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Information on EC 5.4.99.15 - (1->4)-alpha-D-glucan 1-alpha-D-glucosylmutase
for references in articles please use BRENDA:EC5.4.99.15
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EC Tree 5 Isomerases
5.4 Intramolecular transferases
5.4.99 Transferring other groups
5.4.99.15 (1->4)-alpha-D-glucan 1-alpha-D-glucosylmutase
IUBMB Comments
The enzyme from Arthrobacter sp., Sulfolobus acidocaldarius acts on (1→4)-α-D-glucans containing three or more (1→4)-α-linked D-glucose units. Not active towards maltose.
The expected taxonomic range for this enzyme is: Bacteria, Archaea
- 5.4.99.15
-
trehalohydrolase
- sulfolobus
- maltooligosaccharides
- starch
-
transglycosylation
- acidocaldarius
- maltose
- archaeon
-
trey
- maltopentaose
- solfataricus
-
non-reducing
-
arthrobacter
- alpha-amylase
- dextrins
- maltotriose
-
trehalose-producing
- synthesis
- maltohexaose
- anabaena
-
thermoacidophilic
-
archaebacterium
- trehalose-6-phosphate
- shibatae
-
alpha-1,4-glucosidic
- maltotetraose
-
alpha-1,4
Reaction Schemes
showSynonyms
maltooligosyltrehalose synthase, mtsase, maltooligosyl trehalose synthase, malto-oligosyltrehalose synthase, trehalosyl dextrin-forming enzyme, sstdfe, protein st0929, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(1,4)-alpha-D-glucan 1-alpha-D-glucosylmutase
-
-
-
-
(1->4)-alpha-D-Glucan 1-alpha-glucosylmutase
-
-
-
-
Cellulase (Arthrobacter strain Q36 clone pBMT13 trehalose oligosaccharide-forming)
-
-
-
-
Cellulase (Rhizobium strain M11 clone pBMT7 trehalose oligosaccharide-forming)
-
-
-
-
Malto-oligosyltrehalose synthase
-
-
-
-
Maltodextrin alpha-D-glucosyltransferase
-
-
-
-
maltooligosyl trehalose synthase
Maltooligosyl trehalose synthase (Rhizobium strain M-11 clone pBMTU1 gene treY reduced)
-
-
-
-
maltooligosyl-trehalose synthase
maltooligosyltrehalose synthase
MTS
MTSase
MTSH
SEB24
SP3.5
SSO2095
SsTDFE
Synthase, maltooligosyltrehalose (Rhizobium strain M-11 clone pBMTU1 gene treY reduced)
-
-
-
-
Synthase, maltooligosyltrehalose (Sulfolobus acidocaldarius clone pBST1 gene treY)
-
-
-
-
Sythase, maltooligosyltrehalose (Arthrobacter clone pBRT4 gene treY)
-
-
-
-
TDFE
trehalosyl dextrin-forming enzyme
TreY
maltooligosyl trehalose synthase
Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
-
-
maltooligosyltrehalose synthase
Sulfolobus acidocaldarius ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770
-
-
MTSase
-
-
-
-
MTSH
-
fusion enzyme consisting of maltooligosyltrehalose synthase and maltooligosyltrehalose trehalohydrolase
MTSH
-
fusion enzyme consisting of maltooligosyltrehalose synthase and maltooligosyltrehalose trehalohydrolase
-
MTSH
-
fusion enzyme consisting of maltooligosyltrehalose synthase and maltooligosyltrehalose trehalohydrolase
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
4-[(1->4)-alpha-D-glucosyl]n-1-D-glucose = 1-alpha-D-[(1->4)-alpha-D-glucosyl]n-1-alpha-D-glucopyranoside
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
intramolecular transglucosylation
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
trehalose biosynthesis V
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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.
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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)
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-[(1->4)-alpha-D-glucosyl]n-1-D-glucose
1-alpha-D-[(1->4)-alpha-D-glucosyl]n-1-alpha-D-glucopyranoside
alpha-maltotriosyl trehalose
maltopentaose
-
Substrates: -
Products: -
Products: -
?
Short chain amylose
?
-
Substrates: 43% of the activity with maltopentaose
Products: -
Products: -
?
4-[(1->4)-alpha-D-glucosyl]n-1-D-glucose
1-alpha-D-[(1->4)-alpha-D-glucosyl]n-1-alpha-D-glucopyranoside
Substrates: -
Products: -
Products: -
?
4-[(1->4)-alpha-D-glucosyl]n-1-D-glucose
1-alpha-D-[(1->4)-alpha-D-glucosyl]n-1-alpha-D-glucopyranoside
Sulfolobus acidocaldarius ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770
Substrates: -
Products: -
Products: -
?
4-[(1->4)-alpha-D-glucosyl]n-1-D-glucose
1-alpha-D-[(1->4)-alpha-D-glucosyl]n-1-alpha-D-glucopyranoside
Substrates: -
Products: -
Products: -
?
4-[(1->4)-alpha-D-glucosyl]n-1-D-glucose
1-alpha-D-[(1->4)-alpha-D-glucosyl]n-1-alpha-D-glucopyranoside
Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
Substrates: -
Products: -
Products: -
?
dextrin
?
-
Substrates: the enzyme transforms starch and dextrins to the corresponding trehalosyl derivatives with an intramolecular transglycosylation process that converts the glucosidic linkage at the reducing end from alpha-1,4 to alpha-1,1
Products: -
Products: -
?
dextrin
?
Saccharolobus shibatae DMS 5389
-
Substrates: the enzyme transforms starch and dextrins to the corresponding trehalosyl derivatives with an intramolecular transglycosylation process that converts the glucosidic linkage at the reducing end from alpha-1,4 to alpha-1,1
Products: -
Products: -
?
liquified corn starch
?
-
Substrates: -
Products: in presence of maltooligosyltrehalose trehalohydrolase, conversion of soluble starch into trehalose
Products: in presence of maltooligosyltrehalose trehalohydrolase, conversion of soluble starch into trehalose
?
liquified corn starch
?
-
Substrates: -
Products: in presence of maltooligosyltrehalose trehalohydrolase, conversion of soluble starch into trehalose
Products: in presence of maltooligosyltrehalose trehalohydrolase, conversion of soluble starch into trehalose
?
