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Enzyme Nomenclature
Information on EC 2.4.1.4 - amylosucrase
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EC Tree
2.4.1.4 amylosucraseIUBMB Comments
The glucansucrases transfer a D-glucosyl residue from sucrose to a glucan chain. They are classified based on the linkage by which they attach the transferred residue. In some cases, in which the enzyme forms more than one linkage type, classification relies on the relative proportion of the linkages that are generated. This enzyme extends the glucan chain by an alpha(1->4) linkage.
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Word Map
- 2.4.1.4
- neisseria
- polysaccharea
-
deinococcus
-
glucosylated
- geothermalis
- synthesis
- biotechnology
- food industry
-
amylose-like
- amylose
- drug development
- turanose
-
waxy
- amylopectin
- asases
-
transglucosylation
- transglucosidase
-
c-myc-binding
- trehalulose
- maltooligosaccharides
-
glycoside-hydrolase
- industry
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AaAS
ACAS
AmAS
AMS
Amy-1
ASASE
BtAS
CcAS
DGAS
DRAS
DRpAS
MaAS
MFAS
NPAS
NsAS
additional information
additional information
-
the enzyme belongs to the glycoside-hydrolase, GH, family 13
additional information
-
the enzyme is a member of family 13 of the glycoside hydrolases
additional information
the enzyme is a glucansucrase from glycoside hydrolase, GH, family 13
additional information
the enzyme is a member of family 13 of the glycoside hydrolases
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sucrose + [(1->4)-alpha-D-glucosyl]n = D-fructose + [(1->4)-alpha-D-glucosyl]n+1
alpha-retaining mechanism via a double-displacement similar to that described for alpha-amylases
-
sucrose + [(1->4)-alpha-D-glucosyl]n = D-fructose + [(1->4)-alpha-D-glucosyl]n+1
DgAS binds the furanoid tautomers of fructose through a weak network of interactions to enable turanose formation. Such topology at subsite +1 is likely favoring other possible fructose binding modes as reported for Neisseria polysaccharea NpAS in agreement with the higher amount of trehalulose formed by DgAS. Residues Glu326 and Asp284 of DgAS are the general acid/base and the nucleophile, respectively, involved in the formation of the beta-glucosyl intermediate occurring in the alpha-retaining mechanism
-
sucrose + [(1->4)-alpha-D-glucosyl]n = D-fructose + [(1->4)-alpha-D-glucosyl]n+1
in Neisseria polysaccharea NpAS key residues force the fructosyl moiety to bind in an open state with the O3' ideally positioned to explain the preferential formation of turanose by NpAS. Residues Glu328 and Asp286 of NpAS are the general acid/base and the nucleophile, respectively, involved in the formation of the beta-glucosyl intermediate occurring in the alpha-retaining mechanism
sucrose + [(1->4)-alpha-D-glucosyl]n = D-fructose + [(1->4)-alpha-D-glucosyl]n+1
the elongation mechanism involves enzyme conformational changes to allow the entry of sucrose to the active site
-
sucrose + [(1->4)-alpha-D-glucosyl]n = D-fructose + [(1->4)-alpha-D-glucosyl]n+1
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
sucrose:(1->4)-alpha-D-glucan 4-alpha-D-glucosyltransferase
The glucansucrases transfer a D-glucosyl residue from sucrose to a glucan chain. They are classified based on the linkage by which they attach the transferred residue. In some cases, in which the enzyme forms more than one linkage type, classification relies on the relative proportion of the linkages that are generated. This enzyme extends the glucan chain by an alpha(1->4) linkage.
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CAS REGISTRY NUMBER
COMMENTARY
9032-11-5
-
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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 + 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
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
additionally to polymerization, ASase catalyzes isomerization and hydrolysis reactions
-
-
?
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
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 + ?
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 + ?
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
D-fructose + (-)-epicatechin-3'-O-alpha-D-maltotrioside
-
-
-
?
sucrose + (-)-epicatechin
D-fructose + (-)-epicatechin-3'-O-alpha-D-maltotrioside
-
-
-
?
