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Information on EC 2.4.1.4 - amylosucrase
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2.4.1.4 amylosucraseSpecify your search results
Word Map
- 2.4.1.4
- neisseria
- polysaccharea
-
glucosylate
-
deinococcus
- geothermalis
- glucans
-
amylose-like
- asase
- amylose
- transglucosidase
-
waxy
- turanose
- maltooligosaccharides
-
transglucosylation
- amylopectin
-
glycoside-hydrolase
- synthesis
- biotechnology
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
drpas, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ACAS
AMS
ASASE
DGAS
DRpAS
glucosyltransferase, sucrose-1,4-alpha-glucan
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-
-
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MFAS
NPAS
sucrose-glucan glucosyltransferase
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-
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-
additional information
additional information
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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 member of family 13 of the glycoside hydrolases
additional information
the enzyme is a glucansucrase from glycoside hydrolase, GH, family 13
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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
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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
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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
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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
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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
hexosyl group transfer
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-
-
-
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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
-
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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
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-
9.6% glucose + 9.3% maltose + 11.0% maltotriose + 28.8% soluble maltooligosaccharides + 18.4% trehalulose + 15.1% turanose + 7.8% insoluble glucan
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?
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 + amylose
D-fructose + [(1->4)-alpha-D-glucosyl]n+1
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-
-
-
?
sucrose + arbutin
D-fructose + alpha-D-glucopyranosyl-(1,4)-arbutin
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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 + glycerol
(2S)-1-O-alpha-D-glucosyl-glycerol + (2R)-1-O-alpha-D-glucosyl-glycerol + 2-O-alpha-D-glucosyl-glycerol
sucrose + hydroquinone
D-fructose + hydroquinone-O-alpha-D-glucopyranoside
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-
-
-
?
sucrose + maltopentaose
D-fructose + maltohexaose + maltoheptaose
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-
-
?
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 + 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
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?
sucrose + salicin
D-fructose + alpha-D-glucopyranosyl-(1,4)-salicin + alpha-D-glucopyranosyl-(1,4)-alpha-D-glucopyranosyl-(1,4)-salicin
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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
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?
sucrose + (+)-catechin
D-fructose + (+)-catechin-3'-O-alpha-D-glucopyranoside
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-
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?
sucrose + (+)-catechin
D-fructose + (+)-catechin-3'-O-alpha-D-glucopyranoside
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?
sucrose + (1,4-alpha-D-glucosyl)n
D-fructose + (1,4-alpha-D-glucosyl)n+1
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absolute requirement for primer
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?
sucrose + (1,4-alpha-D-glucosyl)n
D-fructose + (1,4-alpha-D-glucosyl)n+1
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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
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constitutive enzyme
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?
sucrose + (1,4-alpha-D-glucosyl)n
D-fructose + (1,4-alpha-D-glucosyl)n+1
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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
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constitutive enzyme
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?
sucrose + (1,4-alpha-D-glucosyl)n
D-fructose + (1,4-alpha-D-glucosyl)n+1
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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
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constitutive enzyme
-
?
sucrose + (1,4-alpha-D-glucosyl)n
D-fructose + (1,4-alpha-D-glucosyl)n+1
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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
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?
sucrose + (1,4-alpha-D-glucosyl)n
D-fructose + (1,4-alpha-D-glucosyl)n+1
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transfers glucose to growing alpha-1,4-glucan chains
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?
sucrose + (1,4-alpha-D-glucosyl)n
D-fructose + (1,4-alpha-D-glucosyl)n+1
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alpha-D-glucopyranosyl fluoride can replace sucrose
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?
sucrose + (1,4-alpha-D-glucosyl)n
D-fructose + (1,4-alpha-D-glucosyl)n+1
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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
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needs mussel or sweet corn glycogen, or corn amylopectin as primer molecule, sucrose alone is no substrate, beta-D-galactosylsucrose can replace sucrose
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?
sucrose + (1,4-alpha-D-glucosyl)n
D-fructose + (1,4-alpha-D-glucosyl)n+1
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needs glucan from Neisseria sp. as primer molecule
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?
sucrose + (1,4-alpha-D-glucosyl)n
D-fructose + (1,4-alpha-D-glucosyl)n+1
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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
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no activity with melezitose
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?
sucrose + (1,4-alpha-D-glucosyl)n
D-fructose + (1,4-alpha-D-glucosyl)n+1
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no activity with melezitose
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?
sucrose + (1,4-alpha-D-glucosyl)n
D-fructose + (1,4-alpha-D-glucosyl)n+1
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constitutive enzyme
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?
