Information on EC 2.4.1.64 - alpha,alpha-trehalose phosphorylase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
2.4.1.64
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RECOMMENDED NAME
GeneOntology No.
alpha,alpha-trehalose phosphorylase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
alpha,alpha-trehalose + phosphate = D-glucose + beta-D-glucose 1-phosphate
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
trehalose degradation IV
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Starch and sucrose metabolism
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
alpha,alpha-trehalose:phosphate beta-D-glucosyltransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
37205-59-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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
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Manually annotated by BRENDA team
Glycine max Merril cv. Beeson 80 in symbiosis with Bradyrhizobium japonicum
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Manually annotated by BRENDA team
strain SM-ZK
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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
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
6-deoxy-D-glucose + alpha-D-glucose 1-phosphate
alpha-D-glucopyranosyl 6-deoxy-alpha-D-glucopyranoside + phosphate
show the reaction diagram
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at 93% the activity with rate of glucose glucosylation
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alpha,alpha-trehalose + phosphate
alpha-D-glucose + beta-D-glucose 1-phosphate
show the reaction diagram
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-
-
-
?
alpha,alpha-trehalose + phosphate
beta-D-glucose 1-phosphate + D-glucose
show the reaction diagram
alpha,alpha-trehalose + phosphate
D-glucose + beta-D-glucose 1-phosphate
show the reaction diagram
alpha-D-galactopyranosyl alpha-D-glucopyranoside + phosphate
D-glucose + beta-D-galactose 1-phosphate
show the reaction diagram
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while the wild type enzyme shows very low activity, the mutant enzyme L649G/A693Q/W371Y displays a strict specificity (99%) for beta-D-galactose 1-phosphate as product
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r
beta-D-glucose 1-phosphate + alpha-D-allose
?
show the reaction diagram
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4.5% activity compared to D-glucose
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r
beta-D-glucose 1-phosphate + alpha-D-arabinose
?
show the reaction diagram
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1.8% activity compared to D-glucose
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r
beta-D-glucose 1-phosphate + alpha-D-fucose
?
show the reaction diagram
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22% activity compared to D-glucose
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r
beta-D-glucose 1-phosphate + alpha-D-galactose
?
show the reaction diagram
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83.7% activity compared to D-glucose
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r
beta-D-glucose 1-phosphate + alpha-D-lyxose
?
show the reaction diagram
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1.3% activity compared to D-glucose
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r
beta-D-glucose 1-phosphate + alpha-D-mannose
?
show the reaction diagram
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14.1% activity compared to D-glucose
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r
beta-D-glucose 1-phosphate + alpha-D-xylose
?
show the reaction diagram
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135.2% activity compared to D-glucose
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r
beta-D-glucose 1-phosphate + alpha-L-fucose
?
show the reaction diagram
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109.2% activity compared to D-glucose
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r
beta-D-glucose 1-phosphate + beta-L-arabinose
?
show the reaction diagram
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79.9% activity compared to D-glucose
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r
beta-D-glucose 1-phosphate + D-galactose
? + phosphate
show the reaction diagram
low activity. The Km value for D-galactose is about 30fold higher than that for D-glucose
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r
beta-D-glucose 1-phosphate + D-glucose
alpha,alpha-trehalose + phosphate
show the reaction diagram
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100% activity with D-glucose
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r
beta-D-glucose-1-phosphate + gentiobiose
6-O-beta-D-glucopyranosyl trehalose + phosphate
show the reaction diagram
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?
beta-D-glucose-1-phosphate + isomaltose
6-O-alpha-D-glucopyranosyl trehalose + phosphate
show the reaction diagram
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-
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?
beta-D-glucose-1-phosphate + isomaltotriose
?
show the reaction diagram
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-
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?
beta-D-glucose-1-phosphate + isopanose
?
show the reaction diagram
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-
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-
?
beta-D-glucose-1-phosphate + melibiose
6-O-alpha-D-galactopyranosyl trehalose + phosphate
show the reaction diagram
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-
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?
D-galactose + beta-D-glucose 1-phosphate
lactotrehalose + phosphate
show the reaction diagram
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r
D-glucose + beta-D-galactose 1-phosphate
alpha-D-galactopyranosyl alpha-D-glucopyranoside + phosphate
show the reaction diagram
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r
D-glucose + beta-D-glucose 1-phosphate
alpha,alpha-trehalose + phosphate
show the reaction diagram
lactotrehalose + phosphate
D-galactose + beta-D-glucose 1-phosphate
show the reaction diagram
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r
xylose + beta-D-glucose 1-phosphate
glucosyl-1,1-xylose 1-phosphate
show the reaction diagram
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glucosylated at 23% of the rate of glucose glucosylation
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additional information
?