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 + 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 glucoside
-
-
-
?
sucrose + hydroquinone
D-fructose + hydroquinone 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 + (+)-catechin-3'-O-alpha-D-maltoside
the enzyme also produces (+)-catechin maltooligosaccharides
-
-
?
sucrose + maltose
D-fructose + (+)-catechin-3'-O-alpha-D-maltoside
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
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
sucrose + phloretin
D-fructose + phloretin glucoside A1 + phloretin glucoside A2 + phloretin glucoside A3
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
-
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
-
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
-
constitutive enzyme
-
?
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
-
constitutive enzyme
-
?
sucrose + (1,4-alpha-D-glucosyl)n
D-fructose + (1,4-alpha-D-glucosyl)n+1
-
constitutive enzyme
-
?
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 + [(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
-
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
-
-
-
?
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
-
-
-
-
?
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 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
?
-
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
?
-
-
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
?
-
-
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 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
?
-
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
?
-
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
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
not inhibited by C-3-modified sucrose derivatives
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
glycogen
-
initial sucrose consumption rate strongly increases with glycogen concentration, at 106 mM sucrose, addition of 30 g/l glycogen increases the initial rate 98fold
additional information
-
the hydroquinone transglycosylation yield is improved by addition of antioxidants
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Carcinoma, Hepatocellular
Glucocorticoid and developmental regulation of amylase mRNAs in mouse liver cells.
Carcinoma, Hepatocellular
Simultaneous expression of salivary and pancreatic amylase genes in cultured mouse hepatoma cells.
Glioma
miR-139 Functions as An Antioncomir to Repress Glioma Progression Through Targeting IGF-1 R, AMY-1, and PGC-1?.
Psychomotor Agitation
Comparative Tolerability of Dopamine D2/3 Receptor Partial Agonists for Schizophrenia.
Sleep Initiation and Maintenance Disorders
Comparative Tolerability of Dopamine D2/3 Receptor Partial Agonists for Schizophrenia.
Tardive Dyskinesia
Comparative Tolerability of Dopamine D2/3 Receptor Partial Agonists for Schizophrenia.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
38.7
sucrose
-
initial sucrose concentration higehr than 20 mM, sucrose hydrolysis
50.2
sucrose
-
initial sucrose concentration higher than 20 mM, sucrose consumption
78.43
sucrose
30°C, pH 7.0, mutant enzyme R226K/I228V/A289I/F290Y/E300I/V331T/G396S/T398V/Q437S/N439D/C445R
128.3
sucrose
30°C, pH 7.0, mutant enzyme R226K/I228V/A289I/F290Y/E300I/V331T/Q437S/N439D/C445A
387
sucrose
-
initial sucrose concentration higher than 20 mM, polymerization
additional information
additional information
classical Michaelis-Menten kinetics in the reactions of sucrose hydrolysis and transglycosylation
-
additional information
sucrose
for initial sucrose concentration of less than 42.3 mM, Km is more than 18 times lower than that of over 42.3 mM of sucrose
additional information
sucrose
-
for initial sucrose concentration of less than 42.3 mM, Km is more than 18 times lower than that of over 42.3 mM of sucrose
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.167
sucrose
-
initial sucrose concentration lower than 20 mM, polymerization
0.333
sucrose
-
initial sucrose concentration lower than 20 mM, sucrose hydrolysis
0.55
sucrose
-
initial sucrose concentration lower than 20 mM, sucrose consumption
0.55
sucrose
-
initial sucrose concentration higher than 20 mM, sucrose hydrolysis
1.28
sucrose
-
initial sucrose concentration higher than 20 mM, sucrose consumption
1.61
sucrose
30°C, pH 7.0, mutant enzyme R226K/I228V/A289I/F290Y/E300I/V331T/Q437S/N439D/C445A
1.88
sucrose
-
