2.4.1.4: amylosucrase
This is an abbreviated version!
For detailed information about amylosucrase, go to the full flat file.
Word Map on EC 2.4.1.4
-
2.4.1.4
-
neisseria
-
polysaccharea
-
deinococcus
-
geothermalis
-
synthesis
-
food industry
-
biotechnology
-
amylose-like
-
transglucosylation
-
waxy
-
drug development
-
turanose
-
asases
-
transglucosidase
-
amylopectin
-
c-myc-binding
-
maltooligosaccharides
-
glycoside-hydrolase
-
trehalulose
-
industry
- 2.4.1.4
- neisseria
- polysaccharea
-
deinococcus
- geothermalis
- synthesis
- food industry
- biotechnology
-
amylose-like
-
transglucosylation
-
waxy
- drug development
- turanose
- asases
- transglucosidase
- amylopectin
-
c-myc-binding
- maltooligosaccharides
-
glycoside-hydrolase
- trehalulose
- industry
Reaction
Synonyms
AaAS, ACAS, AmAS, AMS, Amy-1, ASASE, BtAS, CcAS, DGAS, DRAS, DRpAS, glucosyltransferase, sucrose-1,4-alpha-glucan, MaAS, MFAS, More, NPAS, NsAS, sucrose-glucan glucosyltransferase, SyAS
ECTree
2.4.1.4 amylosucraseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 2.4.1.4 - amylosucrase
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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
sucrose
glucose + maltose + maltotriose + soluble maltooligosaccharides + trehalulose + turanose + insoluble glucan
-
-
9.6% glucose + 9.3% maltose + 11.0% maltotriose + 28.8% soluble maltooligosaccharides + 18.4% trehalulose + 15.1% turanose + 7.8% insoluble glucan
-
?
sucrose
glucose + maltose + maltotriose + turanose + insoluble polymer
enzyme catalyzes both sucrose hydrolysis and oligosaccharide and polymer synthesis in the absence of an activator polymer
with 10 mM sucrose as the sole substrate, 30% glucose, 29% maltose, 18% maltotriose, 11% turanose and 12% insoluble polymer respectively
?
sucrose
maltose + maltotriose + turanose + erlose
compared to the wild-type enzyme, and in agreement with their loss of polymerase activity, all three mutant enzymes incorporate higher amounts of glucosyl units in maltose (27.3% (mutant enzyme R226L/I228V/F229A/A289I/F290Y/E300I/V331T); 24.8% (mutant enzyme R226K/I228V/A289I/F290Y/E300I/V331T/G396S/T398V/Q437R/N439D), 15.3% (mutant enzyme R226K/I228V/A289I/F290Y/E300I/V331T/G396S/T398V/Q437S/N439D/C445R), versus 5.8% for wild-type enzyme) and in maltotriose (20.5% (mutant R226L/I228V/F229A/A289I/F290Y/E300I/V331T); 18.6% (mutant R226K/I228V/A289I/F290Y/E300I/V331T/G396S/T398V/Q437R/N439D), 23% (mutant enzyme R226K/I228V/A289I/F290Y/E300I/V331T/G396S/T398V/Q437S/N439D/C445R), versus 2.9% for wild-type enzyme). Compared to the others, the mutant enzyme R226K/I228V/A289I/F290Y/E300I/V331T/G396S/T398V/Q437S/N439D/C445R is more specialized in turanose production, incorporating nearly 46% of the glucosyl residues in turanose, versus only 19% for the wild-type enzyme. With mutants enzyme R226L/I228V/F229A/A289I/F290Y/E300I/V331T and mutant enzyme R226K/I228V/A289I/F290Y/E300I/V331T/G396S/T398V/Q437R/N439D, 20% and 23% glucosyl units are incorporated into erlose (alpha-D-glucopyranosyl-(1->4)-alpha-D-glucopyranosyl-(1->2)-beta-D-fructose), respectively. Much lower values are observed with mutant enzyme R226K/I228V/A289I/F290Y/E300I/V331T/G396S/T398V/Q437S/N439D/C445R (only 1.4%) and none for the wild-type enzyme. Panose (alpha-D-glucopyranosyl-(1->6)-alpha-D-glucopyranosyl-(1->4)-alpha-D-glucose) is mainly produced by mutants R226K/I228V/A289I/F290Y/E300I/V331T/G396S/T398V/Q437R/N439D and R226K/I228V/A289I/F290Y/E300I/V331T/G396S/T398V/Q437S/N439D/C445R, 13.9% and 8.5% of the glucosyl units incorporated into this trisaccharide, respectively. In comparison, the value goes down to 1.6% with mutant enzyme R226L/I228V/F229A/A289I/F290Y/E300I/V331T and it is not produced by the wild-type enzyme
-
-
?
sucrose + (+)-catechin-3'-O-alpha-D-glucopyranoside
D-fructose + (+)-catechin-3'-O-alpha-D-maltoside
sucrose + (-)-epicatechin-3'-O-alpha-D-glucopyranoside
D-fructose + (-)-epicatechin-3'-O-alpha-D-maltoside
sucrose + aesculetin
D-fructose + aesculetin 7-alpha-D-glucopyranoside
-
-
-
?
sucrose + aesculetin 7-alpha-D-glucopyranoside
D-fructose + aesculetin 7-alpha-D-maltoside
-
-
-
?
sucrose + aesculetin 7-alpha-D-maltoside
D-fructose + aesculetin 7-alpha-D-maltotrioside
-
-
-
?
sucrose + aesculin
D-fructose + aesculin 4-alpha-glucoside
-
-
-
?
sucrose + alpha-D-glucopyranosyl-(1->4)-salicin
D-fructose + alpha-D-glucopyranosyl-(1->4)-alpha-D-glucopyranosyl-(1->4)-salicin
sucrose + amylopectin
?
waxy corn starch selcted as acceptor. The chain length distribution of the elongated waxy corn starchs indicates that all of the branch chains of waxy corn starch are greatly elongated by amylosucrase before occurrence of starch precipitation. Afterwards, however, amylosucrase merely elongates the branch chains whose non-reducing ends are exposed on the surface of the precipitate
-
-
?
sucrose + amylose
D-fructose + [(1->4)-alpha-D-glucosyl]n+1
-
-
-
-
?
