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Information on EC 5.4.99.15 - (1->4)-alpha-D-glucan 1-alpha-D-glucosylmutase and Organism(s) Saccharolobus solfataricus and UniProt Accession Q7LX98
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5.4.99.15 (1->4)-alpha-D-glucan 1-alpha-D-glucosylmutaseIUBMB Comments
The enzyme from Arthrobacter sp., Sulfolobus acidocaldarius acts on (1->4)-alpha-D-glucans containing three or more (1->4)-alpha-linked D-glucose units. Not active towards maltose.
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Word Map
- 5.4.99.15
-
trehalohydrolase
- sulfolobus
- maltooligosaccharides
- starch
-
transglycosylation
- acidocaldarius
- maltose
- archaeon
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trey
- maltopentaose
- solfataricus
-
non-reducing
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arthrobacter
- alpha-amylase
- dextrins
- maltotriose
-
trehalose-producing
- synthesis
- maltohexaose
- anabaena
-
thermoacidophilic
-
archaebacterium
- trehalose-6-phosphate
- shibatae
-
alpha-1,4-glucosidic
- maltotetraose
-
alpha-1,4
The taxonomic range for the selected organisms is: Saccharolobus solfataricus
The expected taxonomic range for this enzyme is: Bacteria, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Reaction Schemes
Synonyms
maltooligosyltrehalose synthase, mtsase, maltooligosyl trehalose synthase, malto-oligosyltrehalose synthase, trehalosyl dextrin-forming enzyme, sstdfe, protein st0929, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(1,4)-alpha-D-glucan 1-alpha-D-glucosylmutase
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(1->4)-alpha-D-Glucan 1-alpha-glucosylmutase
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Cellulase (Arthrobacter strain Q36 clone pBMT13 trehalose oligosaccharide-forming)
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Cellulase (Rhizobium strain M11 clone pBMT7 trehalose oligosaccharide-forming)
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Malto-oligosyltrehalose synthase
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Maltodextrin alpha-D-glucosyltransferase
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Maltooligosyl trehalose synthase (Rhizobium strain M-11 clone pBMTU1 gene treY reduced)
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MTSase
Synthase, maltooligosyltrehalose (Rhizobium strain M-11 clone pBMTU1 gene treY reduced)
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Synthase, maltooligosyltrehalose (Sulfolobus acidocaldarius clone pBST1 gene treY)
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Sythase, maltooligosyltrehalose (Arthrobacter clone pBRT4 gene treY)
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MTSase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
intramolecular transglucosylation
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-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
(1->4)-alpha-D-glucan 1-alpha-D-glucosylmutase
The enzyme from Arthrobacter sp., Sulfolobus acidocaldarius acts on (1->4)-alpha-D-glucans containing three or more (1->4)-alpha-linked D-glucose units. Not active towards maltose.
CAS REGISTRY NUMBER
COMMENTARY
170780-49-1
-
171265-12-6
cellulase (Rhizobium strain M11 clone pBMT7 trehalose oligosaccharide-forming) /maltooligosyl trehalose synthase (Rhizobium strain M-11 clone pBMTU1 gene treY reduced) /synthase, maltooligosyltrehalose (Rhizobium strain M-11 clone pBMTU1 gene treY reduced)
171265-13-7
cellulase (Arthrobacter strain Q36 clone pBMT13 trehalose oligosaccharide-forming) /synthase, maltooligosyltrehalose (Arthrobacter clone pBRT4 gene treY)
184890-98-0
synthase, maltooligosyltrehalose (Sulfolobus acidocaldarius clone pBST1 gene treY)
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
maltoheptaose
alpha-maltopentaosyl trehalose
preferred substrate, ratio of transglycosylation to hydrolysis is 100:0.2, recombinant enzyme
i.e. alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->1)-alpha-D-Glcp
-
?
maltohexaose
alpha-maltotetraosyl trehalose
ratio of transglycosylation to hydrolysis is 90:0.2, recombinant enzyme
i.e. alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->1)-alpha-D-Glcp
-
?
maltotetraose
alpha-maltosyl trehalose
ratio of transglycosylation to hydrolysis is 38:0.6, recombinant enzyme
i.e. alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->1)-alpha-D-Glcp
-
?
maltotriose
alpha-glucosyltrehalose
ratio of transglycosylation to hydrolysis is 10:1.4, recombinant enzyme
i.e. alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->1)-alpha-D-Glcp
-
?