Maltoheptaose
?
-
Substrates: 58% of the activity with maltopentaose
Products: -
Products: -
?
Maltoheptaose
?
-
Substrates: 58% of the activity with maltopentaose
Products: -
Products: -
?
Maltoheptaose
?
-
Substrates: 92% of the activity with maltopentaose
Products: -
Products: -
?
maltoheptaose
alpha-maltopentaosyl trehalose
-
Substrates: -
Products: -
Products: -
?
maltoheptaose
alpha-maltopentaosyl trehalose
-
Substrates: preferred substrate
Products: -
Products: -
?
maltoheptaose
alpha-maltopentaosyl trehalose
-
Substrates: -
Products: -
Products: -
?
maltoheptaose
alpha-maltopentaosyl trehalose
-
Substrates: 88.6% of the activity compared to maltopentaose
Products: -
Products: -
?
maltoheptaose
alpha-maltopentaosyl trehalose
Substrates: preferred substrate, ratio of transglycosylation to hydrolysis is 100:0.2, recombinant enzyme
Products: 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
Products: 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
?
maltoheptaose
alpha-maltopentaosyl trehalose
-
Substrates: -
Products: -
Products: -
?
maltoheptaose
alpha-maltopentaosyl trehalose
-
Substrates: 88.6% of the activity compared to maltopentaose
Products: -
Products: -
?
maltoheptaose
alpha-maltopentaosyl trehalose
-
Substrates: preferred substrate
Products: -
Products: -
?
maltoheptaose
alpha-maltopentaosyl trehalose
Substrates: preferred substrate, ratio of transglycosylation to hydrolysis is 100:0.2, recombinant enzyme
Products: 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
Products: 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
?
-
Substrates: 45% of the activity with maltopentaose
Products: -
Products: -
?
Maltohexaose
?
-
Substrates: 45% of the activity with maltopentaose
Products: -
Products: -
?
Maltohexaose
?
-
Substrates: 145% of the activity with maltopentaose
Products: -
Products: -
?
maltohexaose
alpha-maltotetraosyl trehalose
-
Substrates: -
Products: -
Products: -
?
maltohexaose
alpha-maltotetraosyl trehalose
-
Substrates: -
Products: -
Products: -
?
maltohexaose
alpha-maltotetraosyl trehalose
-
Substrates: -
Products: -
Products: -
?
maltohexaose
alpha-maltotetraosyl trehalose
-
Substrates: -
Products: -
Products: -
?
maltohexaose
alpha-maltotetraosyl trehalose
EF433294
Substrates: -
Products: -
Products: -
?
maltohexaose
alpha-maltotetraosyl trehalose
-
Substrates: -
Products: -
Products: -
?
maltohexaose
alpha-maltotetraosyl trehalose
-
Substrates: preferred substrate
Products: -
Products: -
?
maltohexaose
alpha-maltotetraosyl trehalose
Substrates: ratio of transglycosylation to hydrolysis is 90:0.2, recombinant enzyme
Products: 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
Products: 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
?
maltohexaose
alpha-maltotetraosyl trehalose
-
Substrates: preferred substrate
Products: -
Products: -
?
maltohexaose
alpha-maltotetraosyl trehalose
Substrates: ratio of transglycosylation to hydrolysis is 90:0.2, recombinant enzyme
Products: 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
Products: 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
?
maltohexaose
alpha-maltotetraosyltrehalose
-
Substrates: -
Products: -
Products: -
?
maltohexaose
alpha-maltotetraosyltrehalose
-
Substrates: 80% of the activity compared to maltopentaose
Products: -
Products: -
?
maltohexaose
alpha-maltotetraosyltrehalose
-
Substrates: -
Products: -
Products: -
?
maltohexaose
alpha-maltotetraosyltrehalose
-
Substrates: 80% of the activity compared to maltopentaose
Products: -
Products: -
?
Maltopentaose
alpha-Maltotriosyl trehalose
-
Substrates: -
Products: -
Products: -
?
Maltopentaose
alpha-Maltotriosyl trehalose
-
Substrates: -
Products: -
Products: -
?
Maltopentaose
alpha-Maltotriosyl trehalose
-
Substrates: -
Products: -
Products: -
?
Maltopentaose
alpha-Maltotriosyl trehalose
Substrates: the enzyme also cytalyzes the hydrolysis of maltopentaose
Products: 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
Products: 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
Substrates: ratio of transglycosylation to hydrolysis is 77:0.6, recombinant enzyme
Products: 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
Products: 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
-
Substrates: -
Products: -
Products: -
?
Maltopentaose
alpha-Maltotriosyl trehalose
Substrates: the enzyme also cytalyzes the hydrolysis of maltopentaose
Products: 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
Products: 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
Substrates: ratio of transglycosylation to hydrolysis is 77:0.6, recombinant enzyme
Products: 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
Products: 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
-
Substrates: -
Products: -
Products: -
?
maltopentaose
alpha-maltotriosyltrehalose
-
Substrates: -
Products: -
Products: -
?
maltopentaose
alpha-maltotriosyltrehalose
-
Substrates: -
Products: -
Products: -
?
Maltotetraose
?
-
Substrates: 25% of the activity with maltopentaose
Products: -
Products: -
?
Maltotetraose
?
-
Substrates: 25% of the activity with maltopentaose
Products: -
Products: -
?
Maltotetraose
?