sucrose + (1,4-alpha-D-glucosyl)n
D-fructose + (1,4-alpha-D-glucosyl)n+1
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constitutive enzyme
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?
sucrose + (1,4-alpha-D-glucosyl)n
D-fructose + (1,4-alpha-D-glucosyl)n+1
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involved in biosynthesis of amylopectin-glycogen type polysaccharide
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?
sucrose + (1,4-alpha-D-glucosyl)n
D-fructose + (1,4-alpha-D-glucosyl)n+1
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transfers glucose to growing alpha-1,4-glucan chains
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?
sucrose + (1,4-alpha-D-glucosyl)n
D-fructose + (1,4-alpha-D-glucosyl)n+1
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constitutive enzyme
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?
sucrose + (1,4-alpha-D-glucosyl)n
D-fructose + (1,4-alpha-D-glucosyl)n+1
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recombinant enzyme linearly elongates some branched chains of glycogen to an average degree of polymerization of 75
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sucrose + (1,4-alpha-D-glucosyl)n
D-fructose + (1,4-alpha-D-glucosyl)n+1
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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
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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
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?
sucrose + (1,4-alpha-D-glucosyl)n
D-fructose + (1,4-alpha-D-glucosyl)n+1
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glycogen is the best D-glucosyl unit acceptor. Semiprocessive glycogen elongation mechanism can be proposed on the basis of modeling data
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?
sucrose + (1,4-alpha-D-glucosyl)n
D-fructose + (1,4-alpha-D-glucosyl)n+1
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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
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constitutive enzyme
-
?
sucrose + (1,4-alpha-D-glucosyl)n
D-fructose + (1,4-alpha-D-glucosyl)n+1
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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
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constitutive enzyme
-
?
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 + 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
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-
?
sucrose + phloretin
D-fructose + phloretin glucoside 1 + phloretin glucoside 2 + phloretin glucoside 3
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the enzyme catalyzes the stereospecific glucosylation of phloretin at the 4'-position
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-
?
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
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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'
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?
sucrose + [(1->4)-alpha-D-glucosyl]n
D-fructose + [(1->4)-alpha-D-glucosyl]n+1
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-
?
sucrose + [(1->4)-alpha-D-glucosyl]n
D-fructose + [(1->4)-alpha-D-glucosyl]n+1
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-
-
?
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
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-
-
?
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
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-
?
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
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-
?
sucrose + [(1->4)-alpha-D-glucosyl]n
D-fructose + [(1->4)-alpha-D-glucosyl]n+1
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the enzyme shows polymerization activity using sucrose as a sole substrate
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?
sucrose + [(1->4)-alpha-D-glucosyl]n
D-fructose + [(1->4)-alpha-D-glucosyl]n+1
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-
-
?
sucrose + [(1->4)-alpha-D-glucosyl]n
D-fructose + [(1->4)-alpha-D-glucosyl]n+1
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-
-
?
sucrose + [(1->4)-alpha-D-glucosyl]n
D-fructose + [(1->4)-alpha-D-glucosyl]n+1
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-
-
-
?
sucrose + [(1->4)-alpha-D-glucosyl]n
D-fructose + [(1->4)-alpha-D-glucosyl]n+1
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-
linear alpha-(1,4)-glucans
-
?
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
?
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amylosucrase is a transglucosidase that catalyses the synthesis of an amylose-type polymer from sucrose, an abundant agro-resource
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additional information
?
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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%
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additional information
?
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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
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additional information
?
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arbutin-alpha-glucoside exhibits inhibitory activities of on mushroom tyrosinase and the melanin production in human melanoma cells
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additional information
?
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the hydrolysis reaction is not a rate-limiting step to perform transglycosylation in rDGAS
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additional information
?
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enzymatic production of trehalose from sucrose using amylosucrase and maltooligosyltrehalose synthase-trehalohydrolase, overview
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additional information
?
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NMR product analysis, overview
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additional information
?
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synthesis of sucrose isomers turanose and trehalulose from sucrose in the presence of fructose by DgAS, turanose binding site structure, overview
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additional information
?
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amylosucrase synthesizes alpha-1,4-glucans using sucrose as a sole substrate
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additional information
?
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NMR product analysis, overview
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additional information
?
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NMR product analysis, overview
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additional information
?
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amylosucrase is a transglucosidase that catalyzes amylose-like polymer synthesis from sucrose substrate
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additional information
?
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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
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additional information
?
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the enzyme does not require a nucleotide-activated sugar as a glucosyl-donor
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additional information
?