sucrose + arbutin
D-fructose + alpha-D-glucopyranosyl-(1,4)-arbutin
-
i.e. 4-hydroxyphenyl beta-glucopyranoside, a glycosylated hydroquinone, maximum yield of bioconversion of arbutin to arbutin-alpha-glucoside are 83.5% and 43.5% at 35°C in donor to acceptor ratios of 1:0.5 and 1:1, respectively
product identification by TLC and NMR analysis, product structure, overview
-
?
sucrose + daidzein diglucoside
D-fructose + daidzein triglucoside
-
-
-
?
sucrose + epicatechin-3'-O-alpha-D-maltoside
D-fructose + (-)-epicatechin-3'-O-alpha-D-maltotrioside
sucrose + glycerol
(2S)-1-O-alpha-D-glucosyl-glycerol + (2R)-1-O-alpha-D-glucosyl-glycerol + 2-O-alpha-D-glucosyl-glycerol
sucrose + glycerol
D-fructose + (2R/S)-1-O-alpha-D-glucosyl-glycerol
-
-
-
?
sucrose + glycerol
D-fructose + 2-O-alpha-D-glucosyl-glycerol
-
-
-
?
sucrose + hydroquinone
D-fructose + hydroquinone-O-alpha-D-glucopyranoside
-
-
-
-
?
sucrose + isoquercitrin
D-fructose + isoquercitrin glucoside
-
-
-
?
sucrose + isoquercitrin diglucoside
D-fructose + isoquercitrin triglucoside
-
-
-
?
sucrose + isoquercitrin glucoside
D-fructose + isoquercitrin diglucoside
-
-
-
?
sucrose + maltopentaose
D-fructose + maltohexaose + maltoheptaose
-
-
-
?
sucrose + phloretin
D-fructose + phloretin glucoside 1 + phloretin glucoside 2 + phloretin glucoside 3
sucrose + phloretin
D-fructose + phloretin glucoside A1 + phloretin glucoside A2 + phloretin glucoside A3
sucrose + phloretin
D-fructose + phloretin-4'-O-alpha-D-glucopyranoside
-
-
-
?
sucrose + phloretin-4'-O-alpha-D-glucopyranoside
D-fructose + phloretin-4'-O-alpha-D-maltoside
-
-
-
?
sucrose + phloretin-4'-O-alpha-D-maltoside
D-fructose + phloretin-4'-O-alpha-D-maltotrioside
-
-
-
?
sucrose + salicin
D-fructose + alpha-D-glucopyranosyl-(1,4)-salicin
-
synthesis of salicin glycosides with sucrose serving as the glucopyranosyl donor and salicin as the acceptor molecule, DGAS specifically synthesizes only one salicin transglycosylation product
product determination by NMR and TLC
-
?
sucrose + salicin
D-fructose + alpha-D-glucopyranosyl-(1,4)-salicin + alpha-D-glucopyranosyl-(1,4)-alpha-D-glucopyranosyl-(1,4)-salicin
synthesis of salicin glycosides with sucrose serving as the glucopyranosyl donor and salicin as the acceptor molecule
i.e. glucosyl salicin and maltosyl salicin, identification by NMR and TLC analysis
-
?
sucrose + vanillin
D-fructose + vanillin 4-alpha-D-glucopyranoside
-
-
-
?
sucrose + zingerone
D-fructose + zingerone 4-alpha-D-glucopyranoside
-
-
-
?
n sucrose
[(1->4)-alpha-D-glucosyl]n + n fructose
additionally to polymerization, ASase catalyzes isomerization and hydrolysis reactions
-
-
?
n sucrose
[(1->4)-alpha-D-glucosyl]n + n fructose
84% polymerization products, additionally ASase catalyzes reactions with 10.2% isomerization products and 5.8% hydrolysis products
-
-
?
n sucrose
[(1->4)-alpha-D-glucosyl]n + n fructose
84% polymerization products, additionally ASase catalyzes reactions with 10.2% isomerization products and 5.8% hydrolysis products
-
-
?
n sucrose
[(1->4)-alpha-D-glucosyl]n + n fructose
45% polymerization products, additionally ASase catalyzes reactions with 8% isomerization products and 71% hydrolysis products
-
-
?
n sucrose
[(1->4)-alpha-D-glucosyl]n + n fructose
45% polymerization products, additionally ASase catalyzes reactions with 8% isomerization products and 71% hydrolysis products
-
-
?
n sucrose
[(1->4)-alpha-D-glucosyl]n + n fructose
56.9% polymerization products, additionally ASase catalyzes reactions with 33.5% isomerization products and 9.6% hydrolysis products
-
-
?
n sucrose
[(1->4)-alpha-D-glucosyl]n + n fructose
56.9% polymerization products, additionally ASase catalyzes reactions with 33.5% isomerization products and 9.6% hydrolysis products
-
-
?
n sucrose
[(1->4)-alpha-D-glucosyl]n + n fructose
-
82.7% polymerization products, additionally ASase catalyzes reactions with 11.5% isomerization products and 5.8% hydrolysis products
-
-
?
n sucrose
[(1->4)-alpha-D-glucosyl]n + n fructose
75.5% polymerization products, additionally ASase catalyzes reactions with 15.0% isomerization products and 9.5% hydrolysis products
-
-
?
n sucrose
[(1->4)-alpha-D-glucosyl]n + n fructose
additionally to polymerization, ASase catalyzes isomerization and hydrolysis reactions
-
-
?
n sucrose
[(1->4)-alpha-D-glucosyl]n + n fructose
Methylotuvimicrobium alcaliphilum DSM 19304
additionally to polymerization, ASase catalyzes isomerization and hydrolysis reactions
-
-
?
n sucrose
[(1->4)-alpha-D-glucosyl]n + n fructose
80.1% polymerization products, additionally ASase catalyzes reactions with 14.5% isomerization products and 5.4% hydrolysis products
-
-
?
n sucrose
[(1->4)-alpha-D-glucosyl]n + n fructose
D3A730
additionally to polymerization, ASase catalyzes isomerization and hydrolysis reactions
-
-
?
n sucrose
[(1->4)-alpha-D-glucosyl]n + n fructose
D3A730
additionally to polymerization, ASase catalyzes isomerization and hydrolysis reactions
-
-
?
n sucrose
[(1->4)-alpha-D-glucosyl]n + n fructose
78.4% polymerization products, additionally ASase catalyzes reactions with 19.7% isomerization products and 1.9% hydrolysis products
-
-
?