-
Substrates: 23% of the activity with maltopentaose
Products: -
Products: -
?
maltotetraose
alpha-maltosyl trehalose
Substrates: ratio of transglycosylation to hydrolysis is 38:0.6, recombinant enzyme
Products: i.e. alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->1)-alpha-D-Glcp
Products: i.e. alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->1)-alpha-D-Glcp
?
maltotetraose
alpha-maltosyl trehalose
Substrates: ratio of transglycosylation to hydrolysis is 38:0.6, recombinant enzyme
Products: i.e. alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->1)-alpha-D-Glcp
Products: i.e. alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->1)-alpha-D-Glcp
?
maltotetraose
alpha-maltosyltrehalose
-
Substrates: -
Products: -
Products: -
?
maltotetraose
alpha-maltosyltrehalose
-
Substrates: 46.3% of the activity compared to maltopentaose
Products: -
Products: -
?
maltotetraose
alpha-maltosyltrehalose
-
Substrates: -
Products: -
Products: -
?
maltotetraose
alpha-maltosyltrehalose
-
Substrates: 46.3% of the activity compared to maltopentaose
Products: -
Products: -
?
maltotriose
alpha-glucosyltrehalose
-
Substrates: 5.0% of the activity compared to maltopentaose
Products: -
Products: -
?
maltotriose
alpha-glucosyltrehalose
Substrates: ratio of transglycosylation to hydrolysis is 10:1.4, recombinant enzyme
Products: i.e. alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->1)-alpha-D-Glcp
Products: i.e. alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->1)-alpha-D-Glcp
?
maltotriose
alpha-glucosyltrehalose
-
Substrates: -
Products: -
Products: -
?
maltotriose
alpha-glucosyltrehalose
-
Substrates: 5.0% of the activity compared to maltopentaose
Products: -
Products: -
?
maltotriose
alpha-glucosyltrehalose
Substrates: ratio of transglycosylation to hydrolysis is 10:1.4, recombinant enzyme
Products: i.e. alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->1)-alpha-D-Glcp
Products: i.e. alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->1)-alpha-D-Glcp
?
soluble starch
?
-
Substrates: -
Products: in presence of maltooligosyltrehalose trehalohydrolase, conversion of soluble starch into trehalose
Products: in presence of maltooligosyltrehalose trehalohydrolase, conversion of soluble starch into trehalose
?
soluble starch
?
-
Substrates: -
Products: in presence of maltooligosyltrehalose trehalohydrolase, conversion of soluble starch into trehalose
Products: in presence of maltooligosyltrehalose trehalohydrolase, conversion of soluble starch into trehalose
?
starch
?
-
Substrates: the enzyme transforms starch and dextrins to the corresponding trehalosyl derivatives with an intramolecular transglycosylation process that converts the glucosidic linkage at the reducing end from alpha-1,4 to alpha-1,1
Products: -
Products: -
?
starch
?
Saccharolobus shibatae DMS 5389
-
Substrates: the enzyme transforms starch and dextrins to the corresponding trehalosyl derivatives with an intramolecular transglycosylation process that converts the glucosidic linkage at the reducing end from alpha-1,4 to alpha-1,1
Products: -
Products: -
?
additional information
?
-
-
Substrates: no reaction with maltose
Products: -
Products: -
?
additional information
?
-
-
Substrates: no reaction with maltose
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme converts maltooligosaccharides into maltooligosyltrehalose
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme is involved in the pathway of trehalose synthesis from starch
Products: -
Products: -
?
additional information
?
-
-
Substrates: starch, amylose and amylopectin are no good substrates, MTS is not active on maltotriose
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: key enzyme in the synthesis of trehalose
Products: -
Products: -
?
additional information
?
-
Substrates: key enzyme in the synthesis of trehalose
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme is involved in the pathway of trehalose synthesis from starch
Products: -
Products: -
?
additional information
?
-
-
Substrates: starch, amylose and amylopectin are no good substrates, MTS is not active on maltotriose
Products: -
Products: -
?
additional information
?
-
Substrates: key enzyme in the synthesis of trehalose
Products: -
Products: -
?
additional information
?
-
-
Substrates: possible mechanism of action: after converting the alpha-1,4-glucosidic linkage to an alpha-1,1-glucosidic linkage at the reducing end of maltooligosaccharide Glc(n) is able to release glucose and maltooligosaccharide Glc(n-1) residues. Then the intramolecular transglycosylation and the hydrolytic reaction continues with maltooligosaccharide Glc(n-1) until the initial maltooligosaccharide is reduced to maltose
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme of trehalose biosynthesis
Products: -
Products: -
?
additional information
?
-
-
Substrates: MTSase catalyzes the transglycosylation of the reducing-end maltose alpha-1,4-glucosidic bond of its oligosaccharide substrate to a trehalose alpha-1,1-glucosidic bond
Products: -
Products: -
?
additional information
?
-
Substrates: the archaeal enzyme catalyzes an intramolecular transglycosylation reaction and converts the glycosidic bond at the reducing end of dextrins from alpha-1,4 (reducing end) into alpha-1,1 (non-reducing end). Maltodextrin and maltooligosaccharide are used as substrates by the enzyme but maltose, chitooligosaccharide, sucrose and beta-cyclodextrin are no substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: the archaeal enzyme catalyzes an intramolecular transglycosylation reaction and converts the glycosidic bond at the reducing end of dextrins from alpha-1,4 (reducing end) into alpha-1,1 (non-reducing end). Maltodextrin and maltooligosaccharide are used as substrates by the enzyme but maltose, chitooligosaccharide, sucrose and beta-cyclodextrin are no substrates
Products: -
Products: -
?
additional information
?
-
Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
Substrates: the archaeal enzyme catalyzes an intramolecular transglycosylation reaction and converts the glycosidic bond at the reducing end of dextrins from alpha-1,4 (reducing end) into alpha-1,1 (non-reducing end). Maltodextrin and maltooligosaccharide are used as substrates by the enzyme but maltose, chitooligosaccharide, sucrose and beta-cyclodextrin are no substrates
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-[(1->4)-alpha-D-glucosyl]n-1-D-glucose
1-alpha-D-[(1->4)-alpha-D-glucosyl]n-1-alpha-D-glucopyranoside
4-[(1->4)-alpha-D-glucosyl]n-1-D-glucose
1-alpha-D-[(1->4)-alpha-D-glucosyl]n-1-alpha-D-glucopyranoside
Substrates: -
Products: -
Products: -
?
4-[(1->4)-alpha-D-glucosyl]n-1-D-glucose
1-alpha-D-[(1->4)-alpha-D-glucosyl]n-1-alpha-D-glucopyranoside
Sulfolobus acidocaldarius ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770
Substrates: -
Products: -
Products: -
?
4-[(1->4)-alpha-D-glucosyl]n-1-D-glucose
1-alpha-D-[(1->4)-alpha-D-glucosyl]n-1-alpha-D-glucopyranoside
Substrates: -
Products: -
Products: -
?