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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
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additional information
?
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the enzyme does not require a nucleotide-activated sugar as a glucosyl-donor
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additional information
?
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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
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additional information
?
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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
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additional information
?
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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
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additional information
?
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the enzyme catalyzes the synthesis of a water-insoluble amylose-like polymer from sucrose, a readily available and low-cost agroresource
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additional information
?
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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
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additional information
?
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product patterns formed by wild-type enzyme and selected genetic variants in the presence of sucrose as the sole substrate, overview
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additional information
?
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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
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additional information
?
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synthesis of sucrose isomers turanose and trehalulose from sucrose in the presence of fructose by NpAS, turanose binding site structure, overview
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additional information
?
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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
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additional information
?
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amylosucrase from Neisseria polysaccharea is a transglucosylase that synthesizes an insoluble amylose-like polymer from sole substrate sucrose, product isolation and analysis, overview
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additional information
?
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amylosucrase synthesizes alpha-1,4-glucans using sucrose as a sole substrate
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additional information
?
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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
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additional information
?
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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
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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
?
-
-
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
Q9ZEU2
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
Q1J0W0
-
-
-
?
sucrose + [(1->4)-alpha-D-glucosyl]n
D-fructose + [(1->4)-alpha-D-glucosyl]n+1
Q1J0W0
-
-
-
?
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
G4T024
-
-
-
?
sucrose + [(1->4)-alpha-D-glucosyl]n
D-fructose + [(1->4)-alpha-D-glucosyl]n+1
G4T024
-
-
-
?
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
-
-
-
-
?
sucrose + [(1->4)-alpha-D-glucosyl]n
D-fructose + [(1->4)-alpha-D-glucosyl]n+1
B1XIU7
-
-
-
?
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 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
?
-
-
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
?
-
Q9ZEU2
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
?
-
-
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
?
-
B1XIU7
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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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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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
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
-
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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 higher than 20 mM, sucrose hydrolysis; initial sucrose concentration lower than 20 mM, sucrose consumption
1.28
sucrose
-
initial sucrose concentration higher than 20 mM, sucrose consumption
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
4.8
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
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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
8.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 9.5
7 - 8.5
-
60% of maximal activity at pH 7.0, maximal activity at pH 8.5
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
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
30 - 55
35
37
40
45
50
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 57
-
recombinant enzyme, activity range, 80% of maximal activity at 35-45°C, 20% at 50°C, temperature profile, overview
20 - 50
-
recombinant enzyme, activity range, temperature profile, overview
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
489140, 489141, 489142, 489143, 489146, 489147, 658058, 658732, 659439, 659561, 677056, 719106, 719632, 735805, 735887
-
-
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
-
the enzyme belongs to the glycohydrolase family 13, GH13
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 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 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 is a glucosyltransferase of the glycoside hydrolase 13 family, that does not require a nucleotide-activated sugar as a glucosyl-donor
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 glycoside hydrolase family 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 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
Pseudarthrobacter chlorophenolicus A6 / DSM 12829
-
amylosucrase belongs to the glycoside hydrolase family 13, GH 13
-
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
-
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
-
dynamics and unfolding properties of the enzyme by the gauss network model and the anisotropic network model, overview
additional information
-
ligand binding causes extensive changes in active-site topology
additional information
-
active site topology and structure coparisons, overview; 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
-
loops 3, 4, and 7 of AS form an active-site pocket and play an important role in transglycosylation activity
additional information
-
essential role of enzyme subsite -1 for protein fitness and robustness
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 (182 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
Deinococcus geothermalis (strain DSM 11300)
Q9RVT9