initial sucrose concentration higher than 20 mM, polymerization
3.1
sucrose
-
with maltobiose, pH 7.0, 30°C, recombinant wild-type enzyme
4.5
sucrose
30°C, pH 7.0, mutant enzyme R226K/I228V/A289I/F290Y/E300I/V331T/G396S/T398V/Q437S/N439D/C445R
4.8
sucrose
-
with maltotriose, pH 7.0, 30°C, recombinant wild-type enzyme
7.5
sucrose
-
with maltotetraose, pH 7.0, 30°C, recombinant wild-type enzyme
33
sucrose
-
with maltotriose, pH 7.0, 30°C, recombinant mutant R226N
47
sucrose
-
with maltopentaose, pH 7.0, 30°C, recombinant wild-type enzyme
67
sucrose
-
with maltotetraose, pH 7.0, 30°C, recombinant mutant R226N
173
sucrose
-
with maltopentaose, pH 7.0, 30°C, recombinant mutant R226N
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.012
sucrose
30°C, pH 7.0, mutant enzyme R226K/I228V/A289I/F290Y/E300I/V331T/G396S/T398V/Q437R/N439D
0.013
sucrose
30°C, pH 7.0, mutant enzyme R226K/I228V/A289I/F290Y/E300I/V331T/Q437S/N439D/C445A
0.015
sucrose
30°C, pH 7.0, mutant enzyme R226L/I228V/F229A/A289I/F290Y/E300I/V331T
0.058
sucrose
30°C, pH 7.0, mutant enzyme R226K/I228V/A289I/F290Y/E300I/V331T/G396S/T398V/Q437S/N439D/C445R
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.8
-
sucrose hydrolysis, purified recombinant GST-tagged DgAS, pH 7.0, 37°C
5
-
sucrose hydrolysis, purified recombinant detagged DgAS, pH 7.0, 37°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
8.5
7
WP_018466847
total enzyme activity, polymerization activity and hydrolysis activity
7
highest yield with hydroquinone (98% conversion) or resorcinol (43.6% conversion) as substrate
8
highest yield with catechol (60.6% conversion) as substrate
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 7.5
WP_018466847
pH 5.0: about 50% of maximal activity, pH 7.5: about 60% of maximal activity
5 - 8.5
pH 5.0: 65% of maximal activity, pH 8.0: 45% of maximal activity
5.5 - 9.5
6 - 7.5
7 - 8.5
-
60% of maximal activity at pH 7.0, maximal activity at pH 8.5
7.5 - 9
the enzyme exhibits over 96% of its maximum activity at pH 7.5 to pH 9.0
5.5 - 9.5
activity range, wild-type and mutant enzymes, profile overview
5.5 - 9.5
activity range, wild-type and mutant enzymes, profile overview
6 - 7.5
WP_018466847
pH 6.0: about 55% of maximal activity, pH 7.5: about 45% of maximal activity, polymerization activity
6 - 7.5
WP_018466847
pH 6.0: about 60% of maximal activity, pH 7.5: about 50% of maximal activity, total activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
30 - 55
35
37
40
40 - 45
45
50
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 40
20°C: about 60% of maximal activity, 40°C: about 70% of maximal activity
20 - 50
recombinant enzyme, activity range, temperature profile, overview
20 - 57
-
recombinant enzyme, activity range, 80% of maximal activity at 35-45°C, 20% at 50°C, temperature profile, overview
30 - 50
35 - 50
the enzyme exhibits over 80% of its maximum activity between 35°C to 50°C. The relative activity suddenly dropps to 2% at 55°C
40 - 47
40°C: about 95% of maximal activity, 47°C: about 98% of maximal activity
40 - 60
WP_018466847
more than 80% relative activity between 40°C and 60°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
brenda
-
UniProt
brenda
-
UniProt
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
additional information
-
in cells grown with sucrose, probably bound to polymerized product
-
brenda
additional information
-
in cells grown with sucrose, probably bound to polymerized product
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
physiological function
additional information
evolution
-
amylosucrase belongs to the glycoside hydrolase family 13, GH 13
evolution
-
amylosucrase is a kind of glucosyltransferases belonging to the glycoside hydrolase family 13
evolution
-
the enzyme belongs to the glycohydrolase family 13, GH13
evolution
the enzyme belongs to the glycohydrolase family 13, GH13
evolution
amylosucrase from Neisseria polysaccharea is a transglucosidase from the GH13 family of glycoside-hydrolases. Natural molecular evolution has modeled a dense hydrogen bond network at subsite 21 responsible for the specific recognition of sucrose and conversely, it has loosened interactions at the subsite 11 creating a highly promiscuous subsite 11. The residues forming these subsites are considered to be likely involved in the activity as well as the overall stability of the enzyme
evolution
