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Information on EC 2.4.1.18 - 1,4-alpha-glucan branching enzyme and Organism(s) Aquifex aeolicus and UniProt Accession O66936

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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:
Aquifex aeolicus
UNIPROT: O66936
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Word Map
The taxonomic range for the selected organisms is: Aquifex aeolicus
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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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
amylopectin
amylopectin with additional alpha-1,6-glucosidic linkages
show the reaction diagram
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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
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?
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 8
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soluble and insoluble enzyme form
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
75
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soluble and insoluble enzyme form
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
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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 70°C results in about 30% solubilization of the enzyme activity
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
key biocatalyst in synthesis of polysaccharides
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
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pH 7.0, 30 min, 10% loss of the soluble enzyme form, 50% loss of the insoluble enzyme form
85
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soluble and insoluble enzyme form, stable up to
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Bacillus subtilis
expression in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
food industry
production of food ingredients
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Takata, H.; Ohdan, K.; Takaha, T.; Kuriki, T.; Okada, S.
Properties of branching enzyme from hyperthermophilic bacterium, Aquifex aeolicus, and its potential for production of highly-branched cyclic dextrin
J. Appl. Glycosci.
50
15-20
2003
Aquifex aeolicus
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Manually annotated by BRENDA team
Choi, S.S.; Danielewska-Nikiel, B.; Kojima, I.; Takata, H.
Safety evaluation of 1,4-alpha-glucan branching enzymes from Bacillus stearothermophilus and Aquifex aeolicus expressed in Bacillus subtilis
Food Chem. Toxicol.
47
2044-2051
2009
Geobacillus stearothermophilus, Aquifex aeolicus (O66936), Aquifex aeolicus, Geobacillus stearothermophilus TRBE14
Manually annotated by BRENDA team