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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
alpha,alpha-trehalose + phosphate
D-glucose + beta-D-glucose 1-phosphate
show the reaction diagram
D-galactose + beta-D-glucose 1-phosphate
lactotrehalose + phosphate
show the reaction diagram
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-
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r
D-glucose + beta-D-glucose 1-phosphate
alpha,alpha-trehalose + phosphate
show the reaction diagram
lactotrehalose + phosphate
D-galactose + beta-D-glucose 1-phosphate
show the reaction diagram
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r
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K+
essential for enzymatic activity. Decreasing potassium ion concentrations significantly reduce thermal and pH stabilities of the enzyme
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-deoxynojirimycin
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1 mM, complete inhibition
alpha,alpha-trehalose
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D-glucose
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strong substrate inhibition, 500 mM D-glucose reduces the enzyme activity to 49.1% of the activity at the saturating concentration of 30 mM
fructose 2,6-diphosphate
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inhibition in both directions
Ni2+
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1 mM, 88% inhibition
validamycin A
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10 mM, complete inhibition
Validoxylamine A
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0.2 mM, complete inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.86
alpha,alpha-trehalose
recombinant enzyme, at pH 6.5 and 30C
64.8
alpha-D-arabinose
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in 50 mM MES buffer (pH 6.0), at 60C
171.5
alpha-D-galactose
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in 50 mM MES buffer (pH 6.0), at 60C
20.3
alpha-D-xylose
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in 50 mM MES buffer (pH 6.0), at 60C
183.4
alpha-L-fucose
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in 50 mM MES buffer (pH 6.0), at 60C
0.7 - 3.8
beta-D-galactose 1-phosphate
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0.75 - 38
beta-D-glucose 1-phosphate
3 - 447.6
D-galactose
0.6 - 36.8
D-glucose
23 - 32
glucose
0.14 - 9.4
phosphate
0.97 - 33
trehalose
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
210
alpha,alpha-trehalose
Bacillus selenitireducens
D6XSD4
recombinant enzyme, at pH 6.5 and 30C
51.4
alpha-D-arabinose
Caldanaerobacter subterraneus subsp. pacificus
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in 50 mM MES buffer (pH 6.0), at 60C
54
alpha-D-galactose
Caldanaerobacter subterraneus subsp. pacificus
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in 50 mM MES buffer (pH 6.0), at 60C
64.3
alpha-D-xylose
Caldanaerobacter subterraneus subsp. pacificus
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in 50 mM MES buffer (pH 6.0), at 60C
68.1
alpha-L-fucose
Caldanaerobacter subterraneus subsp. pacificus
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in 50 mM MES buffer (pH 6.0), at 60C
1.2 - 1.6
beta-D-galactose 1-phosphate
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7.4 - 660
beta-D-glucose 1-phosphate
0.5 - 113
D-galactose
4.2 - 86
D-glucose
660
glucose
Kocuria varians
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200
phosphate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.793
alpha-D-arabinose
Caldanaerobacter subterraneus subsp. pacificus
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in 50 mM MES buffer (pH 6.0), at 60C
17683
0.315
alpha-D-galactose
Caldanaerobacter subterraneus subsp. pacificus
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in 50 mM MES buffer (pH 6.0), at 60C
1087
3.17
alpha-D-xylose
Caldanaerobacter subterraneus subsp. pacificus
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in 50 mM MES buffer (pH 6.0), at 60C
2945
0.371
alpha-L-fucose
Caldanaerobacter subterraneus subsp. pacificus
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in 50 mM MES buffer (pH 6.0), at 60C
763
0.149 - 1.29
D-galactose
71
0.872 - 36
D-glucose
35
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
95
alpha,alpha-trehalose
recombinant enzyme, at pH 6.5 and 30C
0.0005 - 0.0012
fructose 2,6-diphosphate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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activity of trehalose phosphorylase in L3 larvae is 10times higher than in L4 larvae
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
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the pH optimum is slightly different for both reaction directions, with a lower optimum (about pH 5.5) for the synthesis reaction
6
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synthesis of trehalose
6 - 7
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synthesis of trehalose
7 - 7.5
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phosphorolysis of trehalose
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 7
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activity is over 90% in the range of pH 4.5 to 7.0
5.5 - 7.5
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stable
5.7 - 7.8
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about half-maximal activity at pH 5.7 and 7.8, trehalose synthesis
6 - 8
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about half-maximal activity at pH 6 and 8, phosphorolysis
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32
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both directions
37
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assay at
70
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both directions
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.4
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calculated from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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from root nodule of Glycine max
Manually annotated by BRENDA team
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and muscle, high activity
