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Information on EC 2.4.1.18 - 1,4-alpha-glucan branching enzyme and Organism(s) Rhodothermus marinus and UniProt Accession Q93HU3
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2.4.1.18 1,4-alpha-glucan branching enzymeIUBMB Comments
Converts amylose into amylopectin. The accepted name requires a qualification depending on the product, glycogen or amylopectin, e.g. glycogen branching enzyme, amylopectin branching enzyme. The latter has frequently been termed Q-enzyme.
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Word Map
- 2.4.1.18
- biloba
- ginkgo
- amylopectin
- endosperm
- maize
- grain
-
pyrophosphorylase
- phosphorylase
-
granule-bound
- glucans
- potato
-
debranching
- polysaccharide
-
polyglucosan
-
herbal
- ssiia
-
ginkgolide
- kernel
- gelatin
-
waxy
- glycogenosis
- amyloplasts
- pullulanase
- andersen
- dextrin
- isoamylase
- bilobalide
- agpase
-
high-amylose
-
amylolytic
-
chain-length
-
lafora
-
rhodothermus
- biotechnology
- medicine
- adpglucose
- glycogenin
- food industry
- nutrition
-
diastase-resistant
- alpha-glucans
- drug development
-
pas-positive
- isorhamnetin
The taxonomic range for the selected organisms is: Rhodothermus marinus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
gbe, branching enzyme, sbeiib, glycogen branching enzyme, starch branching enzyme, sbeiia, beiib, sbeii, starch-branching enzyme, beiia, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha-1,4-glucan:alpha-1,4-glucan 6-glycosyltransferase
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alpha-1,4-glucan:alpha-1,4-glucan-6-glycosyltransferase
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alpha-glucan-branching glycosyltransferase
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amylo-(1,4-1,6)-transglycosylase
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-
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amylose isomerase
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BE
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branching factor, enzymatic
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branching glycosyltransferase
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enzyme Q
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GBE
glucosan transglycosylase
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glycogen branching enzyme
glycosyltransferase, alpha-glucan-branching
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Q-enzyme
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QE
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SBE
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starch branching enzyme
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GBE
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glycogen branching enzyme
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycosyl group transfer
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-
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PATHWAY SOURCE
PATHWAYS
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-, -, -, -
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
9001-97-2
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
amylose
amylose containing alpha-1,6-glucosidic linkages
potato type III amylose
-
-
?
potato amylopectin type III
potato amylopectin type III containing alpha-1,6-glucosidic linkages
potato amylose
potato amylose containing alpha-1,6-glucosidic linkages
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65.4% activity compared to potato amylopectin type III
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-
?
soluble starch
soluble starch containing alpha-1,6-glucosidic linkages
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47.3% activity compared to potato amylopectin type III
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-
?
tapioca starch
tapioca starch containing alpha-1,6-glucosidic linkages
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46.5% activity compared to potato amylopectin type III
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-
?
waxy corn starch
waxy corn starch containing alpha-1,6-glucosidic linkages
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74.7% activity compared to potato amylopectin type III
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-
?
potato amylopectin type III
potato amylopectin type III containing alpha-1,6-glucosidic linkages
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-
-
-
?
potato amylopectin type III
potato amylopectin type III containing alpha-1,6-glucosidic linkages
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100% activity
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-
?
additional information
?
-
a minimal chain length of ten glucosyl units is required for the donor substrate to be recognized by Rhodothermus marinus branching enzyme that essentially produces branches with a degree of polymerization of 3-8. The enzyme preferentially creates new branches by intermolecular mechanism. Branched glucans define better substrates for the enzyme leading to the formation of hyper-branched particles of 30-70 nm in diameter, dextrins. The enzyme catalyzes an additional alpha-4-glucanotransferase activity
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-
?
additional information
?