4-[(1->4)-alpha-D-glucosyl]n-1-D-glucose
1-alpha-D-[(1->4)-alpha-D-glucosyl]n-1-alpha-D-glucopyranoside
Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme converts maltooligosaccharides into maltooligosyltrehalose
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme is involved in the pathway of trehalose synthesis from starch
Products: -
Products: -
?
additional information
?
-
-
Substrates: key enzyme in the synthesis of trehalose
Products: -
Products: -
?
additional information
?
-
Substrates: key enzyme in the synthesis of trehalose
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme is involved in the pathway of trehalose synthesis from starch
Products: -
Products: -
?
additional information
?
-
Substrates: key enzyme in the synthesis of trehalose
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme of trehalose biosynthesis
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
EF433294
134% relative activity at 1 mM, at 50°C in 50 mM phosphate buffer (pH 7.0)
Zn2+
EF433294
122% relative activity at 1 mM, at 50°C in 50 mM phosphate buffer (pH 7.0)
additional information
metal ions are not required for activity. Ca2+, K+, Mg2+, or Na+ have no activating or inhibiting effect on activity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
EDTA
EF433294
31% residual activity at 1 mM, at 50°C in 50 mM phosphate buffer (pH 7.0)
Mg2+
EF433294
66% residual activity at 1 mM, at 50°C in 50 mM phosphate buffer (pH 7.0)
Mn2+
EF433294
51% residual activity at 1 mM, at 50°C in 50 mM phosphate buffer (pH 7.0)
additional information
Ca2+, K+, Mg2+, or Na+ have no activating or inhibiting effect on activity
-
Cu2+
EF433294
54% residual activity at 1 mM, at 50°C in 50 mM phosphate buffer (pH 7.0)
Hg2+
EF433294
42% residual activity at 1 mM, at 50°C in 50 mM phosphate buffer (pH 7.0)
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Dehydration
Molecular Cloning of Maltooligosyltrehalose Trehalohydrolase Gene from Nostoc flagelliforme and Trehalose-Related Response to Stresses.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.24
maltodextrin
pH 6.0, 60°C, mutant enzyme E263G/F284V/F583L/I611T/S615G
3.54
maltodextrin
pH 6.0, 60°C, mutant enzyme G81S/F284V/S615G
1.87
maltohexaose
EF433294
recombinant enzyme, in 50 mM phosphate-citric acid buffer (0.2 M Na3PO4, 0.1 M citric acid, pH 7.0) at 50°C
additional information
additional information
Lineweaver-Burk kinetics
-
additional information
additional information
-
Lineweaver-Burk kinetics
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
216.27
maltodextrin
pH 6.0, 60°C, mutant enzyme G81S/F284V/S615G
228.83
maltodextrin
pH 6.0, 60°C, mutant enzyme E263G/F284V/F583L/I611T/S615G
268.6
maltopentaose
pH 7.0, 45°C, mutant enzyme S316R/S444E/G415P
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
61.09
maltodextrin
pH 6.0, 60°C, mutant enzyme G81S/F284V/S615G
70.62
maltodextrin
pH 6.0, 60°C, mutant enzyme E263G/F284V/F583L/I611T/S615G
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
106.5
purified recombinant enzyme SP3.5, expressed in Pichia pastoris, pH 5.5, 60°C
116.5
purified recombinant enzyme, expressed in Escherichia coli, pH 5.5, 60°C
120
pH and temperature not specified in the publication, mutant enzyme E263G/F284V/F583L/I611T/S615G
additional information
additional information
maximum MTSase activity of crude enzyme expressed in Escherichia coli and Pichia pastoris strains reaches 31.6 and 133.0 U/ml, respectively
additional information
0.51 U/ml and 0.56 U/ml with maltodextrin and maltopentaose as substrates
additional information
-
0.51 U/ml and 0.56 U/ml with maltodextrin and maltopentaose as substrates
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 6
5.5
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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
5.5 - 8
5.5 - 9
pH 5.5: at least 90% of maximal activity, pH 9.0: at least 90% of maximal activity, mutant enzyme E263G/F284V/F583L/I611T/S615G
additional information
both recombinant enzymes retain 80% relative activity after incubation at pH 4.0-7.5 for 24 h at 4°C. The pH stability of SEB24 over 24 h at pH 7.5-10.0 and 4°C is better than that of SP3.5, the relative activity of recombinant SEB24 is higher than that of recombinant SP3.5 from pH 3.5 to pH 5.5
5.5 - 8
pH 5.5: 62% of maximal activity, pH 8.0: 63% of maximal activity, wild-type enzyme
5.5 - 8
-
pH 5.5: about 80% of maximal activity, pH 8.0: about 60% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
60
70
75
40
mutant enzyme G415P, mutant enzyme S361R/S444E and wild-type enzyme
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 45
-
30°C: about 80% of maximal activity, 45°C: about 85% of maximal activity
30 - 55
30°C: about 80% of maximal activity, 55°C: about 55% of maximal activity, wild-type enzyme
45 - 90
45°C: about 60% of maximal activity, 90°C: about 55% of maximal activity
65 - 70
65°C: 98% of maximal activity, 70°C: 93% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
presence of three enzymes for trehalose synthesis: trehalose synthase, maltooligosyltrehalose synthase, and trehalose-6-phosphate synthetase
-
-
brenda
presence of three enzymes for trehalose synthesis: trehalose synthase, maltooligosyltrehalose synthase, and trehalose 6-phosphate synthetase
-
-
brenda
Sulfolobus acidocaldarius ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770
-
UniProt
brenda
Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
i.e. Sulfurisphaera tokodaii
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
8fold increase of enzyme activity in soybean nodules infected with Bradyrhizobium elkanii compared to bacterial culture
brenda
-
10fold increase of enzyme activity in soybean nodules infected with Bradyrhizobium japonicum compared to bacterial culture
brenda
additional information
-
8fold increase of enzyme activity in soybean nodules infected with Bradyrhizobium elkanii compared to bacterial culture
brenda
additional information
-
10fold increase of enzyme activity in soybean nodules infected with Bradyrhizobium japonicum compared to bacterial culture
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
metabolism
key enzyme for the production of trehalose from starch
physiological function
key enzyme in the synthesis of trehalose
physiological function
-
key enzyme in the synthesis of trehalose
-
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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). TREY_MYCTU
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
765
0
82707
Swiss-Prot
-
TREY_MYCTO
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
765
0
82707
Swiss-Prot
-
TREY_ARTSQ
Arthrobacter sp. (strain Q36)
775
0
85356
Swiss-Prot
other Location (Reliability: 4)
Q7LX98_SACS2
Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
732
0
86609
TrEMBL
-
Q973H2_SULTO
Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
704
0
83610
TrEMBL
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
74000
87000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
?