Maltopentaose
alpha-Maltotriosyl trehalose
ratio of transglycosylation to hydrolysis is 77:0.6, recombinant enzyme
i.e. alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->1)-alpha-D-Glcp
-
?
Maltopentaose
alpha-Maltotriosyl trehalose
the enzyme also cytalyzes the hydrolysis of maltopentaose
i.e. alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->1)-alpha-D-Glcp
-
?
maltoheptaose
alpha-maltopentaosyl trehalose
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-
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?
maltoheptaose
alpha-maltopentaosyl trehalose
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preferred substrate
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-
?
maltoheptaose
alpha-maltopentaosyl trehalose
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88.6% of the activity compared to maltopentaose
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-
?
maltohexaose
alpha-maltotetraosyl trehalose
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preferred substrate
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-
?
maltohexaose
alpha-maltotetraosyltrehalose
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80% of the activity compared to maltopentaose
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-
?
maltotetraose
alpha-maltosyltrehalose
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46.3% of the activity compared to maltopentaose
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-
?
maltotriose
alpha-glucosyltrehalose
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5.0% of the activity compared to maltopentaose
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?
additional information
?
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key enzyme in the synthesis of trehalose
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?
additional information
?
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key enzyme in the synthesis of trehalose
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?
additional information
?
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mainly catalyzes an intramolecular transglycosyl reaction to form trehalosyl dextrins from dextrins by converting the alpha-1,4-glucosidic linkage at the reducing end to an alpha-1,1-glucosidic linkage
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?
additional information
?
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enzyme is involved in the pathway of trehalose synthesis from starch
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?
additional information
?
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starch, amylose and amylopectin are no good substrates, MTS is not active on maltotriose
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?
additional information
?
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no activity with maltose. The enzyme never produces a glycosyltrehalose of longer chain length than the substrate used. Glucose and maltooligosaccharide shortened by one glucose residue are produced as by-products
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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
additional information
?
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key enzyme in the synthesis of trehalose
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?
additional information
?
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key enzyme in the synthesis of trehalose
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?
additional information
?
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enzyme is involved in the pathway of trehalose synthesis from starch
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
metal ions are not required for activity. Ca2+, K+, Mg2+, or Na+ have no activating or inhibiting effect on activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
Ca2+, K+, Mg2+, or Na+ have no activating or inhibiting effect on activity
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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
5.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.3 - 6
pH 4.3: about 75% of maximal activity, pH 6.0: about 80% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45 - 90
45°C: about 60% of maximal activity, 90°C: about 55% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
key enzyme in the synthesis of trehalose
physiological function
key enzyme in the synthesis of trehalose
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A406
compared with wild-type enzyme, the hydrolysis:transglycosylation selectivity ratio is significantly increased
