Information on EC 2.4.1.4 - amylosucrase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.4.1.4
-
RECOMMENDED NAME
GeneOntology No.
amylosucrase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
sucrose + [(1->4)-alpha-D-glucosyl]n = D-fructose + [(1->4)-alpha-D-glucosyl]n+1
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Starch and sucrose metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
sucrose:(1->4)-alpha-D-glucan 4-alpha-D-glucosyltransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9032-11-5
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene drpas
-
-
Manually annotated by BRENDA team
gene mfas
-
-
Manually annotated by BRENDA team
gene ams
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
strain NRC 31001
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-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
no activity in Neisseria cuniculi
var. giganta
-
-
Manually annotated by BRENDA team
gene amsA
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
sucrose
?
show the reaction diagram
-
-
-
-
?
sucrose
glucose + maltose + maltotriose + soluble maltooligosaccharides + trehalulose + turanose + insoluble glucan
show the reaction diagram
-
-
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
show the reaction diagram
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 + (+)-catechin
D-fructose + (+)-catechin-3'-O-alpha-D-glucopyranoside
show the reaction diagram
sucrose + (1,4-alpha-D-glucosyl)n
D-fructose + (1,4-alpha-D-glucosyl)n+1
show the reaction diagram
sucrose + amylose
D-fructose + [(1->4)-alpha-D-glucosyl]n+1
show the reaction diagram
-
-
-
-
?
sucrose + arbutin
D-fructose + alpha-D-glucopyranosyl-(1,4)-arbutin
show the reaction diagram
-
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 35C in donor to acceptor ratios of 1:0.5 and 1:1, respectively
product identification by TLC and NMR analysis, product structure, overview
-
?
sucrose + carboxy methyl cellulose
D-fructose + ?
show the reaction diagram
-
-
-
-
?
sucrose + dextran T10
D-fructose + ?
show the reaction diagram
-
-
-
-
?
sucrose + dextran T200
D-fructose + ?
show the reaction diagram
-
-
-
-
?
sucrose + dextran T70
D-fructose + ?
show the reaction diagram
-
-
-
-
?
sucrose + galactomannan
D-fructose + ?
show the reaction diagram
-
-
-
-
?
sucrose + glycerol
(2S)-1-O-alpha-D-glucosyl-glycerol + (2R)-1-O-alpha-D-glucosyl-glycerol + 2-O-alpha-D-glucosyl-glycerol
show the reaction diagram
sucrose + glycogen
?
show the reaction diagram
sucrose + glycogen
D-fructose + ?
show the reaction diagram
-
-
-
-
?
sucrose + hydroquinone
D-fructose + hydroquinone-O-alpha-D-glucopyranoside
show the reaction diagram
-
-
-
-
?
sucrose + laminarin
D-fructose + ?
show the reaction diagram
-
-
-
-
?
sucrose + linterised potato starch
D-fructose + ?
show the reaction diagram
-
-
-
-
?
sucrose + maltobiose
D-fructose + maltotriose
show the reaction diagram
-
-
-
-
?
sucrose + maltoheptaose
?
show the reaction diagram
-
-
-
-
?
sucrose + maltopentaose
D-fructose + maltohexaose
show the reaction diagram
-
-
-
-
?
sucrose + maltopentaose
D-fructose + maltohexaose + maltoheptaose
show the reaction diagram
-
-
-
?
sucrose + maltose
D-fructose + (+)-catechin-3'-O-alpha-D-maltoside
show the reaction diagram
sucrose + maltose
D-fructose + maltotriose
show the reaction diagram
-
-
-
-
?
sucrose + maltotetraose
D-fructose + maltopentaose
show the reaction diagram
-
-
-
-
?
sucrose + maltotriose
D-fructose + maltotetraose
show the reaction diagram
-
-
-
-
?
sucrose + phloretin
D-fructose + phloretin glucoside 1 + phloretin glucoside 2 + phloretin glucoside 3
show the reaction diagram
sucrose + phloretin
D-fructose + phloretin glucoside A1 + phloretin glucoside A2 + phloretin glucoside A3
show the reaction diagram
sucrose + phytoglycogen
D-fructose + ?
show the reaction diagram
-
-
-
-
?
sucrose + pullulan
D-fructose + ?
show the reaction diagram
-
-
-
-
?
sucrose + salicin
D-fructose + alpha-D-glucopyranosyl-(1,4)-salicin
show the reaction diagram
-
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
show the reaction diagram
-
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 + starch
D-fructose + ?
show the reaction diagram
-
-
-
-
?