Sulfolobus acidocaldarius ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770
-
x * 74000, recombinant enzyme, SDS-PAGE
-
?
Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
-
x * 83600, recombinant His-tagged enzyme, SDS-PAGE
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method at 16°C, wild-type enzyme and mutant enzyme S44P
hanging-drop vapour-diffusion method at 4°C. The chemical modification of this enzyme by reductive methylation of lysine residues significantly improves the crystal quality for X-ray diffraction experiments. The crystals of the modified enzyme belong to orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 56.70, b = 140.1, c = 205.2 A measured at cryo-temperature, and are found to contain two enzyme molecules per asymmetric unit
-
recombinant enzyme expressed in Escherichia coli, hanging-drop vapour-diffusion method, chemical modification of this enzyme by reductive methylation of lysine residues significantly improves the crystal quality for X-ray diffraction experiments
-
hanging drop vapor diffusion method, using 0.2 M potassium sodium tartrate tetrahydrate, 20% (w/v) polyethylene glycol 3350
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G415P
higher thermal stability than wild-type enzyme. Over the temperature range of 45-60°C, the relative activity of the mutant enzyme is higher than that of the wild-type enzyme. Relative activity of the mutant enzyme is higher than that of the wild-type enzyme at pH 5.5-6.5. The Km-value of the mutant enzyme decreases by 19.7% compared with the wild-type enzyme, while the kcat/Km value is 10.4% higher than that of the wild-type enzyme
S361R/S444E
higher thermal stability than wild-type enzyme. Over the temperature range of 45-60°C, the relative activity of the mutant enzyme is higher than that of the wild-type enzyme. The mutant enzyme is active over a wider pH range (pH 6.0-7.5) than the wild-type enzyme. The Km-value of the mutant enzyme increases by 7.5% compared with the wild-type enzyme, while its kcat/Km is similar to that of the wild-type, indicating that the catalytic efficiency is not affected by the mutations
S361R/S444E/G415P
higher thermal stability than wild-type enzyme. Over the temperature range of 45-60°C, the relative activity of the mutant enzyme is higher than that of the wild-type enzyme. Relative activity of the mutant enzyme is higher than that of the wild-type enzyme at pH 5.5-6.5. The Km-value of the mutant enzyme decreases by 15.1%, compared with the wild-type enzyme, while the kcat/Km value is 30.4% higher than that of the wild-type enzyme
S44P
mutant enzymed shows an increase in kcat/Km by 2.2fold. It exhibits a trehalose yield of 76.9%, which is 6.6% higher than that obtained by wild-type enzym. S44P exhibits increased thermostability compared to wild-type enzyme
up
-
enzyme expression, as well as accumulations of both trehalose and especially sucrose in filaments, are upregulated significantly under dehydration stress, NaCl stress, and high temperature-drought stress
A406
compared with wild-type enzyme, the hydrolysis:transglycosylation selectivity ratio is significantly increased
A406S
the hydrolysis/transglycosylation selectivity ratio shows little change
D411A
D610A
F405S
-
depending on substrate, 29-97% of wild-type transglycosylation efficiency, hydrolytic activity is 16% of wild-type
F405Y
P402
compared with wild-type enzyme, the hydrolysis:transglycosylation selectivity ratio is significantly decreased
P402Q
the hydrolysis/transglycosylation selectivity ratio is significantly decreased
R614A
V426
little change in hydrolysis:transglycosylation selectivity ratio
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
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
-
P402Q
-
the hydrolysis/transglycosylation selectivity ratio is significantly decreased
-
R614A
-
significant reductions in catalytic efficiency and increase in the transition-state energy
-
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
-
V426
-
little change in hydrolysis:transglycosylation selectivity ratio
-
D228N
-
complete loss of both hydrolytic and transglycosylation activity
D231A
-
significant decrease of both hydrolytic and transglycosylation activity
D275A
-
about 50% and 40% decrease of hydrolytic and transglycosylation activity, resp.
D394A
-
significant decrease of both hydrolytic and transglycosylation activity
D443N
-
complete loss of both hydrolytic and transglycosylation activity
E255Q
-
complete loss of both hydrolytic and transglycosylation activity
E263G/F284V/F583L/I611T/S615G
kcat/Km for maltodextrin is 2.33fold higher than wild-type value. When scaled up to a 3 l fermenter, the mutant activity reaches 624.7 U/ml
E393A
-
complete loss of both hydrolytic and transglycosylation activity
G81S/F284V/S615G
kcat/Km for maltodextrin is 2.0fold higher than wild-type value
H229N
-
complete loss of both hydrolytic and transglycosylation activity
K256T
-
significant decrease of both hydrolytic and transglycosylation activity
K390A
-
increase in hydrolytic, decrease in transglycosylation activity
K390E
-
increase in hydrolytic, decrease in transglycosylation activity
K390H
-
increase in hydrolytic, decrease in transglycosylation activity
K390Q
-
increase in hydrolytic, decrease in transglycosylation activity
K390R
-
increase in hydrolytic, decrease in transglycosylation activity
K390T
K390W
-
complete loss of transglycosylation activity, increase in hydrolytic activity
K390W/K445W
-
complete loss of transglycosylation activity, 40% decrease in hydrolytic activity
K445A
-
increase in hydrolytic, decrease in transglycosylation activity
K445E
-
increase in hydrolytic, decrease in transglycosylation activity
K445H
-
increase in hydrolytic, decrease in transglycosylation activity
K445Q
-
increase in hydrolytic, decrease in transglycosylation activity
K445R
-
increase in hydrolytic, decrease in transglycosylation activity
K445T
-
increase in hydrolytic, significant decrease in transglycosylation activity
K445W
-
complete loss of transglycosylation activity, increase in hydrolytic activity
R192A
-
about 50% and 40% decrease of hydrolytic and transglycosylation activity, resp.