the enzyme belongs to the aglycoside-hydrolase family 13. Genes spsA,sppA, frkA and amsA are grouped in a transcriptional unit that is named Suc cluster
evolution
-
the enzyme belongs to the GH13 family. Amylosucrases adopt a deep pocket topology of about 15 A with the catalytic triad located at the bottom
evolution
-
the enzyme belongs to the glycoside hydrolase family GH13
evolution
-
the enzyme is a glucosyltransferase of the glycoside hydrolase 13 family, that does not require a nucleotide-activated sugar as a glucosyl-donor
evolution
-
the putative MFAS protein shares not only catalytic residues, but also five consensus regions (CR I-V), with other ASases, although the overall protein shows a low level of amino acid sequence homology when compared with known ASases (ACAS, AMAS, DGAS, DRAS, and NPAS), overview
evolution
-
the putative MFAS protein shares not only catalytic residues, but also five consensus regions (CR I-V), with other ASases, although the overall protein shows a low level of amino acid sequence homology when compared with known ASases (ACAS, AMAS, DGAS, DRAS, and NPAS), overview
evolution
Pseudarthrobacter chlorophenolicus A6 / DSM 12829
-
amylosucrase belongs to the glycoside hydrolase family 13, GH 13
evolution
-
the enzyme is a glucosyltransferase of the glycoside hydrolase 13 family, that does not require a nucleotide-activated sugar as a glucosyl-donor
physiological function
-
amylosucrases are sucrose-utilizing alpha-transglucosidases that naturally catalyze the synthesis of alpha-glucans, linked exclusively through alpha-1,4-linkages. Side products and in particular sucrose isomers such as turanose and trehalulose are also produced by these enzymes
physiological function
amylosucrases are sucrose-utilizing alpha-transglucosidases that naturally catalyze the synthesis of alpha-glucans, linked exclusively through alpha-1,4-linkages. Side products and in particular sucrose isomers such as turanose and trehalulose are also produced by these enzymes
additional information
-
dynamics and unfolding properties of the enzyme by the gauss network model and the anisotropic network model, overview
additional information
-
the catalytic domain A of DgAS adopts the typical (alpha/alpha)8-barrel of the GH family 13
additional information
the catalytic domain A of NpAS adopts the typical (alpha/alpha)8-barrel of the GH family 13
additional information
-
the catalytic domain A of NpAS adopts the typical (alpha/alpha)8-barrel of the GH family 13
additional information
-
active site topology and structure coparisons, overview
additional information
-
Arg226, was proposed from molecular modeling studies to play an important role in the formation of the active site topology and in the accessibility of ligands to the catalytic site
additional information
essential role of enzyme subsite -1 for protein fitness and robustness
additional information
-
essential role of enzyme subsite -1 for protein fitness and robustness
additional information
-
ligand binding causes extensive changes in active-site topology
additional information
-
loops 3, 4, and 7 of AS form an active-site pocket and play an important role in transglycosylation activity
additional information
-
loops 3, 4, and 7 of AS form an active-site pocket and play an important role in transglycosylation activity
Show AA Sequence and Transmembrane Helices (331 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70000
71705
-
1 * 72000, SDS-PAGE, 1 * 71705, sequence calculation
72000
72466
x * 72466, sequence calculation, excluding the transit peptide, x * 85000, about, recombinant SBD-fusion enzyme, SDS-PAGE
72822
-
2 * 72000, recombinant His-tagged enzyme, SDS-PAGE, 2 * 72822, sequence calculation
73000
73214
-
x * 73214, sequence calculation, x * 73000, recombinant detagged enzyme, SDS-PAGE
85000
x * 72466, sequence calculation, excluding the transit peptide, x * 85000, about, recombinant SBD-fusion enzyme, SDS-PAGE
72000
-
2 * 72000, recombinant His-tagged enzyme, SDS-PAGE, 2 * 72822, sequence calculation
73000
-
x * 73214, sequence calculation, x * 73000, recombinant detagged enzyme, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
-
three-dimensional structure and dimer interface analysis. The quaternary organization is likely to participate in the enhanced thermal stability of the protein. Structure comparison with the amylosucrase from Neisseria polysaccharea, overview
homotetramer
monomer
additional information
?
