
?
show the reaction diagram
assay at pH 5.0, 37C
-
-
?
starch
starch containing alpha-1,6-glucosidic linkages
show the reaction diagram
waxy maize starch
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ba2+
-
about 2.5% decreased enzyme activity, 5 mM
Co2+
-
upregulates GBE1 gene transcription
Fe2+
-
about 58.3% decreased enzyme activity, 5 mM
Mn2+
-
about 53.5% decreased enzyme activity, 5 mM
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ca2+
the additon of 2.5 mM of Ca2+ slightly inhibits the enzyme
citrate
-
-
Co2+
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%
ethanol
-
about 57.2% decreased enzyme activity, 10%
Fe3+
enzymatic activity is abolished in the presence of Fe3+
maltoheptaose
-
40% inhibition at 15 mM
maltohexaose
-
-
maltononaose
-
-
maltooctaose
-
-
methanol
-
about 45.2% decreased enzyme activity, 10%
Mg2+
the additon of 2.5 mM of Mg2+ slightly inhibits the enzyme
Mn2+
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+
enzymatic activity is abolished in the presence of Zn2+
ZnCl2
-
1 mM, complete inactivation
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(NH4)2SO4
-
10 mM, activates
3-hydroxy-2-oxopropyl dihydrogen phosphate
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10 mM, activates
3-phosphoglycerate
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10 mM, activates
acetate
-
activation
ADP
-
10 mM, activates
ADPglucose
-
10 mM, activates
AMP
-
10 mM, activates
ATP
-
10 mM, activates
Borate
-
activation
citrate
Cl-
-
activation
diphosphate
-
10 mM, activates
dithiothreitol
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
glucose 6-phosphate
-
10 mM, activates
NaCl
-
concentration of 0.5 - 1 M NaCl
NADP+
-
10 mM, activates
phosphate
phosphoenolpyruvate
-
10 mM, activates
potassium alpha-D-glucose 1-phosphate
ribose 5-phosphate
-
10 mM, activates
RuBP
-
10 mM, activates
-
SO42-
-
activation
additional information
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peak of activities at the 28th day post anthesis, higher activity in the cultivar with a high starch content
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0056
amylopectin
-
pH 6.4, 30C, type IV amylopectin
0.00018 - 11
amylose
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.068 - 1000
amylose
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
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
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be1-1 be3-2, T-DNA insertion double mutant in enzyme BE1 and BE3, in vitro assay of starch-branching enzyme activity
0.082
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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
wild-type enzyme, branching assay
7.2
wild-type enzyme, branching assay
28.5
-
mutant enzyme DELTA1-63, micromol Glc incorporated into alpha-D-glucan per min at 30C
42
mutant lacking the N1 domain, i.e. lacking N-terminal residues 1-108, pH 7.0, 25C
63.75
wild-type, pH 7.0, 25C
299
-
branching enzyme II
460
-
branching enzyme I
535.4
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mutant enzyme DELTA1-83, micromol Glc incorporated into alpha-D-glucan per min at 30C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8
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-
6.6 - 7.2
-
-
6.8 - 7.4
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citrate buffer
7.2 - 7.6
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glucose 1-phosphate buffer
7.5 - 8
-
soluble and insoluble enzyme form
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9
-
pH 5.0: about 40% of maximal activity, pH 9.0: about 50% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15 - 20
-
isozyme BE IIb
33
-
isozyme BE I
70
determined by iodine-staining assay
75
-
soluble and insoluble enzyme form
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 50
-
about 50% of maximal activity at 20C and at 50C
22 - 45
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22C: about 50% of maximal activity, 45C: about 60% of maximal activity
30 - 40
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
of transgenic rice, expression of Escherichia coli branching enzyme in caryopses of transgenic Oryza sativa
Manually annotated by BRENDA team
-
developing
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
IbSBEI RNA is found
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
IbSBEI RNA is found
Manually annotated by BRENDA team
IbSBEI RNA is found
Manually annotated by BRENDA team
-
7 isoforms
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
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
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
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli O139:H28 (strain E24377A / ETEC)
Escherichia coli O139:H28 (strain E24377A / ETEC)
Escherichia coli O139:H28 (strain E24377A / ETEC)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Oryza sativa subsp. japonica
Oryza sativa subsp. japonica
Oryza sativa subsp. japonica
Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
Thermococcus kodakarensis (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
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
-
gel filtration
52000
-
gel filtration
60000
-
gel filtration
70000 - 90000
-
-
72000
SDS-PAGE and non-denaturing PAGE
78550
calculated molecular mass of the TK1436 protein
82000
calculation from nucleotide sequence
86060
theoretical mass of the recombinant branching enzyme with N-terminal S-tag and C-terminal His-tag
