5.4.99.16: maltose alpha-D-glucosyltransferase
This is an abbreviated version!
For detailed information about maltose alpha-D-glucosyltransferase, go to the full flat file.
Word Map on EC 5.4.99.16
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5.4.99.16
-
methyltransferase
-
endonuclease
-
cap
-
restriction-modification
-
s-adenosyl-l-methionine
-
adomet
-
s-adenosylmethionine
-
nonstructural
-
enase
-
sinefungin
-
flavivirus
-
trehalose-6-phosphate
-
adomet-dependent
-
hpaii
-
dengue
-
coronaviruses
-
sam-binding
-
medicine
-
smrt
-
adohcy
-
nsp1
-
adomet-binding
-
o6-methylguanine
-
n6-methyladenine
-
cytosine-5-methyltransferase
-
guanylyltransferase
-
n6-adenine
-
isoschizomer
-
trehalase
-
photoelectrochemical
-
synthesis
-
cytosine-5
- 5.4.99.16
- methyltransferase
- endonuclease
- cap
-
restriction-modification
- s-adenosyl-l-methionine
- adomet
- s-adenosylmethionine
-
nonstructural
-
enase
- sinefungin
- flavivirus
- trehalose-6-phosphate
-
adomet-dependent
- hpaii
- dengue
- coronaviruses
-
sam-binding
- medicine
- smrt
-
adohcy
- nsp1
-
adomet-binding
- o6-methylguanine
- n6-methyladenine
-
cytosine-5-methyltransferase
-
guanylyltransferase
-
n6-adenine
-
isoschizomer
- trehalase
-
photoelectrochemical
- synthesis
-
cytosine-5
Reaction
Synonyms
57-KDa trehalose synthase (Saccharomyces cerevisiae), Dgeo_0537, DKY63_02445, DOT40_01605, DrTreS, DrTS, DR_2036, FM102_08285, HMPREF9086_3732, Maltose alpha-D-glucosylmutase, Maltose alpha-D-glucosyltransferase, Maltose glucosylmutase, MTase, MtTS, Protein (Saccharomyces cerevisiae clone pMB14 gene CIF reduced), Protein (Saccharomyces cerevisiae gene CIF1 reduced), PTO0069, PTTS, Synthase, trehalose, Synthase, trehalose (Pimelobacter strain R48 clone pBRM8 gene treS precursor reduced), Synthase, trehalose (Saccharomyces cerevisiae gene TPS1 subunit), Synthase, trehalose (Saccharomyces cerevisiae gene TSL1 subunit), Synthase, trehalose (Thermus aquaticus strain ATCC33923 clone pBTM5), TaTS, Tfu_0584, Trehalose synthase, Trehalose synthase (Pimelobacter strain R48 clone pBRM8 gene treS precursor reduced), Trehalose synthetase, TreS, treSB, TSase, Tter_0330, TtTreS, TtTS
ECTree
5.4.99.16 maltose alpha-D-glucosyltransferaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 5.4.99.16 - maltose alpha-D-glucosyltransferase
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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
high-maltose rice syrup
alpha,alpha-trehalose
-
-
the highest alpha,alpha-trehalose yield (54.6%) can be obtained by 3.5 units/maltose (g) of trehalose synthase from the maltose syrup at 50°C for 20-24 h
-
?
starch
alpha,alpha-trehalose
-
substrate of recombinant fusion protein with N-terminal beta-amylase of Clostridium thermofluorogenes and C-terminal trehalose synthase or vice versa. Catalytic efficiency of fusion protein is higher than that of a mixture of individual enzymes
-
-
?
sucrose
D-glucose + D-fructose + [alpha-D-glucopyranosyl-(1,1)-D-fructofuranose]
-
low activity on sucrose
-
-
?
sucrose
trehalulose
-
activity is very low compared to that with maltose
i.e. 1-O-alpha-D-glucopyranosyl-D-fructose
?
alpha,alpha-trehalose
maltose
-
ratio of kcat to Km value is 2.5fold higher for maltose than for trehalose
-
-
r
alpha,alpha-trehalose
maltose
composition of the TtTreS active site is studied through computer calculation and enzyme analysis. The results are consistent with a two-step double-displacement mechanism. The data suggest that glucose rotation, following breakage of the alpha-1,4 glycosidic bond, is a key factor determining the reaction direction and conversion rate. The N246 residue plays an important role in glucose rotation
-
-
r
alpha,alpha-trehalose
maltose
WP_028494267
1.48fold higher catalytic efficiency (kcat/Km) for maltose than for trehalose
-
-
r
maltose
alpha,alpha-trehalose
conversion of trehalose from maltose is 43.62%. At the same time, TreS produces about 23.85% glucose as a by product after 10 h of incubation
-
-
?