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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 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
-
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 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
-
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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
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
-
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
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
-
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
-
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 - 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
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
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
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
additional information
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
additional information
-
the quaternary organization is likely to participate in the enhanced thermal stability of the protein
additional information
-
the quaternary organization is likely to participate in the enhanced thermal stability of the protein
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
recombinant C-terminally His6-tagged enzyme by nickel affinity chromatography
-
recombinant enzye from Escherichia coli strain BL21 to homogeneity using GST-affinity chromatography followed by dialysis and subsequent tag removal via PreScission protease and reverse affinity chromatography
-
recombinant GST-tagged ASase from Escherichia coli strain BL21 (DE3) by glutathione affinity chromatography, the tag is cleaved off by thrombin
-
recombinant GST-tagged DgAS by glutathione affinity chromatography, followed by proteolytic removal of the GST-tag
-
recombinant GST-tagged DGAS from Escherichia coli by glutathione affinity chromatography
-
recombinant GST-tagged DGAS from Escherichia coli strain BL21 by glutathione affinity chromatography
-
recombinant GST-tagged enzyme from Escherichia coli strain JM109 by glutathione affinity chromatography
-
recombinant GST-tagged NpAS by glutathione affinity chromatography, followed by proteolytic removal of the GST-tag
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis
-
recombinant His-tagged NPAS from Escherichia coli strain BL21 by nickel affinity chromatography
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3)pLyS by cobalt affinity chromatography
recombinant His6-tagged enzyme from Escherichia coli strain MC1061by nickel affinity chromatography
-
recombinant the His-tagged enzyme from Escherichia coli by nickel affinity chromatography
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
DNA library construction and DNA sequence determination and analysis, expression of the His-tagged enzyme in Escherichia coli
-
expression in Escherichia coli
expression of GST-tagged ASase in Escherichia coli strain BL21 (DE3)
-
expression of GST-tagged DgAS
expression of GST-tagged DGAS in Escherichia coli strain BL21
-
expression of wild-type and mutant enzymes in Escherichia coli strain JM109
-
expression of wild-type and random mutants in Escherichia coli strain JM109
-
gene acas, locus CP001341, DNA and amino acid sequence determination and analysis, expression of C-terminally His6-tagged enzyme
-
gene ams, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of the His6-tagged in Escherichia coli strain Rosettta (DE3)
gene ams, recombinant expression as starch-binding domain-fusion protein in Solanum tuberosum plants, cv. Kardal and amf, using the Agrobacterium tumefaciens transformation method
-
gene amsA, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)pLyS
gene dgas, DNA and amino acid sequence determination and analysis, expression of GST-tagged enzyme in Escherichia coli strain JM109
-
gene dgas, recombinant expression of C-terminally His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
gene drpas, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression of the His-tagged enzyme in Escherichia coli
-
gene mfas, DNA and amino acid sequence determination and analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
gene npas, recombinant expression of C-terminally His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
His6-tagged enzyme expression in Escherichia coli strain MC1061 using a constitutive expression system
-
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
-
recombinant expression of GST-tagged wild-type and mutant enzymes in Escherichia coli strain JM109
-
recombinant expression of wild-type and mutant enzymes in Escherichia coli strain JM109
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
genes spsA,sppA, frkA and amsA are grouped the Suc cluster, whose expression is increased in response to a salt treatment
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
synthesis
biotechnology
-
treatment of pre-gelatinized rice and barley starches with amylosucrase from Neisseria polysaccharea is a potential way of replacing commercial resistant starch production
biotechnology
-
the enzyme fused to a starch-binding domain (SBD) is introduced in two potato genetic backgrounds to synthesize starch granules with altered composition, and thereby to broaden starch applications. The modified larger starches not only have great benefit to the potato starch industry by reducing losses during starch isolation, but also have an advantage in many food applications such as frozen food due to its extremely high freeze-thaw stability. Modified starches show a higher digestibility after alpha-amylase treatment
synthesis
-
potentiality of amylosucrase in the design of amylodextrins with controlled morphology, structure, and physicochemical properties
synthesis
-
mutant enzyme R226A, that is activated by the products it forms and yields twice as much insoluble glucan and lower quantities of by-products as the wild-type enzyme is a very promising enzyme for industrial synthesis of amylose-like polymers
synthesis
-
potential of amylosucrase in the design of original carbohydrate-based dendritic nanoparticles
synthesis
-
the enzyme can be used for synthesis of salicin glycosides with sucrose serving as the glucopyranosyl donor and salicin as the acceptor molecule
synthesis
-
the enzyme can efficiently be used for synthesis of salicin glycosides with sucrose serving as the glucopyranosyl donor and salicin as the acceptor molecule
synthesis
-
the enzyme might be useful for important tailoring reactions for the generation of bioactive compounds by glycosylation
synthesis
-
the enzyme might be useful for important tailoring reactions for the generation of bioactive compounds by glycosylation
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Feingold, D.S.; Avigad, G.; Hestrin, S.
Enzymatic synthesis and reactions of a sucrose isomer alpha-D-galactopyranosyl-beta-D-fructofuranoside
J. Biol. Chem.
224
295-307
1957
Neisseria perflava
brenda
Okada, G.; Hehre, E.J.
New studies on amylosucrase, a bacterial alpha-D-glucosylase that directly converts sucrose to a glycogen-like alpha-glucan
J. Biol. Chem.
249
126-135
1974
Neisseria perflava
brenda
MacKenzie, C.R.; Johnson, K.G.; McDonald, I.J.