-
x * 73214, sequence calculation, x * 73000, recombinant detagged enzyme, SDS-PAGE
?
x * 72466, sequence calculation, excluding the transit peptide, x * 85000, about, recombinant SBD-fusion enzyme, SDS-PAGE
dimer
-
2 * 72000, recombinant His-tagged enzyme, SDS-PAGE, 2 * 72822, sequence calculation
dimer
-
2 * 72000, recombinant His-tagged enzyme, SDS-PAGE, 2 * 72822, sequence calculation
monomer
-
1 * 72000, SDS-PAGE, 1 * 71705, sequence calculation
monomer
Pseudarthrobacter chlorophenolicus A6 / DSM 12829
-
1 * 72000, SDS-PAGE, 1 * 71705, sequence calculation
additional information
the active pocket in the enzyme is surrounded by A, B, and B' domains. The A domain serves as a catalytic domain and has the typical (beta/alpha)8-barrel structure of the GH13 family. The B' domain includes oligosaccharide binding sites, and both the B and B' domains of the enzyme contain acceptor subsites (+2, +3, +4, +5, and +6)
additional information
-
the active pocket in the enzyme is surrounded by A, B, and B' domains. The A domain serves as a catalytic domain and has the typical (beta/alpha)8-barrel structure of the GH13 family. The B' domain includes oligosaccharide binding sites, and both the B and B' domains of the enzyme contain acceptor subsites (+2, +3, +4, +5, and +6)
additional information
-
the putative enzyme interface is primarily mediated by two regions from domain N, residues Thr22, Leu25, Arg26, Arg29 and Tyr30 and residues Glu73, Leu76 and Leu77, which are involved in hydrophobic interactions with the corresponding residues from the second protomer
additional information
three-dimensional structure analysis. Structure comparison with the amylosucrase from Deinococcus geothermalis, overview
additional information
-
three-dimensional structure analysis. Structure comparison with the amylosucrase from Deinococcus geothermalis, overview
additional information
-
amylosucrases adopt a deep pocket topology of about 15 A with the catalytic triad located at the bottom
additional information
the active pocket in the enzyme is surrounded by A, B, and B' domains. The A domain serves as a catalytic domain andhas the typical (beta/alpha)8-barrel structure of the GH13 family. The B' domain includes oligosaccharide binding sites, and both the B and B' domains of the enzyme contain acceptor subsites (+2, +3, +4, +5, and +6)
additional information
-
the active pocket in the enzyme is surrounded by A, B, and B' domains. The A domain serves as a catalytic domain andhas the typical (beta/alpha)8-barrel structure of the GH13 family. The B' domain includes oligosaccharide binding sites, and both the B and B' domains of the enzyme contain acceptor subsites (+2, +3, +4, +5, and +6)
additional information
the residues forming subsites -1 and +1 are considered to be likely involved in the activity as well as the overall stability of the enzyme, active site structure, overview
additional information
-
the residues forming subsites -1 and +1 are considered to be likely involved in the activity as well as the overall stability of the enzyme, active site structure, overview
additional information
-
structure homology modeling based on the crystal structures of Neisseria poylsaccharea and Deinococcus geothermalis, structural differences and dynamics. The enzyme from Arthrobacter chlorophenolicus can be divided into two regions of different moving directions, predicted unfolding pathway, overview
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant detagged DgAS, free and in complex with turanose, hanging drop vapor diffusion method, X-ray diffraction structure determination and analysis at 1.97-2.10 A resolution
-
purified wild-type and mutant ligand-free enzyme, hanging drop vapour diffusion method, mixing of 0.0025 ml of 3.3 mg/ml protein in 50 mM HEPES, pH 7.0, 150 mM NaCl, 1 mM EDTA, and 1 mM DTT, with 0.0025 ml of reservoir solution containing 1 M sodium acetate, 0.1 M imidazole, 0.1 M LiCl, pH 6.5, 4°C, X-ray diffraction structure determination and analysis at 3.15 A resolution, modeling
-
cocrystallization of E328Q mutant enzyme with maltoheptaose, X-ray structure at 2.2 A resolution
crystal structure of the acid/base catalyst mutant, E328Q, with a covalently bound glucopyranosyl moiety. The structure is refined to a resolution of 2.2 A and shows that binding of the covalent intermediate results in a backbone movement of 1 A around the location of the nucleophile, Asp286