D411A
significant reductions in catalytic efficiency, increase in the transition-state energy
D610A
significant reductions in catalytic efficiency, increase in the transition-state energy
P402
compared with wild-type enzyme, the hydrolysis:transglycosylation selectivity ratio is significantly decreased
R614A
significant reductions in catalytic efficiency, increase in the transition-state energy
V426
little change in hydrolysis:transglycosylation selectivity ratio
A406S
the hydrolysis/transglycosylation selectivity ratio shows little change
D411A
significant reductions in catalytic efficiency and increase in the transition-state energy
D610A
significant reductions in catalytic efficiency and increase in the transition-state energy
F405S
-
depending on substrate, 29-97% of wild-type transglycosylation efficiency, hydrolytic activity is 16% of wild-type
F405Y
P402Q
the hydrolysis/transglycosylation selectivity ratio is significantly decreased
R614A
significant reductions in catalytic efficiency and increase in the transition-state energy
Y290F
-
mutation located near subsite +1 constructed to alter enzyme selectivity. Catalytic efficiency for hydrolysis and transglycosylation reaction are 6.6 and 5.6% resp., of wild-type
Y367F
-
mutation located near subsite +1 constructed to alter enzyme selectivity. Catalytic efficiency for hydrolysis and transglycosylation reaction are about half of wild-type
Y409F
-
mutation located near subsite +1 constructed to alter enzyme selectivity. Catalytic efficiency for hydrolysis is similar to wild-type, for transglycosylation reaction somewhat lower than wild-type
F405Y
-
mutation located near subsite +1 constructed to alter enzyme selectivity. Catalytic efficiency for transglycosylation reaction is similar to wild-type, for hydrolysis somewhat lower than wild-type
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
75
-
MTS proves stable at 75°C for more than 24 h, with a half life of about 50 h
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned from the genomic DNA of Sulfolobus solfataricus ATCC 35092 to an expression vector with a T7 lac promoter and then expressed in Escherichia coli
wild-type and mutant enzymes are expressed in Escherichia coli Rosetta (DE3)
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kato, M.; Miura, Y.; Kettoku, M.; Shindo, K.; Iwamatsu, A.; Kobayashi, M.
Purification and characterization of new trehalose-producing enzymes isolated from the hyperthermophilic archae, Sulfolobus sulfataricus KM1
Biosci. Biotechnol. Biochem.
60
546-550
1996
Saccharolobus solfataricus, Saccharolobus solfataricus KM1
Fang, T.; Tseng, W.; Chung, Y.; Pan, C.
Mutations on aromatic residues of the active site to alter selectivity of the Sulfolobus solfataricus maltooligosyltrehalose synthase
J. Agric. Food Chem.
54
3585-3590
2006
Saccharolobus solfataricus
Fang, T.Y.; Tseng, W.C.; Pan, C.H.; Chun, Y.T.; Wang, M.Y.
Protein engineering of Sulfolobus solfataricus maltooligosyltrehalose synthase to alter its selectivity
J. Agric. Food Chem.
55
5588-5594
2007
Saccharolobus solfataricus
Fang, T.Y.; Tseng, W.C.; Shih, T.Y.; Wang, M.Y.
Identification of the essential catalytic residues and selectivity-related residues of maltooligosyltrehalose trehalohydrolase from the thermophilic archaeon Sulfolobus solfataricus ATCC 35092
J. Agric. Food Chem.
56
5628-5633
2008
Saccharolobus solfataricus
Cimini, D.; De Rosa, M.; Panariello, A.; Morelli, V.; Schiraldi, C.
Production of a thermophilic maltooligosyl-trehalose synthase in Lactococcus lactis
J. Ind. Microbiol. Biotechnol.
35
1079-1083
2008
Saccharolobus solfataricus, Saccharolobus solfataricus MT4
Kato, M.; Miura, Y.; Kettoku, M.; Shindo, K.; Iwamatsu, A.; Kobayashi, K.
Reaction mechanism of a new glycosyltrehalose-producing enzyme isolated from the hyperthermophilic archaeum, Sulfolobus solfataricus KM1
Biosci. Biotechnol. Biochem.
60
921-924
1996
Saccharolobus solfataricus, Saccharolobus solfataricus KM1
Kato, M.
Trehalose production with a new enzymatic system from Sulfolobus solfataricus KM1
J. Mol. Catal. B
6
223-233
1999
Saccharolobus solfataricus, Saccharolobus solfataricus KM1
-
Tseng, W.C.; Lin, C.R.; Hung, X.G.;, Wei, T.Y.; Chen, Y.C.; Fang, T.Y.
Identification of substrate-binding and selectivity-related residues of maltooligosyltrehalose synthase from the thermophilic archaeon Sulfolobus solfataricus ATCC 35092
Enzyme Microb. Technol.
56
53-59
2014
Saccharolobus solfataricus, Saccharolobus solfataricus (Q7LX98), Saccharolobus solfataricus P2 (Q7LX98), Saccharolobus solfataricus ATCC 35092
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