sucrose + waxy maize amylopectin
D-fructose + ?
show the reaction diagram
-
-
-
-
?
sucrose + waxy maize starch
D-fructose + ?
show the reaction diagram
-
-
-
-
?
sucrose + [(1->4)-alpha-D-glucosyl]n
D-fructose + [(1->4)-alpha-D-glucosyl]n+1
show the reaction diagram
sucrose + [(1?4)-alpha-D-glucosyl]n
D-fructose + [(1?4)-alpha-D-glucosyl]n+1
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
sucrose + (1,4-alpha-D-glucosyl)n
D-fructose + (1,4-alpha-D-glucosyl)n+1
show the reaction diagram
sucrose + maltobiose
D-fructose + maltotriose
show the reaction diagram
-
-
-
-
?
sucrose + maltopentaose
D-fructose + maltohexaose
show the reaction diagram
-
-
-
-
?
sucrose + maltotetraose
D-fructose + maltopentaose
show the reaction diagram
-
-
-
-
?
sucrose + maltotriose
D-fructose + maltotetraose
show the reaction diagram
-
-
-
-
?
sucrose + phloretin
D-fructose + phloretin glucoside A1 + phloretin glucoside A2 + phloretin glucoside A3
show the reaction diagram
sucrose + [(1->4)-alpha-D-glucosyl]n
D-fructose + [(1->4)-alpha-D-glucosyl]n+1
show the reaction diagram
additional information
?
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4,6-Dideoxysucrose
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noncompetitive inhibition
6-Deoxy-6-fluorosucrose
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competitive inhibition
6-Deoxysucrose
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competitive inhibition
D-fructose
Sucrose
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above 100 mM, substrate inhibition
Tris-HCl buffer
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-
additional information
-
not inhibited by C-3-modified sucrose derivatives
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
glycogen
maltooligosaccharides
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activate recombinant enzyme
starch
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activates recombinant enzyme
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.014 - 11
maltobiose
-
0.024 - 61
maltopentaose
0.026 - 30
maltotetraose
0.0123 - 16
maltotriose
1.9 - 387
Sucrose
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.1 - 14
maltobiose
-
47 - 173
maltopentaose
7.5 - 67
maltotetraose
4.8 - 33
maltotriose
0.167 - 173
Sucrose
additional information
additional information
Neisseria polysaccharea
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-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.28 - 0.99
maltobiose
210600
0.77 - 7.2
maltopentaose
272
0.25 - 2.6
maltotetraose
269
0.3 - 2.7
maltotriose
188
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.5
6-Deoxy-6-fluorosucrose
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-
6.2
6-Deoxysucrose
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-
14 - 50
D-fructose
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.8
-
sucrose hydrolysis, purified recombinant GST-tagged DgAS, pH 7.0, 37C
5
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sucrose hydrolysis, purified recombinant detagged DgAS, pH 7.0, 37C
9.57
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recombinant enzyme
44
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purified recombinant enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
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recombinant enzyme
7 - 8
-
wild-type enzyme
8 - 9
wild-type enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 9.5
7 - 8.5
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60% of maximal activity at pH 7.0, maximal activity at pH 8.5
7 - 9
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high activity range
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
assay at room temperature
30 - 55
36
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recombinant wild-type enzyme and mutant P351S
40 - 45
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recombinant His-tagged enzyme
42
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wild-type enzyme
47
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recombinant enzyme
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 57
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recombinant enzyme, activity range, 80% of maximal activity at 35-45C, 20% at 50C, temperature profile, overview
20 - 50
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recombinant enzyme, activity range, temperature profile, overview
25 - 50
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activity range, profile overview
30 - 55
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activity range, profile overview
37 - 50
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no activity above 50C, optimum activity around 37C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.3
-
sequence calculation
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
PDB
SCOP
CATH
ORGANISM
UNIPROT
Deinococcus geothermalis (strain DSM 11300)
Deinococcus geothermalis (strain DSM 11300)
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70000
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; native PAGE
74560
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sequence calculation
152100
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recombinant His-tagged enzyme, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
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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
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
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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, 4C, X-ray diffraction structure determination and analysis at 3.15 A resolution, modeling
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cocrystallization of E328Q mutant enzyme with maltoheptaose, X-ray structure at 2.2 A resolution
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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
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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
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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
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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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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
-
native enzyme, half-life: 15-20 h
40 - 50
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half-life of the enzyme is 421.4 h at 40C and 3.3 h at 45C, the thermostability of DRpAS dramatically decreases at 50C, Tm value is 50.7C and the half-life of the enzyme is 7.2 min at 50C
40
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the purified recombinant His-tagged ACAS is stable up to 40C, 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 45C and their melting temperatures are 43.25C and 51.52C, respectively
