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Information on EC 2.4.1.25 - 4-alpha-glucanotransferase and Organism(s) Thermus brockianus and UniProt Accession Q2VJA0

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EC Tree
     2 Transferases
         2.4 Glycosyltransferases
             2.4.1 Hexosyltransferases
                2.4.1.25 4-alpha-glucanotransferase
IUBMB Comments
This entry covers the former separate entry for EC 2.4.1.3 (amylomaltase). The plant enzyme has been termed D-enzyme. An enzymic activity of this nature forms part of the mammalian and yeast glycogen debranching system (see EC 3.2.1.33 amylo-alpha-1,6-glucosidase).
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This record set is specific for:
Thermus brockianus
UNIPROT: Q2VJA0
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Word Map
The taxonomic range for the selected organisms is: Thermus brockianus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
amylomaltase, d-enzyme, 4-alpha-glucanotransferase, disproportionating enzyme, amase, maltosyltransferase, alphagt, mq-01, alphagtase, pyamase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amylomaltase
-
-
-
-
D-enzyme
-
-
-
-
debranching enzyme maltodextrin glycosyltransferase
-
-
-
-
dextrin glycosyltransferase
-
-
-
-
dextrin glycosyltransferase,
-
-
-
-
dextrin transglycosylase
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-
-
-
disproportionating enzyme
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
(1->4)-alpha-D-glucan:(1->4)-alpha-D-glucan 4-alpha-D-glycosyltransferase
This entry covers the former separate entry for EC 2.4.1.3 (amylomaltase). The plant enzyme has been termed D-enzyme. An enzymic activity of this nature forms part of the mammalian and yeast glycogen debranching system (see EC 3.2.1.33 amylo-alpha-1,6-glucosidase).
CAS REGISTRY NUMBER
COMMENTARY hide
9032-09-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
maltotriose
maltooligosaccharides
show the reaction diagram
-
-
-
?
additional information
?
-
-
the enzyme reacts with small oligosaccharides, especially maltotriose, to form various maltooligosaccharides by using its disproportionating activity
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-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2 - 165
maltotriose
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0017 - 0.08
maltotriose
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00035 - 0.007
maltotriose
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q2VJA0_THEBO
500
0
57287
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
57220
-
calculated from sequence
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to 2.3 A resolution. Structure shows a pattern of conformational flexibility in the 250s loop with higher B-factor. The conformational flexibility of the loop may be involved in substrate binding in the GH77 family
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F251G
mutation results in significantly lower glucose production but increased maltose production from maltopentose substrates, showing an altered substrate-binding affinity
Q256G
mutation results in increased Km for maltotriose and a sharp decrease of the transglycosylation factor for maltose
W258G
mutant shows neither cyclization nor coupling activity, suggesting that residue Trp258 plays an essential role in all catalytic activities including hydrolysis and transglycosylation activities
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpressed in Escherichia coli BL21
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bang, B.; Kim, H.; Kim, H.; Baik, M.; Ahn, S.; Kim, C.H.; Park, C.
Cloning and overexpression of 4-alpha-glucanotransferase from Thermus brockianus (TBGT) in E. coli
J. Microbiol. Biotechnol.
16
1809-1813
2006
Thermus brockianus
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Manually annotated by BRENDA team
Jung, J.; Jung, T.; Seo, D.; Yoon, S.; Choi, H.; Park, B.; Park, C.; Woo, E.
Structural and functional analysis of substrate recognition by the 250s loop in amylomaltase from Thermus brockianus
Proteins
79
633-644
2011
Thermus brockianus (Q2VJA0), Thermus brockianus
Manually annotated by BRENDA team