Glycogen synthesis by amylosucrase from Neisseria perflava
Can. J. Microbiol.
23
1303-1307
1977
Neisseria perflava, Neisseria perflava NRC 31001
brenda
MacKenzie, C.R.; McDonald, I.J.; Johnson, K.G.
Glycogen metabolism in the genus Neisseria: synthesis from sucrose by amylosucrase
Can. J. Microbiol.
24
357-362
1978
Bergeriella denitrificans, Moraxella cuniculi, Neisseria canis, Neisseria cinerea, Neisseria perflava, Neisseria sicca, Neisseria subflava, no activity in Neisseria cuniculi
brenda
Tao, B.Y.; Reilly, P.J.; Robyt, J.F.
Neisseria perflava amylosucrase: characterization of its product polysaccharide and a study of its inhibition by sucrose derivatives
Carbohydr. Res.
181
163-174
1988
Neisseria perflava
brenda
Okada, G.; Hehre, E.J.
De novo synthesis of glycosidic linkages by glycosylases: utilization of alpha-D-glucopyranosyl fluoride by amylosucrase
Carbohydr. Res.
26
240-243
1973
Neisseria perflava
brenda
Remaud-Simeon, M.; Albaret, F.; Canard, B.; Varlet, I.; Colonna, P.; Willemot, R.M.; Monsan, P.
Studies on a recombinant amylosucrase
Prog. Biotechnol.
10
313-320
1995
Neisseria polysaccharea
-
brenda
De Montalk, G.P.; Remaud-Simeon, M.; Willemot, R.M.; Planchot, V.; Monsan, P.
Sequence analysis of the gene encoding amylosucrase from Neisseria polysaccharea and characterization of the recombinant enzyme
J. Bacteriol.
181
375-381
1999
Neisseria polysaccharea
brenda
Potocki de Montalk, G.; Remaud-Simeon, M.; Willemot, R.M.; Sarcabal, P.; Planchot, V.; Monsan, P.
Amylosucrase from Neisseria polysaccharea: novel catalytic properties
FEBS Lett.
471
219-223
2000
Neisseria polysaccharea
brenda
Potocki de Montalk, G.; Remaud-Simeon, M.; Willemot, R.M.; Monsan, P.
Characterization of the activator effect of glycogen on amylosucrase from Neisseria polysaccharea
FEMS Microbiol. Lett.
186
103-108
2000
Neisseria polysaccharea
brenda
Skov, L.K.; Mirza, O.; Henriksen, A.; de Montalk, G.P.; Remaud-Simeon, M.; Sarcabal, P.; Willemot, R.M.; Monsan, P.; Gajhede, M.
Amylosucrase, a glucan-synthesizing enzyme from the alpha-amylase family
J. Biol. Chem.
276
25273-25278
2001
Neisseria polysaccharea, Neisseria polysaccharea (Q9ZEU2)
brenda
Skov, L.K.; Mirza, O.; Sprogoe, D.; Dar, I.; Remaud-Simeon, M.; Albenne, C.; Monsan, P.; Gajhede, M.
Oligosaccharide and Sucrose Complexes of Amylosucrase
J. Biol. Chem.
277
47741-47747
2002
Neisseria polysaccharea (Q9ZEU2)
brenda
Mirza, O.; Skov, L.K.; Remaud-Simeon, M.; Potocki de Montalk, G.; Albenne, C.; Monsan, P.; Gajhede, M.
Crystal structures of amylosucrase from Neisseria polysaccharea in complex with D-glucose and the active site mutant Glu328Gln in complex with the natural substrate sucrose
Biochemistry
40
9032-9039
2001
Neisseria polysaccharea
brenda
Albenne, C.; Potocki De Montalk, G.; Monsan, P.; Skov, L.; Mirza, O.; Gajhede, M.; Remaud-Simeon, M.
Site-directed mutagenesis of key amino acids in the active site of amylosucrase from Neisseria polysaccharea
Biologia (Bratisl. )
57
119-128
2002
Neisseria polysaccharea
-
brenda
Jensen, M.H.; Mirza, O.; Albenne, C.; Remaud-Simeon, M.; Monsan, P.; Gajhede, M.; Skov, L.K.
Crystal structure of the covalent intermediate of amylosucrase from Neisseria polysaccharea
Biochemistry
43
3104-3110
2004
Neisseria polysaccharea
brenda
Potocki-Veronese, G.; Putaux, J.L.; Dupeyre, D.; Albenne, C.; Remaud-Simeon, M.; Monsan, P.; Buleon, A.