45
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inactivation within 10 min
50 - 62
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half-lives of mutant DGAS-B are 30.70 and 3.39 min at 50C and 55C, respectively, whereas that of the wild-type DGAS is 65.74 min at 55C. The melting temperatures of mutant DGAS-B and wild-type DGAS are 54.23C and 61.42C, respectively
55
-
DGAS shows a half-life of 6.8 h at 55C
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
rapid freezing or deep freezing inactivates
-
the enzyme is quite instable
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, several months, no loss of activity
-
2-4C, t1/2: 15-20 h
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant C-terminally His6-tagged enzyme by nickel affinity chromatography
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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
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recombinant enzyme
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recombinant GST-tagged ASase from Escherichia coli strain BL21 (DE3) by glutathione affinity chromatography, the tag is cleaved off by thrombin
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recombinant GST-tagged DgAS by glutathione affinity chromatography, followed by proteolytic removal of the GST-tag
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recombinant GST-tagged DGAS from Escherichia coli by glutathione affinity chromatography
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recombinant GST-tagged DGAS from Escherichia coli strain BL21 by glutathione affinity chromatography
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recombinant GST-tagged enzyme from Escherichia coli strain JM109 by glutathione affinity chromatography
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recombinant GST-tagged NpAS by glutathione affinity chromatography, followed by proteolytic removal of the GST-tag
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recombinant His-tagged enzyme from Escherichia coli
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recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis
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recombinant His-tagged NPAS from Escherichia coli strain BL21 by nickel affinity chromatography
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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
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recombinant the His-tagged enzyme from Escherichia coli by nickel affinity chromatography
-
wild-type and mutant enzymes
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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
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expression in Escherichia coli
expression of GST-tagged ASase in Escherichia coli strain BL21 (DE3)
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expression of GST-tagged DgAS
expression of GST-tagged DGAS in Escherichia coli strain BL21
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expression of His-tagged NPAS in Escherichia coli strain BL21
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expression of wild-type and mutant enzymes in Escherichia coli strain JM109
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expression of wild-type and random mutants in Escherichia coli strain JM109
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gene acas, locus CP001341, DNA and amino acid sequence determination and analysis, expression of C-terminally His6-tagged enzyme
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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
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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
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gene dgas, expression of GST-tagged DGAS in Escherichia coli
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gene dgas, recombinant expression of C-terminally His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
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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
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gene mfas, DNA and amino acid sequence determination and analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
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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
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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
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recombinant expression in Escherichia coli strain BL21
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recombinant expression of GST-tagged wild-type and mutant enzymes in Escherichia coli strain JM109
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recombinant expression of wild-type and mutant enzymes in Escherichia coli strain JM109
-
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
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A170V/Q353L
-
random mutagenesis, the mutant shows 3.5fold increased thermostabilty at 50C compared to the wild-type enzyme
P351S
-
random mutagenesis, the mutant shows 8fold increased thermostabilty at 50C compared to the wild-type enzyme
R20C/A451T
-
random mutagenesis, the mutant shows 10fold increased thermostabilty at 50C compared to the wild-type enzyme
D144A
-
site-directed mutagenesis
D144E
-
site-directed mutagenesis
D144I
-
site-directed mutagenesis
D394A
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23.5% of the wild-type activity, according to the initial rate of sucrose consumption, very poor ativation by glycogen
D507A
-
site-directed mutagenesis
D507I
-
site-directed mutagenesis
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
F250A
-
site-directed mutagenesis
F250N
-
site-directed mutagenesis
F250Y
-
site-directed mutagenesis
H187L
-
site-directed mutagenesis
H187Q
-
site-directed mutagenesis
H392P
-
site-directed mutagenesis
N387D
-
60% increase in activity compared to wild-type enzyme, increased stability at 50C
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
R284D
-
site-directed mutagenesis
R284H
-
site-directed mutagenesis
R284K
-
site-directed mutagenesis
R284V
-
site-directed mutagenesis
R415A
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4.3% of the activity compared with the wild-type enzyme. No synthesis of any insoluble modified glycogen
R446E
-
site-directed mutagenesis
R446F
-
site-directed mutagenesis
R509Q
-
site-directed mutagenesis
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
Y147A
-
site-directed mutagenesis
Y147F
-
site-directed mutagenesis
Y147N
-
site-directed mutagenesis
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
synthesis