n sucrose
[(1->4)-alpha-D-glucosyl]n + n fructose
78.4% polymerization products, additionally ASase catalyzes reactions with 19.7% isomerization products and 1.9% hydrolysis products
-
-
?
n sucrose
[(1->4)-alpha-D-glucosyl]n + n fructose
SMQ77851
additionally to polymerization, ASase catalyzes isomerization and hydrolysis reactions
-
-
?
sucrose
alpha-(1,4) glucan
when the conversion of 100 mM sucrose is catalyzed at 35°C, 45°C, and 55°C for 24 h, the enzyme produces alpha-(1,4) glucans with average degrees of polymerisation of 59, 45, and 37, respectively
-
-
?
sucrose
alpha-(1,4) glucan
when the conversion of 100 mM sucrose is catalyzed at 35°C, 45°C, and 55°C for 24 h, the enzyme produces alpha-(1,4) glucans with average degrees of polymerisation of 59, 45, and 37, respectively
-
-
?
sucrose
alpha-glucan + turanose + trehalulose
transglucosylation activity is significantly higher than the hydrolytic activity. The main product generated from sucrose is structurally determined to be alpha-(1,4)-glucan. A small amount of glucose is produced by hydrolysis, and sucrose isomers including turanose and trehalulose are generated as minor products. The ratio of hydrolytic, polymerization, and isomerization reactions is calculated to be 5.8:84.0:10.2. The enzyme favors production of long-chain insoluble alpha-glucan at lower temperature
-
-
?
sucrose
alpha-glucan + turanose + trehalulose
transglucosylation activity is significantly higher than the hydrolytic activity. The main product generated from sucrose is structurally determined to be alpha-(1,4)-glucan. A small amount of glucose is produced by hydrolysis, and sucrose isomers including turanose and trehalulose are generated as minor products. The ratio of hydrolytic, polymerization, and isomerization reactions is calculated to be 5.8:84.0:10.2. The enzyme favors production of long-chain insoluble alpha-glucan at lower temperature
-
-
?
sucrose
D-fructose + alpha-1,4-glucan
WP_018466847
alpha-1,4-glucan is the predominant product at pH 6.0-8.0 and 30-60°C
-
-
?
sucrose
D-fructose + alpha-1,4-glucan
WP_018466847
alpha-1,4-glucan is the predominant product at pH 6.0-8.0 and 30-60°C
-
-
?
sucrose
turanose + ?
D3A730
the reaction pattern of the enzyme at a sucrose range of 0.1-1.0 M shows that at 0.7 M of sucrose, the production yield of insoluble linearx02alpha-(1,4)-glucans reaches 24% maximum, and any further increase in sucrose results in a slight decrease in yield. The production yield of turanose significantly increases from 16 to 29% by increasing sucrose from 0.1 to 1.0 M. The synthesized glucan has degrees of polymerization for 0.1, 0.4, 0.7,and 1.0 M sucrose, the degree of polymerization values are 77, 49, 39, and 31 respectively
-
-
?
sucrose
turanose + ?
D3A730
the reaction pattern of the enzyme at a sucrose range of 0.1-1.0 M shows that at 0.7 M of sucrose, the production yield of insoluble linearx02alpha-(1,4)-glucans reaches 24% maximum, and any further increase in sucrose results in a slight decrease in yield. The production yield of turanose significantly increases from 16 to 29% by increasing sucrose from 0.1 to 1.0 M. The synthesized glucan has degrees of polymerization for 0.1, 0.4, 0.7,and 1.0 M sucrose, the degree of polymerization values are 77, 49, 39, and 31 respectively
-
-
?
sucrose + (+)-catechin
D-fructose + (+)-catechin-3'-O-alpha-D-glucopyranoside
-
-
-
?
sucrose + (+)-catechin
D-fructose + (+)-catechin-3'-O-alpha-D-glucopyranoside
-
-
-
?
sucrose + (+)-catechin
D-fructose + (+)-catechin-3'-O-alpha-D-glucopyranoside
-
-
-
-
?
sucrose + (+)-catechin-3'-O-alpha-D-glucopyranoside
D-fructose + (+)-catechin-3'-O-alpha-D-maltoside
-
-
-
?
sucrose + (+)-catechin-3'-O-alpha-D-glucopyranoside
D-fructose + (+)-catechin-3'-O-alpha-D-maltoside
-
-
-
?
sucrose + (+)-taxifolin
D-fructose + (+)-taxifolin-4'-O-alpha-D-glucopyranoside
-
-
-
?
sucrose + (+)-taxifolin
D-fructose + (+)-taxifolin-4'-O-alpha-D-glucopyranoside
-
-
-
?
sucrose + (-)-epicatechin
D-fructose + (-)-epicatechin-3'-O-alpha-D-glucopyranoside
-
-
-
?
sucrose + (-)-epicatechin
D-fructose + (-)-epicatechin-3'-O-alpha-D-glucopyranoside
-
-
-
?
sucrose + (-)-epicatechin-3'-O-alpha-D-glucopyranoside
D-fructose + (-)-epicatechin-3'-O-alpha-D-maltoside
-
-
-
?
sucrose + (-)-epicatechin-3'-O-alpha-D-glucopyranoside
D-fructose + (-)-epicatechin-3'-O-alpha-D-maltoside
-
-
-
?
sucrose + (1,4-alpha-D-glucosyl)n
D-fructose + (1,4-alpha-D-glucosyl)n+1
-
absolute requirement for primer
-
?
sucrose + (1,4-alpha-D-glucosyl)n
D-fructose + (1,4-alpha-D-glucosyl)n+1
-
needs glucan from Neisseria sp. as primer molecule
highly branched
?
sucrose + (1,4-alpha-D-glucosyl)n
D-fructose + (1,4-alpha-D-glucosyl)n+1
-
constitutive enzyme
-
?
sucrose + (1,4-alpha-D-glucosyl)n
D-fructose + (1,4-alpha-D-glucosyl)n+1
-
needs glucan from Neisseria sp. as primer molecule
highly branched
?
sucrose + (1,4-alpha-D-glucosyl)n
D-fructose + (1,4-alpha-D-glucosyl)n+1
-
constitutive enzyme
-
?
sucrose + (1,4-alpha-D-glucosyl)n
D-fructose + (1,4-alpha-D-glucosyl)n+1
-
needs glucan from Neisseria sp. as primer molecule
highly branched
?
sucrose + (1,4-alpha-D-glucosyl)n
D-fructose + (1,4-alpha-D-glucosyl)n+1
-
constitutive enzyme
-
?