Amylose synthesized in vitro by amylosucrase: morphology, structure, and properties
Biomacromolecules
6
1000-1011
2005
Neisseria polysaccharea
brenda
van der Veen, B.A.; Potocki-Veronese, G.; Albenne, C.; Joucla, G.; Monsan, P.; Remaud-Simeon, M.
Combinatorial engineering to enhance amylosucrase performance: construction, selection, and screening of variant libraries for increased activity
FEBS Lett.
560
91-97
2004
Neisseria polysaccharea
brenda
Pizzut-Serin, S.; Potocki-Veronese, G.; van der Veen, B.A.; Albenne, C.; Monsan, P.; Remaud-Simeon, M.
Characterisation of a novel amylosucrase from Deinococcus radiodurans
FEBS Lett.
579
1405-1410
2005
Deinococcus radiodurans
brenda
Albenne, C.; Skov, L.K.; Mirza, O.; Gajhede, M.; Feller, G.; D'Amico, S.; Andre, G.; Potocki-Veronese, G.; van der Veen, B.A.; Monsan, P.; Remaud-Simeon, M.
Molecular basis of the amylose-like polymer formation catalyzed by Neisseria polysaccharea amylosucrase
J. Biol. Chem.
279
726-734
2004
Neisseria polysaccharea
brenda
Rolland-Sabate, A.; Colonna, P.; Potocki-Veronese, G.; Monsan, P.; Planchot, V.
Elongation and insolubilisation of ?-glucans by the action of Neisseria polysaccharea amylosucrase.
J. Cereal Sci.
40
17-30
2004
Neisseria polysaccharea
brenda
Putaux, J.L.; Potocki-Veronese, G.; Remaud-Simeon, M.; Buleon, A.
alpha-D-Glucan-based dendritic nanoparticles prepared by in vitro enzymatic chain extension of glycogen
Biomacromolecules
7
1720-1728
2006
Neisseria polysaccharea
brenda
van der Veen, B.A.; Skov, L.K.; Potocki-Veronese, G.; Gajhede, M.; Monsan, P.; Remaud-Simeon, M.
Increased amylosucrase activity and specificity, and identification of regions important for activity, specificity and stability through molecular evolution
FEBS J.
273
673-681
2006
Neisseria polysaccharea (Q9ZEU2)
brenda
Albenne, C.; Skov, L.K.; Tran, V.; Gajhede, M.; Monsan, P.; Remaud-Simeon, M.; Andre-Leroux, G.
Towards the molecular understanding of glycogen elongation by amylosucrase
Proteins
66
118-126
2007
Neisseria polysaccharea
brenda
Emond, S.; Mondeil, S.; Jaziri, K.; Andre, I.; Monsan, P.; Remaud-Simeon, M.; Potocki-Veronese, G.
Cloning, purification and characterization of a thermostable amylosucrase from Deinococcus geothermalis
FEMS Microbiol. Lett.
285
25-32
2008
Deinococcus geothermalis
brenda
Emond, S.; Potocki-Veronese, G.; Mondon, P.; Bouayadi, K.; Kharrat, H.; Monsan, P.; Remaud-Simeon, M.
Optimized and automated protocols for high-throughput screening of amylosucrase libraries
J. Biomol. Screen.
12
715-723
2007
Neisseria polysaccharea (Q9ZEU2)
brenda
Emond, S.; Andre, I.; Jaziri, K.; Potocki-Veronese, G.; Mondon, P.; Bouayadi, K.; Kharrat, H.; Monsan, P.; Remaud-Simeon, M.
Combinatorial engineering to enhance thermostability of amylosucrase
Protein Sci.
17
967-976
2008
Deinococcus radiodurans
brenda
Schneider, J.; Fricke, C.; Overwin, H.; Hofmann, B.; Hofer, B.
Generation of amylosucrase variants that terminate catalysis of acceptor elongation at the di- or trisaccharide stage
Appl. Environ. Microbiol.
75
7453-7460
2009
Neisseria polysaccharea (Q9ZEU2)
brenda
Jung, J.H.; Seo, D.H.; Ha, S.J.; Song, M.C.; Cha, J.; Yoo, S.H.; Kim, T.J.; Baek, N.I.; Baik, M.Y.; Park, C.S.
Enzymatic synthesis of salicin glycosides through transglycosylation catalyzed by amylosucrases from Deinococcus geothermalis and Neisseria polysaccharea
Carbohydr. Res.