R402S
-
about 30% decrease of both hydrolytic and transglycosylation activity
T439A/Q585R
kcat/Km for maltodextrin is 1.5fold higher than wild-type value
Y274S
-
significant decrease of both hydrolytic and transglycosylation activity
Y400S
-
about 25% and 20% decrease of hydrolytic and transglycosylation activity, resp.
additional information
D411A
significant reductions in catalytic efficiency, increase in the transition-state energy
D411A
significant reductions in catalytic efficiency and increase in the transition-state energy
D610A
significant reductions in catalytic efficiency, increase in the transition-state energy
D610A
significant reductions in catalytic efficiency and increase in the transition-state energy
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
R614A
significant reductions in catalytic efficiency, increase in the transition-state energy
R614A
significant reductions in catalytic efficiency and increase in the transition-state energy
K390T
-
increase in hydrolytic, significant decrease in transglycosylation activity
K390T
-
increase in hydrolytic, decrease in transglycosylation activity
additional information
-
overexpression of BvMTSH, a fusion gene for maltooligosyltrehalose synthase and maltooligosyltrehalose trehalohydrolase, enhances drought tolerance in transgenic Oryza sativa without growth inhibition. The transgenic pants show an abscisic acid-hyposensitive phenotype in the roots, phenotype, overview. Construction of the bifunctional in-frame fusion of maltooligosyltrehalose synthase and maltooligosyltrehalose trehalohydrolase from the nonpathogenic bacterium Brevibacterium helvolum under the control of the constitutive rice cytochrome c promoter (101MTSH) or the ABA-inducible Ai promoter (105MTSH). BvMTS converts maltooligosaccharides into maltooligosyltrehalose and BvMTH releases trehalose
additional information
comparative study of maltooligosyltrehalose synthase from Sulfolobus acidocaldarius expressed in Pichia pastoris strain KM71 and Escherichia coli strain BL21(DE3) for enzyme production. Comparison of the effect of different promoters on MTSase expression in Pichia pastoris, two different expression vectors are investigated: pPIC3.5 K, which contains an inducible alcohol oxidase (AOX1) promoter, and pGAPZA, which contains a constitutive glyceraldehyde-3-phosphate dehydrogenase (GAP) promoter. The optimal pH, optimal temperature, pH stability, and temperature stability of MTSase expressed in different hosts are investigated and compared, overview. Both of the recombinant enzymes meet the demands of industrial trehalose production with respect to temperature stability
additional information
Sulfolobus acidocaldarius ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770
-
comparative study of maltooligosyltrehalose synthase from Sulfolobus acidocaldarius expressed in Pichia pastoris strain KM71 and Escherichia coli strain BL21(DE3) for enzyme production. Comparison of the effect of different promoters on MTSase expression in Pichia pastoris, two different expression vectors are investigated: pPIC3.5 K, which contains an inducible alcohol oxidase (AOX1) promoter, and pGAPZA, which contains a constitutive glyceraldehyde-3-phosphate dehydrogenase (GAP) promoter. The optimal pH, optimal temperature, pH stability, and temperature stability of MTSase expressed in different hosts are investigated and compared, overview. Both of the recombinant enzymes meet the demands of industrial trehalose production with respect to temperature stability
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 11
purified recombinant enzyme, 75°C, 10 h, highly stable
3
purified recombinant enzyme, 75°C, 10 h, 65% activity remaining
4
purified recombinant enzyme, 75°C, 10 h, 90% activity remaining
4.5 - 9.5
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
58
10 min, the residual enzyme activities of wild-type enzyme is 43.4%, residual activity of the G415P mutant enzyme is 80.7%, the residual activity of the S361R/S444E mutant enzyme is 83.5%, activity of the S361R/S444E/G415P mutant enzyme is almost unchanged
60
t1/2: 4.6 min, wild-type enzyme. t1/2: 13.7 min, mutant enzyme G415P, t1/2: 14.9 min, mutant enzyme S361R/S444E. t1/2: 90.8 min, mutant enzyme S361R/S444E/G415P
60 - 75
temperature stability of recombinant SEB24 and SP3.5, both of them have a half-life of 12 h at 75°C. The half-lives of SEB24 and SP3.5 at 60°C are 6 d and 6.5 d, respectively. SP3.5 and SEB24 retain 80% and 97% of their original activity after incubation for 2 days at 60°C
70 - 80
-
the MTSH fusion enzyme exhibits a high degree of thermostability, retaining 80% of the activity when pre-incubated at 70°C for 48 h, the stability is gradually abolished by incubating the fusion enzyme at above 80°C for 30 min
75
-
MTS proves stable at 75°C for more than 24 h, with a half life of about 50 h
75 - 85
purified recombinant enzyme, pH 5.0, 10 h, highly stable
80
85
95
95
purified recombinant enzyme, pH 5.0, 8 h, 60% activity remaining
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme 4.6fold from Pichia pastoris strain KM71. and 5.6fold from Escherichia coli strain BL21(DE3), by ammonium sulfate fractionation, dialysis, and anion exchange chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21 CodonPlus(DE3)-RIL by nickel affinity chromatography to homogeneity
Resource ISO column chromatography, Resource Q column chromatography, and Superdex 200 gel filtration
-
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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
expressed in Escherichia coli BL21(DE3)pLysS cells as fusion enzyme with maltooligosyltrehalose trehalohydrolase
-
expression in Escherichia coli
gene mts, DNA and amino acid sequence determination and analysis, expression analysis
-
gene treY, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21 CodonPlus(DE3)-RIL
inserted into an expression vector, pBV220, to yield the recombinant plasmid pSBGT1. MTSase gene in pBSGT1 is expressed in Escherichia coli
-
