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Information on EC 2.4.1.25 - 4-alpha-glucanotransferase and Organism(s) Thermococcus litoralis and UniProt Accession O32462
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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: Thermococcus litoralis
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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debranching enzyme maltodextrin glycosyltransferase
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-
-
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dextrin glycosyltransferase
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-
-
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dextrin glycosyltransferase,
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-
-
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dextrin transglycosylase
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-
-
-
disproportionating enzyme
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-
-
-
amylomaltase
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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
2-chloro-4-nitrophenyl 4'''',6''''-O-(3-oxobutylidene)maltopentaoside + D-glucose
?
-
the disproportionation reaction of the enzyme involves a ping-pong bi-bi mechanism. On the basis of this reaction mechanism, the glycosyl-enzyme intermediate, in which a donor substrate is covalently bound to the catalytic nucleophile, is trapped by treating the enzyme with 3-ketobutylidene-beta-2-chloro-4-nitrophenyl maltopentaoside in the absence of an acceptor and is detected by matrix-assisted laser desorption ionization time-of-flight mass spectrometry after peptic digestion
-
-
?
amylose + D-glucose
low molecular mass oligosaccharides
-
synthetic amylose AS-320
-
?
maltooligosaccharides
maltooligosaccharides + D-glucose
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-
-
?
maltotriose + maltotriose
maltopentaose + maltotetraose
-
-
-
?
starch + D-glucose
low molecular mass oligosaccharides
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soluble starch
-
?
amylose + maltopentaose
cyclic alpha-1,4-glucan
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-
cycloamylose
?
amylose + maltopentaose
cyclic alpha-1,4-glucan
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-
cycloamylose
?
amylose + maltopentaose
cyclic alpha-1,4-glucan
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-
cycloamylose
?
amylose + maltopentaose
cyclic alpha-1,4-glucan
-
cycloamylose
?
maltose + maltose
maltotriose + glucose
key role in maltose metabolism
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-
?
additional information
?
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enzyme catalyzes not only intermolecular transglycosylation to produce linear alpha-1,4-glucan, but also intramolecular transglycosylation to produce cyclic alpha-1,4-glucan
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-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
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
90
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70 - 105
70°C: about 60% of maximal activity, 105°C: about 50% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
key enzymes in the pathway for maltose catabolism. Glucose derived from the action of 4-alpha-glucanotransferase is subsequently metabolized via an Embden-Meyerhof pathway
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method at 25°C, crystal structure of the enzyme with and without an inhibitor, acarbose. The acarbose-bound structure clarifies that Glu123 and Asp214 are the catalytic nucleophile and acid/base catalyst, respectively
crystallized in 2 forms, I and II, form I crystals belongs to hexagonal space group P6(4)22, form II crystals to orthorhombic space group P2(1)2(1)2
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D214N
the specific activity of the D214N mutant is decreased about 10000fold as compared with that of the wild-type enzyme
E123Q
-
the specific activity of the mutant enzyme toward maltotriose is about 15000fold lower than the specific activity of the wild-type enzyme
E129Q
-
the specific activity of the mutant enzyme is almost the same as that of the wild-type enzyme
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
genes of wild-type and mutant enzymes are coexpressed in Escherichia coli cells with GroELS, tRNA(AGA), and tRNA(AGG)
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Imamura, H.; Jeon, B.; Wakagi, T.; Matsuzawa, H.
High level expression of Thermococcus litoralis 4-alpha-glucanotransferase in a soluble form in Escherichia coli with a novel expression system involving minor arginine tRNAs and GroELS
FEBS Lett.
457
393-396
1999
Thermococcus litoralis
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)
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
Imamura, H.; Fushinobu, S.; Yamamoto, M.; Kumasaka, T.; Jeon, B.S.; Wakagi, T.; Matsuzawa, H.
Crystal structures of 4-alpha-glucanotransferase from Thermococcus litoralis and its complex with an inhibitor
J. Biol. Chem.
278
19378-19386
2003
Dictyoglomus thermophilum, Pyrococcus furiosus, Thermococcus kodakarensis, Solanum tuberosum, Thermococcus litoralis, Thermococcus litoralis (O32462), Thermus aquaticus, Thermococcus litoralis DSM 5473 (O32462)
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
Imamura, H.; Fushinobu, S.; Jeon, B.S.; Wakagi, T.; Matsuzawa, H.
Identification of the catalytic residue of Thermococcus litoralis 4-alpha-glucanotransferase through mechanism-based labeling
Biochemistry
40
12400-12406
2001
Thermococcus litoralis
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