sucrose + (1,4-alpha-D-glucosyl)n
D-fructose + (1,4-alpha-D-glucosyl)n+1
-
alpha-D-galactopyranosyl-beta-D-fructofuranoside, i.e. galsucrose can replace sucrose, no activity with beta-D-fructofuranosyl-alpha-D-xyloside, i.e. xylsucrose, melibiose and raffinose
-
?
sucrose + (1,4-alpha-D-glucosyl)n
D-fructose + (1,4-alpha-D-glucosyl)n+1
-
transfers glucose to growing alpha-1,4-glucan chains
-
?
sucrose + (1,4-alpha-D-glucosyl)n
D-fructose + (1,4-alpha-D-glucosyl)n+1
-
alpha-D-glucopyranosyl fluoride can replace sucrose
-
?
sucrose + (1,4-alpha-D-glucosyl)n
D-fructose + (1,4-alpha-D-glucosyl)n+1
-
no activity with 3-deoxysucrose and alpha-D-allopyranosyl beta-fructofuranoside
glycogen-like polysaccharide
?
sucrose + (1,4-alpha-D-glucosyl)n
D-fructose + (1,4-alpha-D-glucosyl)n+1
-
needs mussel or sweet corn glycogen, or corn amylopectin as primer molecule, sucrose alone is no substrate, beta-D-galactosylsucrose can replace sucrose
-
?
sucrose + (1,4-alpha-D-glucosyl)n
D-fructose + (1,4-alpha-D-glucosyl)n+1
-
needs glucan from Neisseria sp. as primer molecule
-
?
sucrose + (1,4-alpha-D-glucosyl)n
D-fructose + (1,4-alpha-D-glucosyl)n+1
-
needs glucan from Neisseria sp. as primer molecule
highly branched
?
sucrose + (1,4-alpha-D-glucosyl)n
D-fructose + (1,4-alpha-D-glucosyl)n+1
-
no activity with melezitose
-
?
sucrose + (1,4-alpha-D-glucosyl)n
D-fructose + (1,4-alpha-D-glucosyl)n+1
-
no activity with melezitose
-
?
sucrose + (1,4-alpha-D-glucosyl)n
D-fructose + (1,4-alpha-D-glucosyl)n+1
-
constitutive enzyme
-
?
sucrose + (1,4-alpha-D-glucosyl)n
D-fructose + (1,4-alpha-D-glucosyl)n+1
-
constitutive enzyme
-
?
sucrose + (1,4-alpha-D-glucosyl)n
D-fructose + (1,4-alpha-D-glucosyl)n+1
-
involved in biosynthesis of amylopectin-glycogen type polysaccharide
-
?
sucrose + (1,4-alpha-D-glucosyl)n
D-fructose + (1,4-alpha-D-glucosyl)n+1
-
transfers glucose to growing alpha-1,4-glucan chains
-
?
sucrose + (1,4-alpha-D-glucosyl)n
D-fructose + (1,4-alpha-D-glucosyl)n+1
-
constitutive enzyme
-
?
sucrose + (1,4-alpha-D-glucosyl)n
D-fructose + (1,4-alpha-D-glucosyl)n+1
-
-
recombinant enzyme linearly elongates some branched chains of glycogen to an average degree of polymerization of 75
?
sucrose + (1,4-alpha-D-glucosyl)n
D-fructose + (1,4-alpha-D-glucosyl)n+1
-
-
recombinant enzyme produces glucopolysaccharide mainly composed of alpha-(1-4) glucosidic linkages and a very low degree, i.e. less than 5%, of alpha-(1-6) branched linkages
?
sucrose + (1,4-alpha-D-glucosyl)n
D-fructose + (1,4-alpha-D-glucosyl)n+1
-
amylosucrase initializes polymer formation by releasing, through sucrose hydrolysis, a glucose molecule that is subsequently used as the first acceptor molecule. Maltooligosaccharides of increasing size are produced and successively elongated at their nonreducing ends until they reached a critical size and concentration, causing precipitation
-
-
?
sucrose + (1,4-alpha-D-glucosyl)n
D-fructose + (1,4-alpha-D-glucosyl)n+1
-
glycogen is the best D-glucosyl unit acceptor. Semiprocessive glycogen elongation mechanism can be proposed on the basis of modeling data
-
-
?
sucrose + (1,4-alpha-D-glucosyl)n
D-fructose + (1,4-alpha-D-glucosyl)n+1
-
needs glucan from Neisseria sp. as primer molecule
highly branched
?
sucrose + (1,4-alpha-D-glucosyl)n
D-fructose + (1,4-alpha-D-glucosyl)n+1
-
constitutive enzyme
-
?
sucrose + (1,4-alpha-D-glucosyl)n
D-fructose + (1,4-alpha-D-glucosyl)n+1
-
needs glucan from Neisseria sp. as primer molecule
highly branched
?
sucrose + (1,4-alpha-D-glucosyl)n
D-fructose + (1,4-alpha-D-glucosyl)n+1
-
constitutive enzyme
-
?
sucrose + 4'-hydroxyflavanone
D-fructose + ?
3-OH and 7-OH positions of the mono-hydroxyflavones and -hydroxyflavanones are resistant to transglycosylation by Deinococcus geothermalis amylosucrase, whereas the 6-OH and 4'-OH positions of the mono-hydroxyflavones and mono-hydroxyflavanones exhibit relatively strong transglycosylation reactivities with the glucose donors released from sucrose by amylosucrase from Deinococcus geothermalis. The 6-OH position is considerably more reactive (54fold higher kcat) than the 4'-OH position in both hydroxyflavones and hydroxyflavanones. Further, the transglycosylation reactions with di- and tri-hydroxyflavones and hydroxyflavanones are also investigated and observed to exhibit similar results to those observed for the mono-hydroxyflavones and mono-hydroxyflavanones molecules
-
-
?
sucrose + 4'-hydroxyflavanone
D-fructose + ?
3-OH and 7-OH positions of the mono-hydroxyflavones and -hydroxyflavanones are resistant to transglycosylation by Deinococcus geothermalis amylosucrase, whereas the 6-OH and 4'-OH positions of the mono-hydroxyflavones and mono-hydroxyflavanones exhibit relatively strong transglycosylation reactivities with the glucose donors released from sucrose by amylosucrase from Deinococcus geothermalis. The 6-OH position is considerably more reactive (54fold higher kcat) than the 4'-OH position in both hydroxyflavones and hydroxyflavanones. Further, the transglycosylation reactions with di- and tri-hydroxyflavones and hydroxyflavanones are also investigated and observed to exhibit similar results to those observed for the mono-hydroxyflavones and mono-hydroxyflavanones molecules
-
-
?
sucrose + 6,7-dihydroxyflavone
D-fructose + ?