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a minimal chain length of ten glucosyl units is required for the donor substrate to be recognized by Rhodothermus marinus branching enzyme that essentially produces branches with a degree of polymerization of 3-8. The enzyme preferentially creates new branches by intermolecular mechanism. Branched glucans define better substrates for the enzyme leading to the formation of hyper-branched particles of 30-70 nm in diameter, dextrins. The enzyme catalyzes an additional alpha-4-glucanotransferase activity
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-
?
additional information
?
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the enzyme catalyzes starch branching by the cleavage of alpha(1->4) linkage and transfer in alpha(1->6) of the fragment in non-reducing position, but the enzyme also shows an additional alpha-4-glucanotransferase activity not described so far for a member of the GH13 family. The enzyme is able to transfer alpha(1->4)-linked-glucan in C4 position (instead of C6 position for the branching activity) of a glucan to create new alpha(1->4) linkages yielding to the elongation of linear chains subsequently used for further branching, overview
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-
?
additional information
?
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-
the enzyme catalyzes starch branching by the cleavage of alpha(1->4) linkage and transfer in alpha(1->6) of the fragment in non-reducing position, but the enzyme also shows an additional alpha-4-glucanotransferase activity not described so far for a member of the GH13 family. The enzyme is able to transfer alpha(1->4)-linked-glucan in C4 position (instead of C6 position for the branching activity) of a glucan to create new alpha(1->4) linkages yielding to the elongation of linear chains subsequently used for further branching, overview
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-
?
additional information
?
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increased branching of the starch from maize and potato following BE treatment, short chains increase whereas the number of long chains decrease after BE treatment, molecular size distribution of branching enzyme-treated and control starch, granular structure, NMR analysis, overview
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
potato amylopectin type III
potato amylopectin type III containing alpha-1,6-glucosidic linkages
-
-
-
-
?
additional information
?
-
the enzyme catalyzes starch branching by the cleavage of alpha(1->4) linkage and transfer in alpha(1->6) of the fragment in non-reducing position, but the enzyme also shows an additional alpha-4-glucanotransferase activity not described so far for a member of the GH13 family. The enzyme is able to transfer alpha(1->4)-linked-glucan in C4 position (instead of C6 position for the branching activity) of a glucan to create new alpha(1->4) linkages yielding to the elongation of linear chains subsequently used for further branching, overview
-
-
?
additional information
?
-
-
the enzyme catalyzes starch branching by the cleavage of alpha(1->4) linkage and transfer in alpha(1->6) of the fragment in non-reducing position, but the enzyme also shows an additional alpha-4-glucanotransferase activity not described so far for a member of the GH13 family. The enzyme is able to transfer alpha(1->4)-linked-glucan in C4 position (instead of C6 position for the branching activity) of a glucan to create new alpha(1->4) linkages yielding to the elongation of linear chains subsequently used for further branching, overview
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
additional information
-
addition of Li+, Na+ or K+ has almost no effect on enzyme activity
Ca2+
-
Ca2+ does not promote the activity of purified enzyme, but may be required for its activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
EDTA
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the enzyme retains 73.39%, 39.01%, 19.06%, 7.64%, and 3.30% of its activity in the presence of 1, 2, 4, 8, and 10 mM EDTA, respectively
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Km-value for amylose is 0.7 mg/ml, 30°C, pH 7.0
-
additional information
additional information
-
Km-value for amylose is 0.7 mg/ml, 30°C, pH 7.0
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additional information
additional information
enzyme reaction kinetics with different branched or unbranched alpha-glucans of controlled structure
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additional information