344
1612-1619
2009
Deinococcus geothermalis, Neisseria polysaccharea, Neisseria polysaccharea (Q9ZEU2)
brenda
Seo, D.; Jung, J.; Ha, S.; Song, M.; Cha, J.; Yoo, S.; Kim, T.; Baek, N.; Park, C.
Highly selective biotransformation of arbutin to arbutin-alpha-glucoside using amylosucrase from Deinococcus geothermalis DSM 11300
J. Mol. Catal. B
60
113-118
2009
Deinococcus geothermalis
-
brenda
Seo, D.H.; Jung, J.H.; Ha, S.J.; Cho, H.K.; Jung, D.H.; Kim, T.J.; Baek, N.I.; Yoo, S.H.; Park, C.S.
High-yield enzymatic bioconversion of hydroquinone to alpha-arbutin, a powerful skin lightening agent, by amylosucrase
Appl. Microbiol. Biotechnol.
94
1189-1197
2012
Deinococcus geothermalis
brenda
Wang, R.; Kim, J.H.; Kim, B.S.; Park, C.S.; Yoo, S.H.
Preparation and characterization of non-covalently immobilized amylosucrase using a pH-dependent autoprecipitating carrier
Biores. Technol.
102
6370-6374
2011
Neisseria polysaccharea, Neisseria polysaccharea ATCC 43768
brenda
Cho, H.K.; Kim, H.H.; Seo, D.H.; Jung, J.H.; Park, J.H.; Baek, N.I.; Kim, M.J.; Yoo, S.H.; Cha, J.; Kim, Y.R.; Park, C.S.
Biosynthesis of (+)-catechin glycosides using recombinant amylosucrase from Deinococcus geothermalis DSM 11300
Enzyme Microb. Technol.
49
246-253
2011
Deinococcus geothermalis, Deinococcus geothermalis (Q1J0W0), Deinococcus geothermalis DSM 11300, Deinococcus geothermalis DSM 11300 (Q1J0W0)
brenda
Kim, J.H.; Wang, R.; Lee, W.H.; Park, C.S.; Lee, S.; Yoo, S.H.
One-pot synthesis of cycloamyloses from sucrose by dual enzyme treatment: combined reaction of amylosucrase and 4-alpha-glucanotransferase
J. Agric. Food Chem.
59
5044-5051
2011
Neisseria polysaccharea
brenda
Guerin, F.; Barbe, S.; Pizzut-Serin, S.; Potocki-Veronese, G.; Guieysse, D.; Guillet, V.; Monsan, P.; Mourey, L.; Remaud-Simeon, M.; Andre, I.; Tranier, S.
Structural investigation of the thermostability and product specificity of amylosucrase from the bacterium Deinococcus geothermalis
J. Biol. Chem.
287
6642-6654
2012
Deinococcus geothermalis, Neisseria polysaccharea, Neisseria polysaccharea (Q9ZEU2)
brenda
Seo, D.H.; Jung, J.H.; Choi, H.C.; Cho, H.K.; Kim, H.H.; Ha, S.J.; Yoo, S.H.; Cha, J.; Park, C.S.
Functional expression of amylosucrase, a glucan-synthesizing enzyme, from Arthrobacter chlorophenolicus A6
J. Microbiol. Biotechnol.
22
1253-1257
2012
Pseudarthrobacter chlorophenolicus, Pseudarthrobacter chlorophenolicus A6 / DSM 12829
brenda
Liu, M.; Wang, S.; Sun, T.; Su, J.; Zhang, Y.; Yue, J.; Sun, Z.
Insight into the structure, dynamics and the unfolding property of amylosucrases: implications of rational engineering on thermostability
PLoS ONE
7
e40441
2012
Deinococcus geothermalis
brenda
Kim, H.; Jung, J.; Seo, D.; Ha, S.; Yoo, S.; Kim, C.; Park, C.
Novel enzymatic production of trehalose from sucrose using amylosucrase and maltooligosyltrehalose synthase-trehalohydrolase
World J. Microbiol. Biotechnol.
27
2851-2856
2011
Deinococcus geothermalis
brenda
Skov, L.K.; Pizzut-Serin, S.; Remaud-Simeon, M.; Ernst, H.A.; Gajhede, M.; Mirza, O.
The structure of amylosucrase from Deinococcus radiodurans has an unusual open active-site topology
Acta Crystallogr. Sect. F
69
973-978
2013
Deinococcus radiodurans
brenda
Jeong, J.W.; Seo, D.H.; Jung, J.H.; Park, J.H.; Baek, N.I.; Kim, M.J.; Park, C.S.