-
crystal structure of wild-type amylosucrase in complex with beta-D-glucose at 1.66 A, crystal structure of E328Q mutant enzyme in complex with sucrose at 2.0 A resolution
-
purified recombinant detagged NpAS in complex with turanose, hanging drop vapor diffusion method, 1:1 v/v ratio of protein, containing 6 mg/ml in 20 mM Tris, pH 8.0, to precipitant solution containing 1.5 M sodium acetate, 0.1 M sodium cacodylate, pH 7.0, 2 weeks, X-ray diffraction structure determination and analysis at 1.85 A resolution
recombinant enzyme, equal amounts of 4 mg/ml enzyme in 150 mM NaCl, 50 mM Tris-HCl, pH 7.0, 1 mM EDTA and 1 mM dithiothreitol and reservoir solution consisting of 30% polyethylene glycol 6000 and 100 mM HEPES, pH 7.0, crystal structure at 1.4 A resolution
the mutant enzyme R226K/I228V/A289I/F290Y/E300I/V331T/Q437S/N439D/C445A is crystallized by hanging drop vapor diffusion method at 12°C
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A170V/Q353L
-
random mutagenesis, the mutant shows 3.5fold increased thermostabilty at 50°C compared to the wild-type enzyme
P351S
-
random mutagenesis, the mutant shows 8fold increased thermostabilty at 50°C compared to the wild-type enzyme
R20C/A451T
-
random mutagenesis, the mutant shows 10fold increased thermostabilty at 50°C compared to the wild-type enzyme
D394A
-
23.5% of the wild-type activity, according to the initial rate of sucrose consumption, very poor ativation by glycogen
E227G
mutant enzyme is a highly efficient polymerase that produces a longer polymer than the wild-type enzyme. Decreased stability and the temperature optimum compared to wild-type enzyme
E328Q
N387D
60% increase in activity compared to wild-type enzyme, increased stability at 50°C
R226A
-
activated by the products it forms. The mutant yields twice as much insoluble glucan as the wild-type enzyme and leads to the production of lower quantities of by-products, mutant enzyme is strongly activated by glycogen
R226K/I228V/A289I/F290Y/E300I/V331T/G396S/T398V/Q437R/N439D
compared to the wild-type enzyme, and in agreement with the loss of polymerase activity, the mutant enzyme incorporates higher amounts of glucosyl units in maltose (24.8% versus 5.8% for wild-type enzyme) and in maltotriose (18.6% versus 2.9% for wild-type enzyme). The mutant enzyme incorporates 23% glucosyl units into erlose (alpha-D-glucopyranosyl-(1->4)-alpha-D-glucopyranosyl-(1->2)-beta-D-fructose). No glucosyl units are incorporated into erlose (alpha-D-glucopyranosyl-(1->4)-alpha-D-glucopyranosyl-(1->2)-beta-D-fructose)by the wild-type enzyme. Panose (alpha-D-glucopyranosyl-(1->6)-alpha-D-glucopyranosyl-(1->4)-alpha-D-glucose) is produced by the mutant enzyme, 13.9% of the glucosyl units are incorporated into this trisaccharide. No panose is produced by the wild-type enzyme. The Tm-value is slightly lowered compared to wild-type enzyme (-3°C)
R226K/I228V/A289I/F290Y/E300I/V331T/G396S/T398V/Q437S/N439D/C445R
compared to the wild-type enzyme, and in agreement with the loss of polymerase activity, the mutant enzyme incorporates higher amounts of glucosyl units in maltose (15.3% versus 5.8% for wild-type enzyme) and in maltotriose (23% versus 2.9% for wild-type enzyme). The mutant enzyme incorporates nearly 46% of the glucosyl residues in turanose, versus only 19% for the wild-type enzyme. Panose (alpha-D-glucopyranosyl-(1->6)-alpha-D-glucopyranosyl-(1->4)-alpha-D-glucose) is produced by the mutant enzyme, 8.5% of the glucosyl units are incorporated into this trisaccharide. No panose is produced by the wild-type enzyme. The Tm-value is slightly lowered compared to wild-type enzyme (-1.9°C)
R226K/I228V/A289I/F290Y/E300I/V331T/Q437S/N439D/C445A
mutant enzyme that shows a 6fold enhanced activity toward sucrose compared to the wild-type enzyme. Only soluble maltooligosaccharide products of controlled size chains (2 < DP < 21) with a narrow polydispersity are observed. This variant, containing 9 mutations in the active site, is characterized at both biochemical and structural levels. Its X-ray structure is determined and further investigated by molecular dynamics to understand the molecular origins of its higher activity on sucrose and higher production of small maltooligosaccharides, with a totally abolished insoluble glucan synthesis
R226L/I228V/F229A/A289I/F290Y/E300I/V331T