maltose
alpha,alpha-trehalose
-
the maximum conversion yield reaches 69% at 25°C after 9 h of reaction
-
-
r
maltose
alpha,alpha-trehalose
-
the maximum conversion yield reaches 69% at 25°C after 9 h of reaction
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
r
maltose
alpha,alpha-trehalose
Deinococcus radiodurans ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422
-
-
-
r
maltose
alpha,alpha-trehalose
Deinococcus radiodurans ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422
-
-
-
r
maltose
alpha,alpha-trehalose
Deinococcus radiodurans ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422
-
-
-
r
maltose
alpha,alpha-trehalose
the enzyme has a 2fold higher catalytic efficiency (kcat/Km) for maltose than for trehalose indicating maltose as the preferred substrate
TreS also has a weak hydrolytic property with D-glucose as the byproduct
-
r
maltose
alpha,alpha-trehalose
an enzymatic intramolecular rearrangement reaction
-
-
r
maltose
alpha,alpha-trehalose
the enzyme has a 2fold higher catalytic efficiency (kcat/Km) for maltose than for trehalose indicating maltose as the preferred substrate
TreS also has a weak hydrolytic property with D-glucose as the byproduct
-
r
maltose
alpha,alpha-trehalose
an enzymatic intramolecular rearrangement reaction
-
-
r
maltose
alpha,alpha-trehalose
bioconversions results in final trehalose levels of 60%. The enzyme produces reduced amounts of the byproduct glucose (15%)
-
-
?
maltose
alpha,alpha-trehalose
two-step, double-displacement mechanism
-
-
r
maltose
alpha,alpha-trehalose
two-step, double-displacement mechanism
-
-
r
maltose
alpha,alpha-trehalose
-
as a byproduct, about 13% glucose is also produced
-
r
maltose
alpha,alpha-trehalose
-
as a byproduct, about 13% glucose is also produced
-
r
maltose
alpha,alpha-trehalose
-
ratio of kcat to Km value is 2.5fold higher for maltose than for trehalose. Maximum conversion rate for maltose into trehalose is independent of substrate concentration and reaches 71% at 20°C
-
-
r
maltose
alpha,alpha-trehalose
-
one-step conversion via intramolecular transglucosylation reaction
-
-
?
maltose
alpha,alpha-trehalose
Picrophilus torridus ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828
-
-
-
r
maltose
alpha,alpha-trehalose
conversion of 59% maltose by the purified recombinant enzyme with about 5.1% D-glucose as by-product
-
-
r
maltose
alpha,alpha-trehalose
Pseudomonas putida ATCC 47054 / DSM 6125 / NCIMB 11950 / KT2440
-
-
-
r
maltose
alpha,alpha-trehalose
Pseudomonas putida ATCC 47054 / DSM 6125 / NCIMB 11950 / KT2440
conversion of 59% maltose by the purified recombinant enzyme with about 5.1% D-glucose as by-product
-
-
r
maltose
alpha,alpha-trehalose
Pseudomonas putida ATCC 47054 / DSM 6125 / NCIMB 11950 / KT2440
-
-
-
r
maltose
alpha,alpha-trehalose
bioconversions results in final trehalose levels of 60%. The enzyme produces reduced amounts of the byproduct glucose (10%)
-
-
?
maltose
alpha,alpha-trehalose
composition of the TtTreS active site is studied through computer calculation and enzyme analysis. The results are consistent with a two-step double-displacement mechanism. The data suggest that glucose rotation, following breakage of the alpha-1,4 glycosidic bond, is a key factor determining the reaction direction and conversion rate. The N246 residue plays an important role in glucose rotation
-
-
r
maltose
alpha,alpha-trehalose
WP_028494267
1.48fold higher catalytic efficiency (kcat/Km) for maltose than for trehalose
-
-
r
maltose
alpha,alpha-trehalose
-
the recombinant enzyme has a 4.1fold higher catalytic efficientcy for maltose than for trehalose
-
-
r
maltose
alpha,alpha-trehalose + D-glucose + maltose
-
-
the product is composed of alpha,alpha-trehalose (48%), D-glucose (20%), maltose (32%)
-
?
maltose
alpha,alpha-trehalose + D-glucose + maltose
-
-
the product is composed of alpha,alpha-trehalose (48%), D-glucose (20%), maltose (32%)
-
?
additional information
?
-
does not use acarbose and glucose as substrates
-
-
?
additional information
?
-
does not use acarbose and glucose as substrates
-
-
?
additional information
?
-
the enzyme yields 59-69% trehalose from 15 mM maltose at 25-35°C in 4-9 h with 14.4-21.7% D-glucose by-product
-
-
?
additional information
?
-
the enzyme yields 59-69% trehalose from 15 mM maltose at 25-35°C in 4-9 h with 14.4-21.7% D-glucose by-product
-
-
?
additional information
?