56% conversion
-
-
?
sucrose + 6,7-dihydroxyflavone
D-fructose + ?
56% conversion
-
-
?
sucrose + 6-hydroxyflavanone
D-fructose + ?
3-OH and 7-OH positions of the mono-hydroxyflavones and -hydroxyflavanones are resistant to transglycosylation by Deinococcus geothermalis amylosucrase, whereas the 6-OH and 4'-OH positions of the mono-hydroxyflavones and -hydroxyflavanones exhibit relatively strong transglycosylation reactivities with the glucose donors released from sucrose by amylosucrase from Deinococcus geothermalis. The 6-OH position is considerably more reactive (54fold higher kcat) than the 4'-OH position in both hydroxyflavones and hydroxyflavanones. Further, the transglycosylation reactions with di- and tri-hydroxyflavones and hydroxyflavanones are also investigated and observed to exhibit similar results to those observed for the mono-hydroxyflavones and mono-hydroxyflavanones molecules
-
-
?
sucrose + 6-hydroxyflavanone
D-fructose + ?
3-OH and 7-OH positions of the mono-hydroxyflavones and -hydroxyflavanones are resistant to transglycosylation by Deinococcus geothermalis amylosucrase, whereas the 6-OH and 4'-OH positions of the mono-hydroxyflavones and -hydroxyflavanones exhibit relatively strong transglycosylation reactivities with the glucose donors released from sucrose by amylosucrase from Deinococcus geothermalis. The 6-OH position is considerably more reactive (54fold higher kcat) than the 4'-OH position in both hydroxyflavones and hydroxyflavanones. Further, the transglycosylation reactions with di- and tri-hydroxyflavones and hydroxyflavanones are also investigated and observed to exhibit similar results to those observed for the mono-hydroxyflavones and mono-hydroxyflavanones molecules
-
-
?
sucrose + aesculin 4-alpha-glucoside
D-fructose + aesculin 4-alpha-maltoside
-
-
-
?
sucrose + aesculin 4-alpha-glucoside
D-fructose + aesculin 4-alpha-maltoside
-
-
-
?
sucrose + alpha-D-glucopyranosyl-(1->4)-salicin
D-fructose + alpha-D-glucopyranosyl-(1->4)-alpha-D-glucopyranosyl-(1->4)-salicin
-
-
-
?
sucrose + alpha-D-glucopyranosyl-(1->4)-salicin
D-fructose + alpha-D-glucopyranosyl-(1->4)-alpha-D-glucopyranosyl-(1->4)-salicin
-
-
-
?
sucrose + alpha-D-glucopyranosyl-(1->4)-salicin
D-fructose + alpha-D-glucopyranosyl-(1->4)-alpha-D-glucopyranosyl-(1->4)-salicin
-
-
-
?
sucrose + apigenin
D-fructose + ?
19.6% conversion
-
-
?
sucrose + arbutin
D-fructose + 4-hydroxyphenyl beta-maltoside
-
-
-
?
sucrose + arbutin
D-fructose + 4-hydroxyphenyl beta-maltoside
-
-
-
?
sucrose + baicalein
D-fructose + ?
59% conversion
-
-
?
sucrose + baicalein
D-fructose + baicalein 6-O-alpha-D-glucopyranoside
-
-
-
?
sucrose + baicalein
D-fructose + baicalein 6-O-alpha-D-glucopyranoside
-
-
-
?
sucrose + catechol
D-fructose + catechol glucoside
-
-
-
?
sucrose + epicatechin-3'-O-alpha-D-maltoside
D-fructose + (-)-epicatechin-3'-O-alpha-D-maltotrioside
-
-
-
?
sucrose + epicatechin-3'-O-alpha-D-maltoside
D-fructose + (-)-epicatechin-3'-O-alpha-D-maltotrioside
-
-
-
?
sucrose + glycerol
(2S)-1-O-alpha-D-glucosyl-glycerol + (2R)-1-O-alpha-D-glucosyl-glycerol + 2-O-alpha-D-glucosyl-glycerol
-
glycerol is transglycosylated by the intermolecular transglycosylation activity of MFAS. The two major products are determined to be (2S)-1-O-alpha-D-glucosyl-glycerol or (2R)-1-O-alpha-D-glucosyl-glycerol, and 2-O-alpha-D-glucosyl-glycerol, in which a glucose molecule is linked to glycerol via an alpha-glycosidic linkage, NMR identification
-
-
?
sucrose + glycerol
(2S)-1-O-alpha-D-glucosyl-glycerol + (2R)-1-O-alpha-D-glucosyl-glycerol + 2-O-alpha-D-glucosyl-glycerol
-
glycerol is transglycosylated by the intermolecular transglycosylation activity of MFAS. The two major products are determined to be (2S)-1-O-alpha-D-glucosyl-glycerol or (2R)-1-O-alpha-D-glucosyl-glycerol, and 2-O-alpha-D-glucosyl-glycerol, in which a glucose molecule is linked to glycerol via an alpha-glycosidic linkage, NMR identification
-
-
?
sucrose + homoorientin
D-fructose + ?