compared to the wild-type enzyme, and in agreement with the loss of polymerase activity, the mutant enzyme incorporates higher amounts of glucosyl units in maltose (27.3% versus 5.8% for wild-type enzyme) and in maltotriose (20.5% versus 2.9% for wild-type enzyme). With the mutant enzyme 20% glucosyl units are incorporated into erlose (alpha-D-glucopyranosyl-(1->4)-alpha-D-glucopyranosyl-(1->2)-beta-D-fructose). No glucosyl units are incorporated into erlose by the wild-type enzyme. 1.6% panose is produced by the mutants enzyme and it is not produced by the wild-type enzyme. The Tm-value is slightly lowered compared to wild-type enzyme (-3°C)
R226N
-
site-directed mutagenesis, compared to the wild-type enzyme, the mutant shows a 10fold enhancement in the catalytic efficiency and a nearly twofold higher production of an insoluble amylose-like polymer
R226X
-
site-directed mutagenesis, the single site mutants, except R226N, show reduced activity compare to the wild-type enzyme
R415A
-
4.3% of the activity compared with the wild-type enzyme. No synthesis of any insoluble modified glycogen
R446A
synthesis
-
potential use for the synthesis or the modification of polysaccharides is limited by its low catalytic efficiency on sucrose alone, its low stability, and its side reactions resulting in sucrose isomer formation. Development of a zero background expression cloning strategy for the generation of large variant libraries, a selection mechanism to discard inactive variants, and a screening method for identification of interesting clones
additional information
E328Q
inactive mutant, sucrose binding structure analysis using the crystal structure, PDB ID 1JGI
R446A
-
15% of the wild-type activity, according to the initial rate of sucrose consumption, no synthesis of any insoluble modified glycogen
additional information
construction of chimeric enzymes using gene dgas and gene npas from Neisseria polysaccharea by overlap extension polymerase chain reaction, the mutants show altered polymerization activity and thermostability. Three-dimensional modeling structure and molecular dynamics of mutant DGAS-B, quaternary structure
additional information
-
construction of chimeric enzymes using gene dgas and gene npas from Neisseria polysaccharea by overlap extension polymerase chain reaction, the mutants show altered polymerization activity and thermostability. Three-dimensional modeling structure and molecular dynamics of mutant DGAS-B, quaternary structure
additional information
-
random mutagenesis and screening for enzyme variants with increased thermostability, molecular dynamics simulations, overview
additional information
random mutagenesis, high-throughput screening and isolation of amylosucrase variants displaying higher thermostability or increased resistance to organic solvents, overview
additional information
generation of amylosucrase variants that terminate catalysis of acceptor elongation at the di- or trisaccharide stage, product patterns formed by wild-type enzyme and selected genetic variants in the presence of sucrose as the sole substrate, overview
additional information
-
non-covalent immobilization of the recombinant enzyme for use as biocatalyst, about 87% of enzyme activity and 96% of protein are recovered after immobilization, repeated catalysis with acceptable stability, significantly improved thermostability at 40°C compared to the native enzyme, and unaltered temperature and pH profiles, overview
additional information
amylosucrase from Neisseria polysaccharea is fused to a starch-binding domain (SBD) of cyclodextrin glycosyltransferase from Bacillus circulans, expression of the amylosucrase-SBD and SBD-amylosucrase fusion proteins in the amylose-containing (cv. Kardal) and amylose-free (amf) Solanum tuberosum plants, respectively. Expression of SBD-amylosucrase fusion protein in the amylose-containing potato results in starch granules with a rough surface, a twofold increase in median granule size, and altered physico-chemical properties including improved freeze-thaw stability, higher end viscosity, and better enzymatic digestibility. These effects are possibly a result of the physical interaction between amylosucrase and starch granules
additional information