overexpression in Escherichia coli using the T7-expression system
-
overexpression of enzyme and maltooligosyltrehalose trehalohydrolase alone or with UPD-glucose pyrophosphorylase in a synthetic operon to improve trehalose production in Escherichia coli
-
the gene of maltooligosyltrehalose synthase is amplified by PCR. The primers are designed according to the published sequence of homologous gene from Sulfolobus acidocaldarius ATCC33909. This gene is inserted into the plasmid pBV220 and the resultant recombinant plasmid pBV220-GT is transformed to Escherichia coli DH5 alpha
-
two synthetic genes encoding the MTSase from Sulfolobus acidocaldarius strain ATCC 33909 are synthesized, recombinant expression of codon-optimized enzyme in Pichia pastoris strain KM71 (protein SP3.5) and in Escherichia coli strain BL21(DE3) (protein SEB24), method evaluation and optimization, overview
wild-type and mutant enzymes are expressed in Escherichia coli Rosetta (DE3)
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
industry
key enzyme required for industrial preparation of trehalose
synthesis
synthesis
-
overexpression of the enzyme treY gene and the treY/treZ synthetic operon encoding enzyme and maltooligosyltrehalose trehalohydrolase significantly increases maltooligosyltrehalose synthase activity, the rate-limiting step, and improves the specific productivity and the final titer of trehalose. Furthermore, a strong decrease is noted in glycogen accumulation. Expression of UDP-glucose pyrophosphorylase/maltooligosyltrehalose synthase and UDP-glucose pyrophosphorylase/maltooligosyltrehalose synthase/maltooligosyltrehalose trehalohydrolase synthetic operons shows a partial recovery in the intracellular glycogen levels and a significant improvement in both intra- and extracellular trehalose content
synthesis
-
production of trehalose by enzyme plus maltooligosyltrehalose trehalohydrolase is increased in presence of 4-alpha-glucanotransferase, converting 70% of maltopentaose into trehalose after 6 h, while 60% is converted without 4-alpha-glucanotransferase
synthesis
-
conditions for the production of trehalose from starch by thermostable maltooligosyl trehalose synthase and maltooligosyl trehalose trehalohydrolase from Sulfolubus acidocaldarius ATCC 33909
synthesis
use of the mutant enzyme E263G/F284V/F583L/I611T/S615G with enzymatic activity 3.3fold superior to that of the wild-type activity can significantly lower the cost of trehalose production
synthesis
-
production of trehalose by enzyme plus maltooligosyltrehalose trehalohydrolase is increased in presence of 4-alpha-glucanotransferase, converting 70% of maltopentaose into trehalose after 6 h, while 60% is converted without 4-alpha-glucanotransferase
-
synthesis
-
conditions for the production of trehalose from starch by thermostable maltooligosyl trehalose synthase and maltooligosyl trehalose trehalohydrolase from Sulfolubus acidocaldarius ATCC 33909
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Maruta, K.; Hattori, K.; Nakada, T.; Kubota, M.; Sugimoto, T.; Kurimoto, M.
Cloning and sequencing of trehalose biosynthesis genes from Rhizobium sp. M-11
Biosci. Biotechnol. Biochem.
60
717-720
1996
Rhizobium sp., Rhizobium sp. M-11
brenda
Maruta, K.; Mitsuzumi, H.; Nakada, T.; Kubota, M.; Chaen, H.; Fukuda, S.; Sugimoto, T.; Kurimoto, M.
Cloning and sequencing of a cluster of genes encoding novel enzymes of trehalose biosynthesis from thermophilic archaebacterium Sulfolobus acidocaldarius
Biochim. Biophys. Acta
1291
177-181
1996
Sulfolobus acidocaldarius
brenda
Nakada, T.; Maruta, K.; Tsusaki, K.; Kubota, M.; Chaen, H.; Sugimoto, T.; Kurimoto, M.; Tsujisaka, Y.
Purification and properties of a novel enzyme, maltooligosyl trehalose synthase, from Arthrobacter sp. Q36
Biosci. Biotechnol. Biochem.
59
2210-2214
1995
Arthrobacter sp., Arthrobacter sp. Q36
brenda
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
brenda
Nakada, T.; Ikegami, S.; Chaen, H.; Kubota, M.; Fukuda, S.; Sugimoto, T.; Kurimoto, M.; Tsujisaka, Y.
Purification and characterization of thermostable maltooligosyl trehalose synthase from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius
Biosci. Biotechnol. Biochem.
60
263-266
1996
Sulfolobus acidocaldarius
brenda
Kobayashi, M.; Kubota, M.; Matsuura, Y.
Crystallization and improvement of crystal quality for X-ray diffraction of maltooligosyl trehalose synthase by reductive methylation of lysine residues
Acta Crystallogr. Sect. D
55
931-933
1999
Sulfolobus acidocaldarius
-
brenda
Gueguen, Y.; Rolland, J.L.; Schroeck, S.; Flament, D.; Defretin, S.; Saniez, M.H.; Dietrich, J.
Characterization of the maltooligosyl trehalose synthase from the thermophilic archaeon Sulfolobus acidocaldarius
FEMS Microbiol. Lett.
194
201-206
2001
Sulfolobus acidocaldarius
brenda
Carpinelli, J.; Kraemer, R.; Agosin, E.
Metabolic engineering of Corynebacterium glutamicum for trehalose overproduction: role of the TreYZ trehalose biosynthetic pathway
Appl. Environ. Microbiol.
72
1949-1955
2006
Corynebacterium glutamicum
brenda
Streeter, J.G.; Gomez, M.L.
Three enzymes for trehalose synthesis in Bradyrhizobium cultured bacteria and in bacteroids from soybean nodules
Appl. Environ. Microbiol.
72
4250-4255
2006
Bradyrhizobium japonicum, Bradyrhizobium elkanii
brenda
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
brenda
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
brenda
Maruta, K.; Kubota, M.; Yamashita, H.; Nishimoto, T.; Chaen, H.; Fukuda, S.
Creation of a novel hydrolase by site-directed mutagenesis of malto-oligosyltrehalose synthase
J. Appl. Glycosci.
53
199-203
2006
Sulfolobus acidocaldarius
-
brenda
Seo, J.S.; An, J.H.; Baik, M.Y.; Park, C.S.; Cheong, J.J.; Moon, T.W.; Park, K.H.; Choi, Y.D.; Kim, C.H.
Molecular cloning and characterization of trehalose biosynthesis genes from hyperthermophilic archaebacterium Metallosphaera hakonesis
J. Microbiol. Biotechnol.
17
123-129
2007
Metallosphaera hakonensis
brenda
Lee, J.S.; Hai, T.; Pape, H.; Kim, T.J.; Suh, J.W.
