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Information on EC 2.4.1.25 - 4-alpha-glucanotransferase and Organism(s) Thermotoga maritima and UniProt Accession P80099

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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:
Thermotoga maritima
UNIPROT: P80099
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Word Map
The taxonomic range for the selected organisms is: Thermotoga maritima
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
4-alpha-glucanotransferase
-
-
4-alpha-GTase
-
-
amylomaltase
D-enzyme
-
-
-
-
debranching enzyme maltodextrin glycosyltransferase
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-
-
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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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disproportionating enzyme
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-
-
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maltodextrin glycosyltransferase
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-
maltosyltransferase
-
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
maltoheptaose + maltoheptaose
?
show the reaction diagram
chain length distribution of the transfer products ranges from DP2 to about DP20, which is the upper size limit of oligosaccharides resolved with the TLC system used, but presumably even larger oligomers are also formed. Glucose is not observed as a product. The transfer products exclusively contain 1,4-glucosidic linkages
-
-
?
maltohexaose + maltohexaose
?
show the reaction diagram
chain length distribution of the transfer products ranges from DP2 to about DP20, which is the upper size limit of oligosaccharides resolved with the TLC system used, but presumably even larger oligomers are also formed. Glucose is not observed as a product. The transfer products exclusively contain 1,4-glucosidic linkages
-
-
?
amylopectin
?
show the reaction diagram
incubation of the enzyme with starch or its constituents, i.e. amylose and amylopectin, leads to the formation of a set of multiples of maltose (i.e. maltose, maltotetraose, maltohexaose etc.)
-
-
?
amylopectin + maltopentaose
maltooligosaccharides
show the reaction diagram
-
-
-
?
amylopectin + maltose
?
show the reaction diagram
-
Gtase
-
-
?
amylose
?
show the reaction diagram
incubation of the enzyme with starch or its constituents, i.e. amylose and amylopectin, leads to the formation of a set of multiples of maltose (i.e. maltose, maltotetraose, maltohexaose etc.)
-
-
?
amylose + maltopentaose
maltooligosaccharides
show the reaction diagram
-
-
-
?
amylose + maltose
?
show the reaction diagram
-
Gtase
-
-
?
maltoheptaose + maltopentaose
maltooligosaccharides
show the reaction diagram
-
-
-
?
maltohexaose + maltopentaose
maltooligosaccharides
show the reaction diagram
-
-
-
?
maltopentaose + maltopentaose
maltooligosaccharides
show the reaction diagram
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
new oligosaccharides
show the reaction diagram
-
-
-
-
?
maltotetraose + maltopentaose
maltooligosaccharides
show the reaction diagram
-
-
-
?
maltotriose + maltotriose
maltodextrins
show the reaction diagram
-
Mtase
-
?
starch
?
show the reaction diagram
incubation of the enzyme with starch or its constituents, i.e. amylose and amylopectin, leads to the formation of a set of multiples of maltose (i.e. maltose, maltotetraose, maltohexaose etc.)
-
-
?
starch + maltopentaose
alpha-1,4-D-glucans
show the reaction diagram
-
starch can serve as acceptor molecule in glycosyl transfer reactions
-
?
starch + maltose
?
