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Information on EC 2.4.1.18 - 1,4-alpha-glucan branching enzyme and Organism(s) Thermococcus kodakarensis and UniProt Accession Q5JDJ7

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EC Tree
     2 Transferases
         2.4 Glycosyltransferases
             2.4.1 Hexosyltransferases
                2.4.1.18 1,4-alpha-glucan branching enzyme
IUBMB 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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This record set is specific for:
Thermococcus kodakarensis
UNIPROT: Q5JDJ7
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The taxonomic range for the selected organisms is: Thermococcus kodakarensis
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TK1436
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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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
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glucosan transglycosylase
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glycogen branching enzyme
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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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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycosyl group transfer
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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 hide
9001-97-2
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
additional information
?
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loop 220-245, named as catalytic loop, acts as a lid retaining the intermediate reaction product for subsequent transfer to a new a-1,6 position. The active site comprises two acidic catalytic residues, Glu183 and Asp354, the polarizer His10, aromatic gate-keepers Trp28, Trp270, Trp407, and Trp416 and the residue Tyr233
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
determined by iodine-staining assay
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
determined by iodine-staining assay
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
558000
TK1436deltaH protein, gel filtration on a Superdex 200 HR 10/30 column
78550
calculated molecular mass of the TK1436 protein
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
recombinant TK1436 protein (amino acids [aa] 1 to 675) and a deletion derivative devoid of the C-terminal two-copy helix-hairpin-helix (HhH)2 motif (TK1436deltaH, aa 1 to 562)
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
90
the protein is stable up to 90°C, the activity decreases gradually during the incubation at 100°C
additional information
high thermal tolerance even at boiling temperatures
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stable protein even at high concentrations of chaotropic agents
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
the TK1436 protein shows rapid degradation within 2 to 3 days of storage at 4°C, while the TK1436deltaH protein is stable unter the same conditions
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
anion exchange column and hydrophobic column
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli Bl21-CodonPlus(DE3)-RIL and pET21a(+)
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
unfolding equilibrium is a two-state process with no intermediates
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Murakami, T.; Kanai, T.; Takata, H.; Kuriki, T.; Imanaka, T.
A novel branching enzyme of the GH-57 family in the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1
J. Bacteriol.
188
5915-5924
2006
Thermococcus kodakarensis (Q5JDJ7)
Manually annotated by BRENDA team
Santos, C.; Tonoli, C.; Trindade, D.; Betzel, C.; Takata, H.; Kuriki, T.; Kanai, T.; Imanaka, T.; Arni, R.; Murakami, M.
Structural basis for branching-enzyme activity of glycoside hydrolase family 57: Structure and stability studies of a novel branching enzyme from the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1
Proteins
79
547-557
2011
Thermococcus kodakarensis (Q5JDJ7)
Manually annotated by BRENDA team