57.0% conversion
-
-
?
sucrose + hydroquinone
D-fructose + alpha-arbutin
-
-
-
?
sucrose + hydroquinone
D-fructose + alpha-arbutin
-
-
-
?
sucrose + hydroquinone
D-fructose + hydroquinone alpha-glucopyranoside
-
-
-
?
sucrose + hydroquinone
D-fructose + hydroquinone alpha-glucopyranoside
-
-
-
?
sucrose + hydroquinone
D-fructose + hydroquinone alpha-glucopyranoside
-
-
-
?
sucrose + hydroquinone
D-fructose + hydroquinone alpha-glucoside
-
-
-
?
sucrose + hydroquinone
D-fructose + hydroquinone alpha-glucoside
-
-
-
?
sucrose + isoquercetin
D-fructose + isoquercitrin-glucoside
isoquercitrin i.e. quercetin-3-O-beta-D-glucoside
-
-
?
sucrose + isoquercetin
D-fructose + isoquercitrin-glucoside
isoquercitrin i.e. quercetin-3-O-beta-D-glucoside
-
-
?
sucrose + isoquercitrin-diglucoside
D-fructose + isoquercitrin-triglucoside
isoquercitrin i.e. quercetin-3-O-beta-D-glucoside
-
-
?
sucrose + isoquercitrin-diglucoside
D-fructose + isoquercitrin-triglucoside
isoquercitrin i.e. quercetin-3-O-beta-D-glucoside
-
-
?
sucrose + isoquercitrin-glucoside
D-fructose + isoquercitrin-diglucoside
isoquercitrin i.e. quercetin-3-O-beta-D-glucoside
-
-
?
sucrose + isoquercitrin-glucoside
D-fructose + isoquercitrin-diglucoside
isoquercitrin i.e. quercetin-3-O-beta-D-glucoside
-
-
?
sucrose + isorhoifolin
D-fructose + isorhoifolin-4'-O-alpha-D-glucopyranoside
1.8% conversion
-
-
?
sucrose + isorhoifolin
D-fructose + isorhoifolin-4'-O-alpha-D-glucopyranoside
1.8% conversion
-
-
?
sucrose + luteolin
D-fructose + luteolin-4'-O-alpha-D-glucopyranoside
-
-
-
?
sucrose + luteolin
D-fructose + luteolin-4'-O-alpha-D-glucopyranoside
86.0% conversion
-
-
?
sucrose + luteolin
D-fructose + luteolin-4'-O-alpha-D-glucopyranoside
-
-
-
?
sucrose + maltose
D-fructose + maltotriose
the enzyme also produces (+)-catechin maltooligosaccharides
-
-
?
sucrose + maltose
D-fructose + maltotriose
the enzyme also produces (+)-catechin maltooligosaccharides
-
-
?
sucrose + phloretin
D-fructose + phloretin glucoside 1 + phloretin glucoside 2 + phloretin glucoside 3
the enzyme catalyzes the stereospecific glucosylation of phloretin at the 4'-position
-
-
?
sucrose + phloretin
D-fructose + phloretin glucoside 1 + phloretin glucoside 2 + phloretin glucoside 3
the enzyme catalyzes the stereospecific glucosylation of phloretin at the 4'-position
-
-
?
sucrose + phloretin
D-fructose + phloretin glucoside A1 + phloretin glucoside A2 + phloretin glucoside A3
the enzyme is a non-Leloir glycosyltransferase that catalyzes the stereospecific glucosylation of phloretin at the 4'-position. Phloretin and its glucosylation derivatives are cytotoic, overview
three major phloretin-dependent sugar-positive products are observed containing one to three Glc residues (Phlo-A1, -A2, -A3), identification by TLC and NMR spectrometry. In all three metabolites the first Glc, GlcA, is linked to the aglycone at C4'
-
?
sucrose + phloretin
D-fructose + phloretin glucoside A1 + phloretin glucoside A2 + phloretin glucoside A3
the enzyme is a non-Leloir glycosyltransferase that catalyzes the stereospecific glucosylation of phloretin at the 4'-position. Phloretin and its glucosylation derivatives are cytotoic, overview
three major phloretin-dependent sugar-positive products are observed containing one to three Glc residues (Phlo-A1, -A2, -A3), identification by TLC and NMR spectrometry. In all three metabolites the first Glc, GlcA, is linked to the aglycone at C4'
-
?
sucrose + piceid
D-fructose + glucosyl-alpha-(1->4)-piceid
-
-
-
?
sucrose + quercetin
D-fructose + isoquercitrin
isoquercitrin i.e. quercetin-3-O-beta-D-glucoside
-
-
?
sucrose + quercetin
D-fructose + isoquercitrin
isoquercitrin i.e. quercetin-3-O-beta-D-glucoside
-
-
?
sucrose + resorcinol
D-fructose + resorcinol glucoside
-
-
-
?
sucrose + resorcinol
D-fructose + resorcinol glucoside
-
-
-
?
sucrose + salicin
D-fructose + alpha-D-glucopyranosyl-(1->4)-salicin
-
-
-
?
sucrose + salicin
D-fructose + alpha-D-glucopyranosyl-(1->4)-salicin
-
-
-
?
sucrose + [(1->4)-alpha-D-glucosyl]n
D-fructose + [(1->4)-alpha-D-glucosyl]n+1
-
-
-
-
?
sucrose + [(1->4)-alpha-D-glucosyl]n
D-fructose + [(1->4)-alpha-D-glucosyl]n+1
-
-
-
?
sucrose + [(1->4)-alpha-D-glucosyl]n
D-fructose + [(1->4)-alpha-D-glucosyl]n+1
a phenolic aglycone compound can also act an acceptor molecule of ASase transglycosylation activity
-
-
?
sucrose + [(1->4)-alpha-D-glucosyl]n
D-fructose + [(1->4)-alpha-D-glucosyl]n+1
-
-
-
?
sucrose + [(1->4)-alpha-D-glucosyl]n
D-fructose + [(1->4)-alpha-D-glucosyl]n+1
a phenolic aglycone compound can also act an acceptor molecule of ASase transglycosylation activity
-
-
?
sucrose + [(1->4)-alpha-D-glucosyl]n
D-fructose + [(1->4)-alpha-D-glucosyl]n+1
-
amylosucrases catalyze the formation of an alpha-1,4-glucosidic linkage by transferring a glucosyl unit from sucrose onto an acceptor alpha-1,4-glucan
-
-
?
sucrose + [(1->4)-alpha-D-glucosyl]n
D-fructose + [(1->4)-alpha-D-glucosyl]n+1
-
the enzyme shows polymerization activity using sucrose as a sole substrate
-
-
?
sucrose + [(1->4)-alpha-D-glucosyl]n
D-fructose + [(1->4)-alpha-D-glucosyl]n+1
-
the enzyme shows polymerization activity using sucrose as a sole substrate
-
-
?
sucrose + [(1->4)-alpha-D-glucosyl]n
D-fructose + [(1->4)-alpha-D-glucosyl]n+1
-
-
-
?
sucrose + [(1->4)-alpha-D-glucosyl]n
D-fructose + [(1->4)-alpha-D-glucosyl]n+1
-
-
-
?
sucrose + [(1->4)-alpha-D-glucosyl]n
D-fructose + [(1->4)-alpha-D-glucosyl]n+1
-
-
-
-
?