Manually annotated by BRENDA team
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and cuticle, high activity
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
170000
gel filtration
190000
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gel filtration
344000
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sucrose density gradient centrifugation
570000 - 580000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
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6 * 105000, SDS-PAGE
homodimer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using either 10% (w/v) PEG 4000, 0.1 M Tris-HCl pH 7.5, and 1% (v/v) 2-propanol or 10% (w/v) PEG 4000, 0.1 M Tris-HCl pH 7.5, and 1% (w/v) n-octyl-beta-D-glucoside
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8
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native enzyme, stable
489322
6 - 9
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stable
489328
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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stable below
40
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stable below, pH 7.0, at least 30 min
65
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no loss of activity after 1 h of incubation at 65C
72
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50% residual activity remains after 1 h of incubation at 72C
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme retains full activity during 5 months at -14C with several freezings and thawings, in presence of 2 mM phosphate buffer, pH 7.0, beta-D-glucose-1-phosphate and alpha-D-glucose-1-phosphate
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loss of activity when extracts are desalted by dialysis or passage through Sephadex G-25 in presence of water. When dialysis is carried out against 5 mM NaCl, glucose 6-phosphate, EDTA, or imidazole-HCl buffer, pH 7.0, the enzymatic activity is maintained only for a few h
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
14C,in presence of 2 mM phosphate buffer, pH 7.0, beta-D-glucose-1-phosphate and alpha-D-glucose-1-phosphate, enzyme retains full activity during 5 months with several freezings and thawings
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
HisTrap column chromatography
Ni-NTA agarose resin column chromatography
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Ni-Sepharose column chromatography and Superdex 200 gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
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expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli XL10 Gold cells
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L649G
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the mutant shows severely reduced production of beta-D-glucose 1-phosphate compared to the wild type enzyme
L649G/A693Q
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the mutant shows severely reduced production of beta-D-glucose 1-phosphate compared to the wild type enzyme
L649G/A693Q/W371Y
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the mutant shows severely reduced production of beta-D-glucose 1-phosphate compared to the wild type enzyme but displays a strict specificity (99%) for beta-D-galactose 1-phosphate as product
A431T
the mutant shows strongly decreased catalytic efficiency for D-glucose and decreased catalytic efficiency for D-galactose compared to the wild type enzyme
A440E
the mutant shows increased catalytic efficiency for D-glucose and wild type catalytic efficiency for D-galactose compared to the wild type enzyme
A440K
the mutant shows increased catalytic efficiencies for D-glucose and D-galactose compared to the wild type enzyme
A440M
the mutant shows increased catalytic efficiencies for D-glucose and D-galactose compared to the wild type enzyme
A440V
the mutant shows increased catalytic efficiencies for D-glucose and D-galactose compared to the wild type enzyme
A440V/N657Y
the mutant shows increased catalytic efficiencies for D-glucose and D-galactose compared to the wild type enzyme
A440V/R448S
the mutant shows increased catalytic efficiency for D-glucose and strongly increased catalytic efficiency for D-galactose compared to the wild type enzyme
N657D
the mutant shows increased catalytic efficiencies for D-glucose and D-galactose compared to the wild type enzyme
N657G
the mutant shows increased catalytic efficiencies for D-glucose and D-galactose compared to the wild type enzyme
N657I
the mutant shows approximate 2fold increase in affinity for D-galactose
N657L
the mutant shows increased catalytic efficiencies for D-glucose and D-galactose compared to the wild type enzyme
N657R
the mutant shows increased catalytic efficiencies for D-glucose and D-galactose compared to the wild type enzyme
N657Y
the mutant shows approximate 2fold increase in affinity for D-galactose
P588H
the mutant shows increased catalytic efficiencies for D-glucose and D-galactose compared to the wild type enzyme
R448D
the mutant shows increased catalytic efficiencies for D-glucose and D-galactose compared to the wild type enzyme
R448F
the mutant shows increased catalytic efficiencies for D-glucose and D-galactose compared to the wild type enzyme
R448N
the mutant shows increased catalytic efficiencies for D-glucose and D-galactose compared to the wild type enzyme
R448S
the mutant shows increased catalytic efficiencies for D-glucose and D-galactose compared to the wild type enzyme
R448S/N657Y
the mutant shows about wild type catalytic efficiencies for D-glucose and D-galactose
R448V
the mutant shows increased catalytic efficiencies for D-glucose and D-galactose compared to the wild type enzyme
additional information
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construction of chimeric phosphorylases of the kojibiose phosphorylase gene and the trehalose phosphorylase gene from Thermoanaerobacter brockii
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
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synthesis of trehalose from maltose by a coupled enzyme system with trehalose phosphorylase and maltose phosphorylase
Show AA Sequence (210 entries)
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