Biosynthesis of glucosyl glycerol, a compatible solute, using intermolecular transglycosylation activity of amylosucrase from Methylobacillus flagellatus KT
Appl. Biochem. Biotechnol.
173
904-917
2014
Methylobacillus flagellatus, Methylobacillus flagellatus ATCC 51484
brenda
But, S.Y.; Khmelenina, V.N.; Reshetnikov, A.S.; Mustakhimov, I.I.; Kalyuzhnaya, M.G.; Trotsenko, Y.A.
Sucrose metabolism in halotolerant methanotroph Methylomicrobium alcaliphilum 20Z
Arch. Microbiol.
197
471-480
2015
Methylomicrobium alcaliphilum 20Z (G4T024), Methylomicrobium alcaliphilum 20Z, Methylomicrobium alcaliphilum (G4T024)
brenda
Cambon, E.; Barbe, S.; Pizzut-Serin, S.; Remaud-Simeon, M.; Andre, I.
Essential role of amino acid position 226 in oligosaccharide elongation by amylosucrase from Neisseria polysaccharea
Biotechnol. Bioeng.
111
1719-1728
2014
Neisseria polysaccharea
brenda
Kim, B.S.; Kim, H.S.; Yoo, S.H.
Characterization of enzymatically modified rice and barley starches with amylosucrase at scale-up production
Carbohydr. Polym.
125
61-68
2015
Neisseria polysaccharea
brenda
Daude, D.; Champion, E.; Morel, S.; Guieysse, D.; Remaud-Simeon, M.; Andre, I.
Probing substrate promiscuity of amylosucrase from Neisseria polysaccharea
ChemCatChem
5
2288-2295
2013
Neisseria polysaccharea (Q9ZEU2)
-
brenda
Seo, D.H.; Jung, J.H.; Jung, D.H.; Park, S.; Yoo, S.H.; Kim, Y.R.; Park, C.S.
An unusual chimeric amylosucrase generated by domain-swapping mutagenesis
Enzyme Microb. Technol.
86
7-16
2016
Deinococcus geothermalis, Deinococcus geothermalis (Q1J0W0), Neisseria polysaccharea, Neisseria polysaccharea (Q9ZEU2)
brenda
Kim, B.K.; Kim, H.I.; Moon, T.W.; Choi, S.J.
Branch chain elongation by amylosucrase: production of waxy corn starch with a slow digestion property
Food Chem.
152
113-120
2014
Neisseria polysaccharea (Q9ZEU2)
brenda
Kim, M.; Seo, D.; Jung, J.; Jung, D.; Joe, M.; Lim, S.; Lee, J.; Park, C.
Molecular cloning and expression of amylosucrase from highly radiation-resistant Deinococcus radiopugnans
Food Sci. Biotechnol.
23
2007-2012
2014
Deinococcus radiopugnans, Deinococcus radiopugnans ATCC 19172
-
brenda
Overwin, H.; Wray, V.; Hofer, B.
Biotransformation of phloretin by amylosucrase yields three novel dihydrochalcone glucosides
J. Biotechnol.
211
103-106
2015
Neisseria polysaccharea, Neisseria polysaccharea (Q9ZEU2), Neisseria polysaccharea ATCC 43768 (Q9ZEU2)
brenda
Perez-Cenci, M.; Salerno, G.L.
Functional characterization of Synechococcus amylosucrase and fructokinase encoding genes discovers two novel actors on the stage of cyanobacterial sucrose metabolism
Plant Sci.
224
95-102
2014
Synechococcus sp. (B1XIU7), Synechococcus sp.
brenda
Huang, X.F.; Nazarian-Firouzabadi, F.; Vincken, J.P.; Ji, Q.; Visser, R.G.; Trindade, L.M.
Expression of an amylosucrase gene in potato results in larger starch granules with novel properties
Planta
240
409-421
2014
Neisseria polysaccharea, Neisseria polysaccharea (Q9ZEU2)
brenda
Liu, M.; Li, P.; Liu, B.; Su, J.; Wang, C.
Insights into the working mechanism and unfolding property of Arthrobacter chlorophenolicus amylosucrase
Prog. Biochem. Biophys.
40
565-577
2013
Pseudarthrobacter chlorophenolicus
-
brenda
Daude, D.; Topham, C.M.; Remaud-Simeon, M.; Andre, I.
Probing impact of active site residue mutations on stability and activity of Neisseria polysaccharea amylosucrase
Protein Sci.
22
1754-1765
2013
Neisseria polysaccharea, Neisseria polysaccharea (Q9ZEU2)
brenda
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