show the reaction diagram
-
Gtase
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
maltopentaose + maltopentaose
maltooligosaccharides
show the reaction diagram
-
metabolism of starch in the bacterium
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FeCl3
1 mM, 40% loss of activity
HgCl2
0.1 mM, complete loss of activity
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
maltoheptaose
-
stimulating effect of maltooligosaccharides on the conversion of amylose, 15 mM, relative activity 124%
maltohexaose
-
stimulating effect of maltooligosaccharides on the conversion of amylose, 15 mM, relative activity 144%
maltopentaose
-
stimulating effect of maltooligosaccharides on the conversion of amylose, 15 mM, relative activity 210%
maltose
-
stimulating effect of maltooligosaccharides on the conversion of amylose, relative activity 259%
maltotetraose
-
stimulating effect of maltooligosaccharides on the conversion of amylose, 15 mM, relative activity 246%
maltotriose
-
stimulating effect of maltooligosaccharides on the conversion of amylose, 15 mM, relative activity 210%
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.2 - 7.5
more than 50% relative activity at pH values between 5.2 and 7.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
85 - 90
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65 - 95
more than 50% relative activity at temperatures between 65°C and 95°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
53000
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SDS-PAGE
56000
-
size exclusion chromatography
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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1 * 53000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapor-diffusion method
Gtase, hanging drop method, inhibitor complex,crystals belong to space group I222, unit-cell dimensions a = 92.6 A, b = 180.3 A, c = 199.2 A, free Gtase crystals a = 94.5 A, b = 181.4 A, c = 197.3 A
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hanging-drop vapor-diffusion method
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.2 - 7.5
2 h, 80°C, less than 25% loss of initial activity
747689
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37 - 80
-
stable at 37°C, retains more than 90% of its maximum activity between 55-80°C, half-life of activity of about 3 h at 80°C
85
half-life: 17 h
90
half-life: 2.5 h
95
50% inactivation within 10 min
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
high-level expression of recombinant 4-alpha-glucanotransferase under control of the tac promoter is achieved in Escherichia coli
chromosomal gene cloned and expressed in Escherichia coli and Corynebacterium glutamicum
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cloned and expressed in Escherichia coli
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expression in Escherichia coli
expression in Escherichia coli strain BL21
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
food industry
TmalphaGT can be used to produce granular corn starch, which contains amylose and amylopectin having lower molecular weights and a thermoreversible gelation property
synthesis
production of isomalto-oligosaccharides
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Liebl, W.; Feil, R.; Gabelsberger, J.; Kellermann, J.; Schleifer, K.H.
Purification and characterization of a novel thermostable 4-alpha-glucanotransferase of Thermotoga maritima cloned in Escherichia coli
Eur. J. Biochem.
207
81-88
1992
Bacillus sp. (in: Bacteria), Thermotoga maritima, Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
Manually annotated by BRENDA team
Goda, S.K.; Eissa, O.; Akhtar, M.; Minton, N.P.
Molecular analysis of a Clostridium butyricum NCIMB 7423 gene encoding 4-alpha-glucanotransferase and characterization of the recombinant enzyme produced in Escherichia coli
Microbiology
143
3287-3294
1997
Clostridium butyricum, Streptococcus pneumoniae, Escherichia coli, Solanum tuberosum, Thermotoga maritima, Clostridium butyricum NCIMB 7423
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Kim, K.Y.; Kim, C.H.
Expression of Thermotoga maritima 4-alpha-glucanotransferase gene in E. coli and characterization of the recombinant enzyme
Agric. Chem. Biotechnol.
47
133-136
2004
Thermotoga maritima
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Oh, E.J.; Choi, S.J.; Lee, S.J.; Kim, C.H.; Moon, T.W.
Modification of granular corn starch with 4-alpha-glucanotransferase from Thermotoga maritima: effects on structural and physical properties
J. Food Sci.
73
C158-C166
2008
Thermotoga maritima (Q60035), Thermotoga maritima
Manually annotated by BRENDA team
Huber, W.; Liebl, W.
Acceptor specificity of 4-alpha-glucanotransferase of Thermotoga maritima
Biocatal. Biotransform.
11
105-115
1994
Thermotoga maritima (P80099), Thermotoga maritima DSM 3109 (P80099)
-
Manually annotated by BRENDA team
Raasch, C.; Roujeinikova, A.; Meissner, H.; Rice, D.; Liebl, W.
Biochemical properties and structural features of the thermostable maltodextrin transglycosidases from Thermotoga maritima
Biologia
57
101-108
2002
Thermotoga maritima (O33838), Thermotoga maritima (P80099), Thermotoga maritima DSM 3109 (O33838), Thermotoga maritima DSM 3109 (P80099)
-
Manually annotated by BRENDA team
Meissner, H.; Liebl, W.
Thermotoga maritima maltosyltransferase, a novel type of maltodextrin glycosyltransferase acting on starch and malto-oligosaccharides
Eur. J. Biochem.
258
1050-1058
1998
Thermotoga maritima (O33838), Thermotoga maritima, Thermotoga maritima DSM 3109 (O33838)
Manually annotated by BRENDA team