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
Western blot
558000
TK1436deltaH protein, gel filtration on a Superdex 200 HR 10/30 column
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 84000, SDS-PAGE
monomer
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
COMMENTARY hide
LITERATURE
glycoprotein
-
enzyme contains 0.03 mg of carbohydrate in 1 mg of enzyme protein
proteolytic modification
additional information
-
no glycoprotein
Crystallization/COMMENTARY
ORGANISM
UNIPROT
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
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
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 8
relatively stable during 1 h of incubation
703793
5
-
irreversible inactivation below
636920
7 - 8.5
-
4C, 16 h, less than 10% loss of activity, isoenzyme SBE1
636954
7 - 9
-
4C, 16 h, less than 10% loss of activity, isoenzyme SBE2
636954
7 - 9.5
-
4C, 16 h, less than 10% loss of activity, enzyme form KBE1 and KBE2; stable
636945
7.3 - 8.1
-
4C, 16 h, stable
636932
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
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
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
45
with a direct enzyme assay at 45C the enzyme retains about 45% activity
50 - 55
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.
51
-
partial inactivation
60 - 65
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
the protein is stable up to 90C, the activity decreases gradually during the incubation at 100C
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stable protein even at high concentrations of chaotropic agents
unstable in diluted solutions
-
urea, 2 M irreversible denaturation
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 50 mM glycylglycine buffer, pH 8.0, 5 mM mercaptoethanol, 1 mM EDTA, 0.02% NaN3, 25% glycerol
-
-20C, stable for 3 months
-
-80C, stable in presence of SH-group reducing agents
-
-85C or 4C, stable for several months
-
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
-
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
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 isozymes
25.4fold after immobilized metal-ion affinity chromatography
3.45fold after Ni-NTA affinity chromatography
-
4 isozymes
-
about 19.0 to 101.9fold after Sephacryl S-200 gel filtration and Q2-sepharose anion exchange chromatography
-
ammonium sulfate, Q-Sepharose column, ultrafiltration, gel filtration with Superdex 200 column, native polyacrylamide gel elektrophoresis
-
anion exchange chromatography
-
anion exchange column and hydrophobic column
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 expressed in E. coli
-
chimeric enzymes; chimeric enzymes
His tag affinity chromatography
His-tag affinity column chromatography
HitrapQ HP anion exchange column
isoform QEIIf
-
isoform RBE 4
-
large scale purification from white potato tuber
-
Ni2+-NTA affinity column and Q-Sepharose column
partial, 800000 Da enzyme form
-
Phenyl Sepharose 6 Fast Flow column and Superdex 200 gel filtration column
Q-sepharose chromatography
-
wild-type and mutant enzymes R384A, R384S, R384Q, E384E and R384K
-
wild-type and truncation mutants
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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-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 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
-
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
-
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
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
gene expression oscillates with a period of approximately 24 h
Sorghum sp.
-
in mutants with suppression of expression SBE IIa; in mutants with suppression of expression SBE IIb or with concominant reduction in SBE IIb
induction of gene expression with abscisic acid or sucrose as source
Sorghum sp.
-
lower expression in amylose-extender mutant of rice
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DELTA1-112
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
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
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D15E-PvSBE2 enzyme shows 31.3% of the specific activity of the wild type enzyme. The large decrease in the specific activities of the mutant is predominatly attributed to the reduced Vmax value.
H24A
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H24A-PvSBE2 enzyme shows 38.3% of the specific activity of the wild type enzyme. The large decrease in the specific activities of the mutant is predominatly attributed to the reduced Vmax value.
R28A
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R28A-PvSBE2 enzyme shows 10.7% of the specific activity of the wild type enzyme. The large decrease in the specific activities of the mutant is predominatly attributed to the reduced Vmax value.
R28K
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R28K-PvSBE2 enzyme shows 93.5% of the specific activity of the wild type enzyme.
R384A
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mutation causes almost complete inactivation
R384E
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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
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
unfolding equilibrium is a two-state process with no intermediates
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
food industry
medicine
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
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