sucrose + [(1->4)-alpha-D-glucosyl]n
D-fructose + [(1->4)-alpha-D-glucosyl]n+1
-
-
-
?
sucrose + [(1->4)-alpha-D-glucosyl]n
D-fructose + [(1->4)-alpha-D-glucosyl]n+1
-
-
linear alpha-(1,4)-glucans
-
?
sucrose + [(1->4)-alpha-D-glucosyl]n
D-fructose + [(1->4)-alpha-D-glucosyl]n+1
the enzyme catalyzes the synthesis of alpha-1,4 glucans from sucrose. The product profile is quite polydisperse, ranging from soluble chains called maltooligosaccharides to high-molecular weight insoluble amylose
-
-
?
sucrose + [(1->4)-alpha-D-glucosyl]n
D-fructose + [(1->4)-alpha-D-glucosyl]n+1
mutant enzyme R226K/I228V/A289I/F290Y/E300I/V331T/Q437S/N439D/C445A only produces soluble oligosaccharides as no insoluble high molecular weight amylose is observed
-
-
?
sucrose + [(1->4)-alpha-D-glucosyl]n
D-fructose + [(1->4)-alpha-D-glucosyl]n+1
-
-
-
-
?
sucrose + [(1->4)-alpha-D-glucosyl]n
D-fructose + [(1->4)-alpha-D-glucosyl]n+1
-
-
-
?
additional information
?
-
-
amylosucrase is a transglucosidase that catalyses the synthesis of an amylose-type polymer from sucrose, an abundant agro-resource
-
-
?
additional information
?
-
-
the purified recombinant enzyme produces an alpha-glucan at 50°C, with an average degree of polymerization of 45 and a polymerization yield of 76%
-
-
?
additional information
?
-
-
the enzyme catalyze the synthesis of an alpha-(1,4)-linked glucan polymer from sucrose instead of an expensive activated sugar, such as ADP- or UDP-glucose
-
-
?
additional information
?
-
-
arbutin-alpha-glucoside exhibits inhibitory activities of on mushroom tyrosinase and the melanin production in human melanoma cells
-
-
?
additional information
?
-
-
the hydrolysis reaction is not a rate-limiting step to perform transglycosylation in rDGAS
-
-
?
additional information
?
-
-
enzymatic production of trehalose from sucrose using amylosucrase and maltooligosyltrehalose synthase-trehalohydrolase, overview
-
-
?
additional information
?
-
NMR product analysis, overview
-
-
?
additional information
?
-
-
synthesis of sucrose isomers turanose and trehalulose from sucrose in the presence of fructose by DgAS, turanose binding site structure, overview
-
-
?
additional information
?
-
amylosucrase synthesizes alpha-1,4-glucans using sucrose as a sole substrate
-
-
?
additional information
?
-
-
amylosucrase synthesizes alpha-1,4-glucans using sucrose as a sole substrate
-
-
?
additional information
?
-
luteolin transglucosylation activity in Corynebacterium glutamicum amylosucrase (cDGAS) is 10% higher than that in the Corynebacterium glutamicum enzyme expressed in Escherichia coli (eDGAS)
-
-
-
additional information
?
-
-
luteolin transglucosylation activity in Corynebacterium glutamicum amylosucrase (cDGAS) is 10% higher than that in the Corynebacterium glutamicum enzyme expressed in Escherichia coli (eDGAS)
-
-
-
additional information
?
-
luteolin transglucosylation activity in Corynebacterium glutamicum amylosucrase (cDGAS) is 10% higher than that in the Corynebacterium glutamicum enzyme expressed in Escherichia coli (eDGAS)
-
-
-
additional information
?
-
NMR product analysis, overview
-
-
?
additional information
?
-
-
NMR product analysis, overview
-
-
?
additional information
?
-
-
amylosucrase is a transglucosidase that catalyzes amylose-like polymer synthesis from sucrose substrate
-
-
?
additional information
?
-
-
amylosucrase is a versatile enzyme that carries out 3 different catalytic reactions: 1. hydrolysis of sucrose to release a glucose molecule and a fructose molecule, 2. synthesis of glucose polymers from liberated glucose molecules, and 3. production of the sucrose isomers turanose and isomaltulose through an isomerization reaction. In addition, the enzyme can attach glucose molecules to an atypical substrate, thereby generating unnatural glucan-conjugates. The enzyme produces glucose, fructose, soluble maltooligosaccharide, insoluble glucan, and sucrose isomers (turanose and trehalulose) using only sucrose as a substrate
-
-
?
additional information
?
-
-
the enzyme does not require a nucleotide-activated sugar as a glucosyl-donor
-
-
?
additional information
?
-
-
amylosucrase is a versatile enzyme that carries out 3 different catalytic reactions: 1. hydrolysis of sucrose to release a glucose molecule and a fructose molecule, 2. synthesis of glucose polymers from liberated glucose molecules, and 3. production of the sucrose isomers turanose and isomaltulose through an isomerization reaction. In addition, the enzyme can attach glucose molecules to an atypical substrate, thereby generating unnatural glucan-conjugates. The enzyme produces glucose, fructose, soluble maltooligosaccharide, insoluble glucan, and sucrose isomers (turanose and trehalulose) using only sucrose as a substrate
-
-
?
additional information
?
-
-
the enzyme does not require a nucleotide-activated sugar as a glucosyl-donor
-
-
?
additional information
?
-
-
the purified recombinant enzyme displays a typical amylosucrase activity by the demonstration of multiple activities of hydrolysis, isomerization, and polymerization. The enzyme also shows sucrose hydrolysis activity
-
-
?
additional information
?
-
-
the purified recombinant enzyme displays a typical amylosucrase activity by the demonstration of multiple activities of hydrolysis, isomerization, and polymerization. The enzyme also shows sucrose hydrolysis activity
-
-
?
additional information
?
-
-
the recombinant amylosucrase is used to glucosylate glycogen particles in vitro in the presence of sucrose as the glucosyl donor. The morphology and structure of the resulting insoluble products are shown to strongly depend on the initial sucrose/glycogen weight ratio. For the lower ratio (1.14), all glucose molecules produced from sucrose are transferred onto glycogen, yielding a slight elongation of the external chains and their organization into small crystallites at the surface of the glycogen particles. With a high initial sucrose/glycogen ratio (342), the external glycogen chains are extended by amylosucrase, yielding dendritic nanoparticles with a diameter 4-5 times that of the initial particle
-
-
?
additional information
?