-
the enzyme yields 56.8-60.4% trehalose from 300 mM maltose at 40°C in 16-24 h with 7.3-8.6% D-glucose by-product
-
-
?
additional information
?
-
Deinococcus geothermalis DSMZ 11300
the enzyme yields 56.8-60.4% trehalose from 300 mM maltose at 40°C in 16-24 h with 7.3-8.6% D-glucose by-product
-
-
?
additional information
?
-
modeling of maltose into the active site, overview
-
-
?
additional information
?
-
-
modeling of maltose into the active site, overview
-
-
?
additional information
?
-
the enzyme yields 58.2% trehalose from 300 mM maltose at 30°C in 24 h with 7.1% D-glucose by-product
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-
?
additional information
?
-
the enzyme yields 58.2% trehalose from 300 mM maltose at 30°C in 24 h with 7.1% D-glucose by-product
-
-
?
additional information
?
-
the enzyme yields 92% trehalose from 800 mM maltose at 5°C in 48 h
-
-
?
additional information
?
-
the enzyme yields 92% trehalose from 800 mM maltose at 5°C in 48 h
-
-
?
additional information
?
-
trehalose synthase catalyzes the reversible conversion of maltose to trehalose. The opening and closing of the active site is probably a rate-limiting protein conformational change
-
-
?
additional information
?
-
-
trehalose synthase catalyzes the reversible conversion of maltose to trehalose. The opening and closing of the active site is probably a rate-limiting protein conformational change
-
-
?
additional information
?
-
Deinococcus radiodurans ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422
trehalose synthase catalyzes the reversible conversion of maltose to trehalose. The opening and closing of the active site is probably a rate-limiting protein conformational change
-
-
?
additional information
?
-
Deinococcus radiodurans ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422
the enzyme yields 58.2% trehalose from 300 mM maltose at 30°C in 24 h with 7.1% D-glucose by-product
-
-
?
additional information
?
-
Deinococcus radiodurans ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422
the enzyme yields 58.2% trehalose from 300 mM maltose at 30°C in 24 h with 7.1% D-glucose by-product
-
-
?
additional information
?
-
Deinococcus radiodurans ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422
the enzyme yields 92% trehalose from 800 mM maltose at 5°C in 48 h
-
-
?
additional information
?
-
Deinococcus radiodurans ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422
the enzyme yields 92% trehalose from 800 mM maltose at 5°C in 48 h
-
-
?
additional information
?
-
the enzyme yields 48% trehalose from 100 mM maltose at 37°C
-
-
?
additional information
?
-
the enzyme yields 48% trehalose from 100 mM maltose at 37°C
-
-
?
additional information
?
-
the enzyme yields 61-64% trehalose from 60 mM maltose at 20-30°C in 24 h with 2.3-4.5% D-glucose by-product
-
-
?
additional information
?
-
-
TreS has also amylase activity by producing trehalose from glycogen or maltoheptaose
-
-
?
additional information
?
-
-
TreS has also amylase activity by producing trehalose from glycogen or maltoheptaose
-
-
?
additional information
?
-
-
the enzyme catalyzes the hydrolytic cleavage of alpha-aryl glucosides as well as alpha-glucosyl fluoride, overview. Reaction of TreS with 5-fluoro-alpha-D-glucosyl fluoride results in the trapping of a covalent glycosyl-enzyme intermediate consistent with TreS being a member of the retaining glycoside hydrolase family 13 enzyme family, thus likely following a two-step, double displacement mechanism. Inability of TreS to incorporate isotope-labeled exogenous glucose into maltose or trehalose, the absence of a secondary deuterium kinetic isotope effect and the general independence of kcat upon leaving group ability both point to a rate-determining conformational change, likely the opening and closing of the enzyme active site
-
-
?
additional information
?
-
trehalose synthase from Mycobacterium smegmatis also possesses an amylase activity, albeit several orders of magnitude lower than its isomerase activity
-
-
?
additional information
?
-
-
trehalose synthase from Mycobacterium smegmatis also possesses an amylase activity, albeit several orders of magnitude lower than its isomerase activity
-
-
?
additional information
?
-
trehalose synthase from Mycobacterium smegmatis also possesses an amylase activity, albeit several orders of magnitude lower than its isomerase activity
-
-
?
additional information
?
-
the enzyme yields 59.5% trehalose from 90 mM maltose at 30°C in 8 h with 13.2% D-glucose by-product
-
-
?
additional information
?
-
the enzyme yields 50-71% trehalose from 150 mM maltose at 20-60°C in 72 h with 3.6-19.2% D-glucose by-product
-
-
?
additional information
?
-
the wild-type and the mutant enzymes show a hydrolytic side activity producing D-glucose from maltose
-
-
?
additional information
?
