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Information on EC 2.4.1.25 - 4-alpha-glucanotransferase and Organism(s) Aquifex aeolicus and UniProt Accession O66937
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2.4.1.25 4-alpha-glucanotransferaseIUBMB 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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Word Map
- 2.4.1.25
- starch
- maltose
- maltodextrins
- amylose
-
transglycosylation
- glucans
- amylopectin
- cycloamylose
-
disproportionation
- malto-oligosaccharides
- maltotetraose
- maltohexaose
- alpha-glucans
- maltopentaose
- synthesis
- alpha-amylases
- amylo-1,6-glucosidase
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maltogenic
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malpq
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large-ring
- alpha-1,4-glucans
- biotechnology
- nutrition
- medicine
- analysis
- food industry
The taxonomic range for the selected organisms is: Aquifex aeolicus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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, alpha-1,4-glucanotransferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
amylomaltase
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-
-
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D-enzyme
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-
-
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debranching enzyme maltodextrin glycosyltransferase
-
-
-
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dextrin glycosyltransferase
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-
-
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dextrin glycosyltransferase,
-
-
-
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dextrin transglycosylase
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-
-
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disproportionating enzyme
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
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
9032-09-1
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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
cycloamylose
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the enzyme produces a cycloamylose with a minimum degree of polymerization of 16
-
-
?
additional information
?
-
-
the smallest acceptor is glucose, the smallest donor is maltose
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-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60 - 100
-
60°C: about 50% of maximal activity, 100°C: about 30% of maximal activity
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Terada, Y.; Fujii, K.; Takaha, T.; Okada, S.
Thermus aquaticus ATCC 33923 amylomaltase gene cloning and expression and enzyme characterization: production of cycloamylose
Appl. Environ. Microbiol.
65
910-915
1999
Aquifex aeolicus, Borreliella burgdorferi, Chlamydia psittaci, Clostridium butyricum, Clostridium butyricum NCIMB 7423, Escherichia coli, Haemophilus influenzae, Hordeum vulgare, Mycobacterium tuberculosis, Solanum tuberosum, Streptococcus pneumoniae, Synechocystis sp., Thermococcus litoralis, Thermus aquaticus, Thermus aquaticus (B7A9X4)
Przylas, I.; Tomoo, K.; Terada, Y.; Takaha, T.; Fujii, K.; Saenger, W.; Strater, N.
Crystal structure of amylomaltase from Thermus aquaticus, a glycosyltransferase catalyzing the production of large cyclic glucans
J. Mol. Biol.
296
873-886
2000
Aquifex aeolicus, Chlamydia pneumoniae, Clostridium butyricum, Escherichia coli, Haemophilus influenzae, Solanum tuberosum, Thermus aquaticus
Roujeinikova, A.; Raasch, C.; Sedelnikova, S.; Liebl, W.; Rice, D.W.
Crystal structure of Thermotoga maritima 4-alpha-glucanotransferase and its acarbose complex: Implications for substrate specificity and catalysis
J. Mol. Biol.
321
149-162
2002
Aquifex aeolicus, Clostridium butyricum, Dictyoglomus thermophilum, Escherichia coli, Haemophilus influenzae, Thermococcus litoralis, Thermotoga maritima, Thermotoga neapolitana, Thermus aquaticus
Kaper, T.; van der Maarel, M.J.; Euverink, G.J.; Dijkhuizen, L.
Exploring and exploiting starch-modifying amylomaltases from thermophiles
Biochem. Soc. Trans.
32
279-282
2004
Escherichia coli, Thermococcus litoralis, Thermococcus litoralis (O32462), Thermus aquaticus, Thermus aquaticus (B7A9X4), Aquifex aeolicus (O66937), Solanum tuberosum (Q06801), Thermotoga maritima (Q60035), Chlamydomonas reinhardtii (Q9FDV9), Arabidopsis thaliana (Q9LV91), Escherichia coli ML
Bhuiyan, S.H.; Kitaoka, M.; Hayashi, K.
A cycloamylose-forming hyperthermostable 4-alpha-glucanotransferase of Aquifex aeolicus expressed in Escherichia coli
J. Mol. Catal. B
22
45-53
2003
Aquifex aeolicus
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