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Information on EC 2.4.1.25 - 4-alpha-glucanotransferase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9LV91
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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
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transglycosylation
- glucans
- amylopectin
- cycloamylose
-
disproportionation
- malto-oligosaccharides
- maltotetraose
- maltohexaose
- alpha-glucans
- maltopentaose
- synthesis
- alpha-amylases
- amylo-1,6-glucosidase
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maltogenic
-
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: Arabidopsis thaliana
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, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
amylomaltase
D-enzyme
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-
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debranching enzyme maltodextrin glycosyltransferase
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dextrin glycosyltransferase
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dextrin glycosyltransferase,
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-
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dextrin transglycosylase
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-
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disproportionating enzyme
amylomaltase
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-
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disproportionating enzyme
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan
catalytic mechanism and domain structure and function
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
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-
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PATHWAY SOURCE
PATHWAYS
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-, -, -, -, -
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
potato amylose + glycosyl acceptor
cycloamylose
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the enzyme can produce cycloamyloses in the range 1650 glucose residues
-
?
1,4-alpha-D-glucan + 1,4-alpha-D-glucan
maltooligosaccharide
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-
-
?
1,4-alpha-D-glucan + 1,4-alpha-D-glucan
maltooligosaccharides
it is proposed that a soluble heteroglycan is the in vivo substrate for DPE2. An alternative route to metabolize the glucan residues in soluble heteroglycane exists in Arabidopsis thaliana
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-
?
additional information
?
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glucose is the major product of the D-enzyme reaction
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?
additional information
?
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glucose is the major product of the D-enzyme reaction
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?
additional information
?
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amylopectin is no substrate, maltose is not a product
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-
?
additional information
?
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amylomaltase is involved in the conversion of maltose to sucrose in the cytosol
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-
?
additional information
?
-
4-alpha-glucanotransferase is essential for maltose metabolism in photosynthetic leaves
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-
?
additional information
?
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DPE2 transfers the non-reducing glucosyl unit from maltose to glycogen by a ping-pong mechanism. The forward reaction, i.e. consumption of maltose, is specific for the beta-anomer of maltose, while the reverse reaction, i.e. production of maltose, is not stereospecific for the acceptor glucose
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-
?
NATURAL SUBSTRATE
NATURAL 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
1,4-alpha-D-glucan + 1,4-alpha-D-glucan
maltooligosaccharides
it is proposed that a soluble heteroglycan is the in vivo substrate for DPE2. An alternative route to metabolize the glucan residues in soluble heteroglycane exists in Arabidopsis thaliana
-
-
?
additional information
?
-
-
amylomaltase is involved in the conversion of maltose to sucrose in the cytosol
-
-
?
additional information
?
-
4-alpha-glucanotransferase is essential for maltose metabolism in photosynthetic leaves
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-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
aplanin
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Bay e 4609, pseudooligosaccharide resembling amylose with a hydroxymethylconduritol unit and a 4-amino-4-deoxy-D-chinorose residue linked to a varying number of alpha-D-glucose units from 7-30
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
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
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). DPE1_ARATH
576
0
64412
Swiss-Prot
Chloroplast (Reliability: 3)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
DPE2 is a modular protein consisting of a family 77 glycosyl hydrolase domain, similar to DPE1, but unlike DPE1 the domain is interrupted by an insertion of about 150 amino acids as well as an N-terminal extension that consists of two carbohydrate binding modules, domain structure and functiosn, overview
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
the glycosyl hydrolase domain alone provides disproportionating activity with a much higher affinity for short maltodextrins than the complete wild-type enzyme, while absence of the carbohydrate binding modules completely abolishes activity with large complex carbohydrates, reflecting the presumed function of DPE2 in vivo
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, stable in 20 mM bis-Tris-propane buffer, pH 6.5, containing 10% glycerol, no loss of activity over 6 months
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lin, T.P.; Preiss, J.
Characterization of D-enzyme (4-alpha-glucanotransferase) in Arabidopsis leaf
Plant Physiol.
86
260-265
1988
Arabidopsis thaliana, Vicia faba, Daucus carota, Solanum lycopersicum, Spinacia oleracea
Kakefuda, G.; Duke, S.H.
Characterization of pea chloroplast D-enzyme (4-alpha-D-glucanotransferase)
Plant Physiol.