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amylosucrase from Neisseria polysaccharea is fused to a starch-binding domain (SBD) of cyclodextrin glycosyltransferase from Bacillus circulans, expression of the amylosucrase-SBD and SBD-amylosucrase fusion proteins in the amylose-containing (cv. Kardal) and amylose-free (amf) Solanum tuberosum plants, respectively. Expression of SBD-amylosucrase fusion protein in the amylose-containing potato results in starch granules with a rough surface, a twofold increase in median granule size, and altered physico-chemical properties including improved freeze-thaw stability, higher end viscosity, and better enzymatic digestibility. These effects are possibly a result of the physical interaction between amylosucrase and starch granules
additional information
construction of chimeric enzymes using gene dgas and gene npas from Deinococcus geothermalis by overlap extension polymerase chain reaction, the mutants show altered polymerization activity and thermostability
additional information
-
construction of chimeric enzymes using gene dgas and gene npas from Deinococcus geothermalis by overlap extension polymerase chain reaction, the mutants show altered polymerization activity and thermostability
additional information
introduction of mutations at D144, Y147, F250, R284, and R509 positions leads to equivalent or impaired stability compared with the wild-type enzyme. Several mutant variants retain their transglucosylation activity and are still able to catalyze the synthesis of maltooligosaccharides. In particular, two mutants H392P and Y147F display original and controlled product distributions compared to the wild-type parental NpAS being more efficient for synthesizing soluble oligosaccharides. Two H187 variants and nine H392 variants show lower free energy values than that calculated for the wild-type enzyme
additional information
-
introduction of mutations at D144, Y147, F250, R284, and R509 positions leads to equivalent or impaired stability compared with the wild-type enzyme. Several mutant variants retain their transglucosylation activity and are still able to catalyze the synthesis of maltooligosaccharides. In particular, two mutants H392P and Y147F display original and controlled product distributions compared to the wild-type parental NpAS being more efficient for synthesizing soluble oligosaccharides. Two H187 variants and nine H392 variants show lower free energy values than that calculated for the wild-type enzyme
additional information
-
non-covalent immobilization of the recombinant enzyme for use as biocatalyst, about 87% of enzyme activity and 96% of protein are recovered after immobilization, repeated catalysis with acceptable stability, significantly improved thermostability at 40°C compared to the native enzyme, and unaltered temperature and pH profiles, overview
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
40
40 - 50
-
half-life of the enzyme is 421.4 h at 40°C and 3.3 h at 45°C, the thermostability of DRpAS dramatically decreases at 50°C, Tm value is 50.7°C and the half-life of the enzyme is 7.2 min at 50°C
43.2 - 51.5
the half-lives of mutant NPAS-B' and wild-type NPAS are 4.28 and 9.99 min at 45°C and their melting temperatures are 43.25°C and 51.52°C, respectively
45
46
46.1
Tm-value, mutant enzyme R226K/I228V/A289I/F290Y/E300I/V331T/Q437S/N439D/C445A
47.1
Tm-value, mutant enzyme R226K/I228V/A289I/F290Y/E300I/V331T/G396S/T398V/Q437S/N439D/C445R
49
50
50 - 62
half-lives of mutant DGAS-B are 30.70 and 3.39 min at 50°C and 55°C, respectively, whereas that of the wild-type DGAS is 65.74 min at 55°C. The melting temperatures of mutant DGAS-B and wild-type DGAS are 54.23°C and 61.42°C, respectively
50.7
55
60
65
additional information
30
high stability, maintaining 83% activity after 2 h
40
retains more than 90% of its initial activity after incubation for 58 h
40
-
the purified recombinant His-tagged ACAS is stable up to 40°C, but rapid loss of activity above, half-life is 1.74 h
45
loses more than 50% of its initial activity after incubation for 1 h
46
Tm-value, mutant enzyme R226K/I228V/A289I/F290Y/E300I/V331T/G396S/T398V/Q437R/N439D
46
Tm-value, mutant enzyme R226L/I228V/F229A/A289I/F290Y/E300I/V331T
50
loses more than 50% of its initial activity after incubation for 5 min
50
-
purified recombinant enzyme, half-life is 26 h, denaturation kinetics, overview
50
-
half-life of the recombinant wild-type enzyme is 3 min, and of mutant R20C/A451T 32 min, of mutant A170V/Q353L 10 min, and of mutant P351S 24 min
50
complete loss of catalytic activity after 30 min