-
-
the wild-type and the mutant enzymes show a hydrolytic side activity producing D-glucose from maltose
-
-
?
additional information
?
-
Picrophilus torridus ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828
the wild-type and the mutant enzymes show a hydrolytic side activity producing D-glucose from maltose
-
-
?
additional information
?
-
the enzyme yields 50-71% trehalose from 150 mM maltose at 20-60°C in 72 h with 3.6-19.2% D-glucose by-product
-
-
?
additional information
?
-
-
no substrates: glucose, fructose, lactose, sucrose, starch
-
-
?
additional information
?
-
-
TreS interconverts maltose and trehalose by an intramolecular mechanism, and therefore does not require external glucose or any other factors during the enzymatic reaction
-
-
?
additional information
?
-
optimal activity of purified recombinant enzyme at 30% substrate concentration
-
-
?
additional information
?
-
Pseudomonas putida ATCC 47054 / DSM 6125 / NCIMB 11950 / KT2440
optimal activity of purified recombinant enzyme at 30% substrate concentration
-
-
?
additional information
?
-
-
TreS interconverts maltose and trehalose by an intramolecular mechanism, and therefore does not require external glucose or any other factors during the enzymatic reaction
-
-
?
additional information
?
-
the enzyme yields 70% trehalose from 100 mM maltose at 37°C in 12 h with 8.0% D-glucose by-product
-
-
?
additional information
?
-
the enzyme yields 75% trehalose from 580 mM maltose at 15°C in 19 h without D-glucose by-product
-
-
?
additional information
?
-
Pseudomonas stutzeri CJ38
the enzyme yields 75% trehalose from 580 mM maltose at 15°C in 19 h without D-glucose by-product
-
-
?
additional information
?
-
the enzyme yields 67% trehalose from 90 mM maltose at 25°C with 12% D-glucose by-product
-
-
?
additional information
?
-
Rhodococcus opacus ATCC 41021
the enzyme yields 67% trehalose from 90 mM maltose at 25°C with 12% D-glucose by-product
-
-
?
additional information
?
-
the enzyme yields 70% trehalose from 150 mM maltose at 45°C in 10 h
-
-
?
additional information
?
-
the enzyme yields 55-65% trehalose from 440 mM maltose at 25°C in 24 h with 10-15% D-glucose by-product
-
-
?
additional information
?
-
the enzyme yields 55-65% trehalose from 440 mM maltose at 25°C in 24 h with 10-15% D-glucose by-product
-
-
?
additional information
?
-
the enzyme yields 70% trehalose at 35°C with 8% D-glucose by-product
-
-
?
additional information
?
-
the enzyme yields 70% trehalose at 35°C with 8% D-glucose by-product
-
-
?
additional information
?
-
-
improvement of activity by reaction condition optimization for trehalose production, overview. Pressure as a stress condition can significantly increase the activity of intracellular enzyme TSase in Thermus aquaticus
-
-
?
additional information
?
-
Thermus aquaticus SQ-11
-
improvement of activity by reaction condition optimization for trehalose production, overview. Pressure as a stress condition can significantly increase the activity of intracellular enzyme TSase in Thermus aquaticus
-
-
?
additional information
?
-
-
the enzyme yields 74% trehalose from 292 mM maltose at 50°C in 10 h
-
-
?
additional information
?
-
the enzyme yields 74% trehalose from 292 mM maltose at 50°C in 10 h
-
-
?
additional information
?
-
-
the enzyme yields 80% trehalose from 800 mM maltose at 30°C in 48 h
-
-
?
additional information
?
-
the enzyme yields 80% trehalose from 800 mM maltose at 30°C in 48 h
-
-
?
additional information
?
-
the wild-type enzyme retains the glucose moiety in the active site during the reaction to effectively produce trehalose. 13C NMR analysis is performed to identify the glycosidic structure of the purified transfer disaccharide product, where the carbon signals are compared with that of alpha-mannose. Activity analysis by thin-layer chromatography
-
-
?
additional information
?
-
-
the wild-type enzyme retains the glucose moiety in the active site during the reaction to effectively produce trehalose. 13C NMR analysis is performed to identify the glycosidic structure of the purified transfer disaccharide product, where the carbon signals are compared with that of alpha-mannose. Activity analysis by thin-layer chromatography
-
-
?
additional information
?
-
the enzyme yields 80% trehalose from 800 mM maltose at 30°C in 48 h
-
-
?
additional information
?
-
the wild-type enzyme retains the glucose moiety in the active site during the reaction to effectively produce trehalose. 13C NMR analysis is performed to identify the glycosidic structure of the purified transfer disaccharide product, where the carbon signals are compared with that of alpha-mannose. Activity analysis by thin-layer chromatography
-
-
?