Three trehalose synthetic pathways in the acarbose-producing Actinoplanes sp. SN223/29 and evidence for the TreY role in biosynthesis of component C
Appl. Microbiol. Biotechnol.
80
767-778
2008
Actinoplanes sp., Actinoplanes sp. SN223/29
brenda
Asthana, R.K.; Nigam, S.; Maurya, A.; Kayastha, A.M.; Singh, S.P.
Trehalose-producing enzymes MTSase and MTHase in Anabaena 7120 under NaCl stress
Curr. Microbiol.
56
429-435
2008
Anabaena sp., Anabaena sp. 7120
brenda
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
brenda
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
brenda
Seo, J.S.; An, J.H.; Cheong, J.J.; Choi, Y.D.; Kim, C.H.
Bifunctional recombinant fusion enzyme between maltooligosyltrehalose synthase and maltooligosyltrehalose trehalohydrolase of thermophilic microorganism Metallosphaera hakonensis
J. Microbiol. Biotechnol.
18
1544-1549
2008
Metallosphaera hakonensis, Metallosphaera hakonensis JCM 8857
brenda
Wu, S.; Shen, R.; Zhang, X.; Wang, Q.
Molecular cloning and characterization of maltooligosyltrehalose synthase gene from Nostoc flagelliforme
J. Microbiol. Biotechnol.
20
579-586
2010
Nostoc flagelliforme (EF433294), Nostoc flagelliforme
brenda
Cielo, C.B.; Okazaki, S.; Suzuki, A.; Mizushima, T.; Masui, R.; Kuramitsu, S.; Yamane, T.
Structure of ST0929, a putative glycosyl transferase from Sulfolobus tokodaii
Acta Crystallogr. Sect. F
66
397-400
2010
Sulfurisphaera tokodaii
brenda
Shuangxiu, W.; He, L.; Shen, R.; Zhang, X.; Wang, Q.
Molecular cloning of maltooligosyltrehalose trehalohydrolase gene from Nostoc flagelliforme and trehalose-related response to stresses
J. Microbiol. Biotechnol.
21
830-837
2011
Nostoc flagelliforme
brenda
Wang, H.; Chen, W.; Wu, J.; Jin, C.
Cloning and expression of maltooligosyltrehalose synthase from Sulfolobus acidocaldarius in Escherichia coli
Sheng Wu Gong Cheng Xue Bao
17
339-341
2001
Sulfolobus acidocaldarius, Sulfolobus acidocaldarius ATCC 49426
brenda
Chen, W.; Liu, L.; Sun, P.; Jin, C.
Cloning and expression of the gene encoding maltoologosyl trehalose synthase from Sulfolobus shibatae in E. coli
Wei Sheng Wu Xue Bao
40
57-61
2000
Saccharolobus shibatae
brenda
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
-
brenda
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
-
brenda
Mukai, K.; Tabuchi, A.; Nakada, T.; Shibuya, T.; Chaen, H.; Fukuda, S.; Kurimoto, M.; Tsujisaka, O.;
Production of Trehalose from Starch by Thermostable Enzymes from Sulfolobus acidocaldarius
Starch
49
26-30
1997
Sulfolobus acidocaldarius, Sulfolobus acidocaldarius DSM 639
-
brenda
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
brenda
Fang, T.Y.; Hung, X.G.; Shih, T.Y.; Tseng, W.C.
Characterization of the trehalosyl dextrin-forming enzyme from the thermophilic archaeon Sulfolobus solfataricus ATCC 35092
Extremophiles
8
335-343
2004
Saccharolobus solfataricus (Q7LX98), Saccharolobus solfataricus P2 (Q7LX98)
brenda
Joo, J.; Choi, H.J.; Lee, Y.H.; Lee, S.; Lee, C.H.; Kim, C.H.; Cheong, J.J.; Choi, Y.D.; Song, S.I.
Over-expression of BvMTSH, a fusion gene for maltooligosyltrehalose synthase and maltooligosyltrehalose trehalohydrolase, enhances drought tolerance in transgenic rice
BMB Rep.
47
27-32
2014
Brevibacterium helvolum
brenda
Di Lernia, I.; Morana, A.; Ottombrino, A.; Fusco, S.; Rossi, M.; De Rosa, M.
Enzymes from Sulfolobus shibatae for the production of trehalose and glucose from starch
Extremophiles
2
409-416
1998
Saccharolobus shibatae, Saccharolobus shibatae DMS 5389
brenda
Zhao, M.; Xu, X.; Yang, S.; Liu, T.; Liu, B.
Cloning, expression and characterization of the maltooligosyl trehalose synthase from the archaeon Sulfolobus tokodaii
Pak. J. Pharm. Sci.
31
599-601
2018
Sulfurisphaera tokodaii (Q973H2), Sulfurisphaera tokodaii, Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7 (Q973H2)
brenda
Han, C.; Su, L.; Hong, R.; Wu, S.; Wu, J.
A comparative study of maltooligosyltrehalose synthase from Sulfolobus acidocaldarius expressed in Pichia pastoris and Escherichia coli
Process Biochem.
60
35-41
2017
Sulfolobus acidocaldarius (Q53688), Sulfolobus acidocaldarius ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770 (Q53688)
-
brenda
Chen, C.; Su, L.; Wu, L.; Zhou, J.; Wu, J.
Enhanced the catalytic efficiency and thermostability of maltooligosyltrehalose synthase from Arthrobacter ramosus by directed evolution
Biochem. Eng. J.
162
107724
2020
Arthrobacter ramosus (Q9AJN7)
-
brenda
Chen, C.; Su, L.; Xu, F.; Xia, Y.; Wu, J.
Improved thermostability of maltooligosyltrehalose synthase from Arthrobacter ramosus by directed evolution and site-directed mutagenesis
J. Agric. Food Chem.
67
5587-5595
2019
Arthrobacter ramosus (Q9AJN7)
brenda
Su, L.; Yao, K.; Wu, J.
Improved activity of Sulfolobus acidocaldarius maltooligosyltrehalose synthase through directed evolution
J. Agric. Food Chem.
68
4456-4463
2020
Sulfolobus acidocaldarius (Q53688)
brenda
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