-
the enzyme catalyzes the synthesis of a water-insoluble amylose-like polymer from sucrose, a readily available and low-cost agroresource
-
-
?
additional information
?
-
the enzyme catalyze the synthesis of an alpha-(1,4)-linked glucan polymer from sucrose instead of an expensive activated sugar, such as ADP- or UDP-glucose
-
-
?
additional information
?
-
-
the enzyme catalyze the synthesis of an alpha-(1,4)-linked glucan polymer from sucrose instead of an expensive activated sugar, such as ADP- or UDP-glucose
-
-
?
additional information
?
-
product patterns formed by wild-type enzyme and selected genetic variants in the presence of sucrose as the sole substrate, overview
-
-
?
additional information
?
-
-
synthesis of cycloamyloses from sucrose by dual enzyme treatment via combined reaction of amylosucrase and 4-alpha-glucanotransferase from Synechocystis sp., EC 2.4.1.25, overview
-
-
?
additional information
?
-
synthesis of sucrose isomers turanose and trehalulose from sucrose in the presence of fructose by NpAS, turanose binding site structure, overview
-
-
?
additional information
?
-
-
synthesis of sucrose isomers turanose and trehalulose from sucrose in the presence of fructose by NpAS, turanose binding site structure, overview
-
-
?
additional information
?
-
amylosucrase (AS), a glucosyltransferase from Neiserria polysaccharea, produces an insoluble alpha-1,4-linked glucan polymer by consuming sucrose and releasing fructose. This reaction does not require a-D-glucosyl-nucleotide-diphosphate like ADP- or UDP-glucose, but rather uses the energy generated by splitting sucrose in order to synthesise the glucan polymer
-
-
?
additional information
?
-
-
amylosucrase from Neisseria polysaccharea is a transglucosylase that synthesizes an insoluble amylose-like polymer from sole substrate sucrose, product isolation and analysis, overview
-
-
?
additional information
?
-
amylosucrase synthesizes alpha-1,4-glucans using sucrose as a sole substrate
-
-
?
additional information
?
-
-
amylosucrase synthesizes alpha-1,4-glucans using sucrose as a sole substrate
-
-
?
additional information
?
-
the amylosucrase from Neisseria polysaccharea naturally catalyzes the synthesis of alpha-glucans from the widely available donor sucrose. NpAS is highly specific for its natural substrate and subsite -1 (according to GH nomenclature) plays a major role in the recognition of the sucrose glucosyl moiety through a highly efficient hydrogen bonding interaction network, subsite 21 is responsible for the high affinity for sucrose
-
-
?
additional information
?
-
-
the amylosucrase from Neisseria polysaccharea naturally catalyzes the synthesis of alpha-glucans from the widely available donor sucrose. NpAS is highly specific for its natural substrate and subsite -1 (according to GH nomenclature) plays a major role in the recognition of the sucrose glucosyl moiety through a highly efficient hydrogen bonding interaction network, subsite 21 is responsible for the high affinity for sucrose
-
-
?
additional information
?
-
-
treatment of pre-gelatinized rice and barley starches with amylosucrase from Neisseria polysaccharea for resistant starch production. Analysis of reaction efficiency, resistant starch content, amylopectin branch-chain length distribution, solubility, welling power, pasting viscosity, and thermal transition properties, detailed overview
-
-
?
additional information
?
-
analysis of enzyme substrate specificity, from 11 potential donors harboring selective derivatizations that are experimentally evaluated, only 4-nitrophenyl-alpha-D-glucopyranoside is used by the wild-type enzyme, and this underlines the high specificity of the -1 subsite of enzyme NpAS for glucosyl donor substrates. Acceptor substrate promiscuity is explored by screening 20 hydroxylated molecules, including D- and L-monosaccharides as well as polyols. With the exception of one compound, all are successfully glucosylated, and showig the tremendous plasticity of the +1 subsite of NpAS, which is responsible for acceptor recognition. Acceptor substrates are arabinose, galactose, altrose, fucose, xylose, allose, mannose, D-sorbitol, Darabitol, D-mannitol, xylitol, myo-inositol, and maltitol. Analysis of product structures and enzyme enantiopreference by in silico docking analyses. The enzyme is able to discriminate very similar molecules such as enantiomers. Arabinose and altrose are more efficiently glucosylated by NpAS in their L forms, whereas xylose is better recognized in its D form. Glucosylation of mannose, xylose, and galactose are less discriminant, while the enzyme isstrictly enantiospecific toward D-fucose
-
-
?
additional information
?
-
crystalline structures of waxy corn starch treated with the enzyme, detailed overview. The crystalline structures in the amylosucrase-modified starch are the result of the formation of intermolecular double helices among amylopectins with elongated external chains. The degree of mutual binding by hydrogen bonds between amylopectins is responsible for the amount of crystalline structure. When these bonds are strong and numerous, the chains associate as crystalline structures, resulting in high SDS and/or RS content. The internal structures of AS-modified starch are not significantly different from the control. This is a plausible explanation for the insignificant change in RS content of the AS-modified starches with the varying reaction times
-
-
?
additional information
?
-
hydrolysis of p-nitrophenyl-alpha-D-glucopyranoside is used for activity measurements. Substrate specificities of recombinant wild-type and mutant enzymes, overview
-
-
?
additional information
?
-
-
hydrolysis of p-nitrophenyl-alpha-D-glucopyranoside is used for activity measurements. Substrate specificities of recombinant wild-type and mutant enzymes, overview
-
-
?
additional information
?
-
-
in presence of an activator polymer , in vitro, the enzyme is capable to caalyze the synthesis of an amylose-like polysaccharide composed of only alpha-1,4-linkages using sucrose as the only energy source
-
-
?
additional information
?
-
the enzyme AMS exhibits multiple catalytic activities. Primarily, it can hydrolyze sucrose to glucose and fructose or transfer glucose from sucrose hydrolysis to another glucose or acceptormolecule. As a side reaction, it is also able to catalyze the isomerization of sucrose to turanose or trehalulose
-
-
?
additional information
?
-
-
the enzyme AMS exhibits multiple catalytic activities. Primarily, it can hydrolyze sucrose to glucose and fructose or transfer glucose from sucrose hydrolysis to another glucose or acceptormolecule. As a side reaction, it is also able to catalyze the isomerization of sucrose to turanose or trehalulose
-
-
?