additional information
-
enzyme reaction kinetics with different branched or unbranched alpha-glucans of controlled structure
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 7.5
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the enzyme shows at least 80% of maximal activity from pH 5.5 to pH 7.5. The enzyme activity decreases rapidly at pH values lower than 5.5 and higher than 9.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50 - 80
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the enzyme has more than 60% activity between 50 and 80°C, 93.85% of maximal activity at 60°C, and 95.61% of maximal activity at 70°C
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
enzyme produced by pure culture manufacture of a genetically modified strain of Bacillus subtilis containing a synthetic gene coding for glycogen BE from Rhodothermus obamensis
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the enzyme belongs to the glycoside hydrolase family GH13
metabolism
glycogen and starch branching enzymes catalyze the formation of alpha(1->6) linkages in storage polysaccharides by rearrangement of preexisting alpha-glucans. This reaction occurs through the cleavage of alpha(1->4) linkage and transfer in alpha(1->6) of the fragment in non-reducing position. These enzymes define major elements that control the structure of both glycogen and starch
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDB
SCOP
CATH
UNIPROT
ORGANISM
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 11
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the enzyme has broad pH stability between pH 3.0 and 11.0 at 4°C, and prefers weakly acidic conditions at high temperatures (85°C). More than 96% of the initial enzyme activity is retained after incubation at pH 3.0-11.0 for 1 h. The enzyme loses all activity when incubated for 15 min at pH 3.0 or 4.0, and its half-life is 14.9 min at pH 5.0. The enzyme retains 72.1% of its initial activity after 1 h at pH 6.0 in sodium citrate buffer
758278
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70 - 90
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the enzyme remains stable at temperatures up to 80°C and has a half-life at 85°C of approximately 31 min. The enzyme is quite stable (for at least 2 h) at 70°C or lower, and 92% of the initial enzyme activity is retained at 80°C for 2 h. Furthermore, the enzyme demonstrates half-lives at 85 and 90°C of 31 min and 2.5 min, respectively
75
-
fully active after 100 min incubation, half-life time at 80°C 73.7 min, half-life time at 85°C 16.7 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme shows higher activity in sodium citrate buffer than sodium phosphate buffer at pH 6.0 and higher activity in sodium phosphate buffer than glycine buffer at pH 8.0
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate, Q-Sepharose column, ultrafiltration, gel filtration with Superdex 200 column, native polyacrylamide gel elektrophoresis
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yoon, S.A.; Ryu, S.I.; Lee, S.B.; Moon, T.W.
Purification and characterization of branching specificity of a novel extracellular amylolytic enzyme from marine hyperthermophilic Rhodothermus marinus
J. Microbiol. Biotechnol.
18
457-464
2008
Rhodothermus marinus
Roussel, X.; Lancelon-Pin, C.; Vikso-Nielsen, A.; Rolland-Sabate, A.; Grimaud, F.; Potocki-Veronese, G.; Buleon, A.; Putaux, J.L.; DHulst, C.
Characterization of substrate and product specificity of the purified recombinant glycogen branching enzyme of Rhodothermus obamensis
Biochim. Biophys. Acta
1830
2167-2177
2012
Rhodothermus marinus (Q93HU3), Rhodothermus marinus
Jensen, S.; Larsen, F.; Bandsholm, O.; Blennow, A.
Stabilization of semi-solid-state starch by branching enzyme-assisted chain-transfer catalysis at extreme substrate concentration
Biochem. Eng. J.
72
1-10
2013
Rhodothermus marinus
-
Xin, C.; Ban, X.; Gu, Z.; Li, C.; Cheng, L.; Hong, Y.; Li, Z.
Non-classical secretion of 1,4-alpha-glucan branching enzymes without signal peptides in Escherichia coli
Int. J. Biol. Macromol.
132
759-765
2019
Parageobacillus thermoglucosidasius, Rhodothermus marinus, Parageobacillus thermoglucosidasius STB02, Rhodothermus marinus STB05
Wang, Z.; Xin, C.; Li, C.; Gu, Z.; Cheng, L.; Hong, Y.; Ban, X.; Li, Z.
Expression and characterization of an extremely thermophilic 1,4-alpha-glucan branching enzyme from Rhodothermus obamensis STB05
Protein Expr. Purif.
164
105478
2019
Rhodothermus marinus, Rhodothermus marinus STB05
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