91
136-143
1989
Arabidopsis thaliana, Bacillus subtilis, Paenibacillus macerans, Bos taurus, Daucus carota, Escherichia coli, Solanum lycopersicum, Vigna radiata var. radiata, Pisum sativum, Solanum tuberosum, Spinacia oleracea, Triticum aestivum, Zea mays
Jeon, B.S.; Taguchi, H.; Sakai, H.; Ohshima, T.; Wakagi, T.; Matsuzawa, H.
4-alpha-glucanotransferase from the hyperthermophilic archaeon Thermococcus litoralis. Enzyme purification and characterization, and gene cloning, sequencing and expression in Escherichia coli
Eur. J. Biochem.
248
171-178
1997
Arabidopsis thaliana, Dictyoglomus thermophilum, Pyrococcus furiosus, Solanum tuberosum, Streptococcus mitis, Thermococcus litoralis
Colleoni, C.; Dauvillee, D.; Mouille, G.; Buleon, A.; Gallant, D.; Bouchet, B.; Morell, M.; Samuel, M.; Delrue, B.; d'Hulst, C.; Bliard, C.; Nuzillard, J.M.; Ball, S.
Genetic and biochemical evidence for the involvement of alpha-1,4 glucanotransferases in amylopectin synthesis
Plant Physiol.
120
993-1003
1999
Synechocystis sp., Arabidopsis thaliana, Chlamydomonas reinhardtii, Oryza sativa, Zea mays, Chlamydomonas reinhardtii 137C
Colleoni, C.; Dauvillee, D.; Mouille, G.; Morell, M.; Samuel, M.; Slomiany, M.C.; Lienard, L.; Wattebled, F.; d'Hulst, C.; Ball, S.
Biochemical characterization of the Chlamydomonas reinhardtii alpha-1,4 glucanotransferase supports a direct function in amylopectin biosynthesis
Plant Physiol.
120
1005-1014
1999
Arabidopsis thaliana, Chlamydomonas reinhardtii, Escherichia coli, Solanum tuberosum
Wattebled, F.; Ral, J.P.; Dauvillee, D.; Myers, A.M.; James, M.G.; Schlichting, R.; Giersch, C.; Ball, S.G.; D'Hulst, C.
STA11, a Chlamydomonas reinhardtii locus required for normal starch granule biogenesis, encodes disproportionating enzyme. Further evidence for a function of alpha-1,4 glucanotransferases during starch granule biosynthesis in green algae
Plant Physiol.
132
137-145
2003
Arabidopsis thaliana, Borreliella burgdorferi (O51188), Chlamydomonas reinhardtii, Chlamydomonas reinhardtii (Q9FDV9), Chlamydomonas reinhardtii 137C, Clostridium butyricum (Q59266), Escherichia coli, Oryza sativa, Pisum sativum, Saccharomyces cerevisiae, Solanum tuberosum, Solanum tuberosum (Q06801), Streptococcus pneumoniae (P0A4N1), Synechocystis sp., Zea mays
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
Lu, Y.; Sharkey, T.D.
The role of amylomaltase in maltose metabolism in the cytosol of photosynthetic cells
Planta
218
466-473
2004
Arabidopsis thaliana
Lu, Y.; Steichen, J.M.; Yao, J.; Sharkey, T.D.
The role of cytosolic alpha-glucan phosphorylase in maltose metabolism and the comparison of amylomaltase in Arabidopsis and Escherichia coli
Plant Physiol.
142
878-889
2006
Arabidopsis thaliana (Q8RXD9), Escherichia coli
Steichen, J.M.; Petty, R.V.; Sharkey, T.D.
Domain characterization of a 4-alpha-glucanotransferase essential for maltose metabolism in photosynthetic leaves
J. Biol. Chem.
283
20797-20804
2008
Arabidopsis thaliana (Q8RXD9)
Tantanarat, K.; ONeill, E.; Rejzek, M.; Field, R.; Limpaseni, T.
Expression and characterization of 4-alpha-glucanotransferase genes from Manihot esculenta Crantz and Arabidopsis thaliana and their use for the production of cycloamyloses
Process Biochem.
49
84-89
2014
Manihot esculenta, Arabidopsis thaliana (Q9LV91)
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