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Information on EC 2.4.1.18 - 1,4-alpha-glucan branching enzyme and Organism(s) Deinococcus radiodurans and UniProt Accession Q9RTB7

for references in articles please use BRENDA:EC2.4.1.18
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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:
Deinococcus radiodurans
UNIPROT: Q9RTB7
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Word Map
The taxonomic range for the selected organisms is: Deinococcus radiodurans
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
1,4-alpha-glucan branching enzyme
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glycogen branching enzyme
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alpha-1,4-glucan:alpha-1,4-glucan 6-glycosyltransferase
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-
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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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-
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amylo-(1,4-1,6)-transglycosylase
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-
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amylose isomerase
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-
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BE
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-
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branching factor, enzymatic
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-
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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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-
-
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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
amylopectin
?
show the reaction diagram
iodine assay
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-
?
amylose
?
show the reaction diagram
branching assay, at pH 8.0, reaction stopped by boiling for 5 min
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-
?
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.7
wild-type enzyme, branching assay
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 40
iodine assay
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
after 1 h incubation at fully active
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
His tag affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli BL21
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Palomo, M.; Kralj, S.; van der Maarel, M.J.; Dijkhuizen, L.
The unique branching patterns of Deinococcus glycogen branching enzymes are determined by their N-terminal domains
Appl. Environ. Microbiol.
75
1355-1362
2009
Deinococcus geothermalis (Q1IZQ3), Deinococcus geothermalis, Deinococcus radiodurans (Q9RTB7), Deinococcus radiodurans, Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539 (Q9RTB7)
Manually annotated by BRENDA team