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EC Tree
IUBMB Comments Substrates include sucrose; also catalyses fructotransferase reactions.
The taxonomic range for the selected organisms is: Thermotoga maritima The enzyme appears in selected viruses and cellular organisms
Synonyms
invertase, sucrase, acid invertase, vacuolar invertase, cell wall invertase, yeast invertase, beta-fructofuranosidase, neutral invertase, beta-fructosidase, soluble acid invertase,
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Acid sucrose-6-phosphate hydrolase
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alkaline invertase
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beta-fructofuranosidase
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beta-fructosidase
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beta-h-fructosidase
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fructofuranosidase, beta-
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fructosylinvertase
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Sucrose-6-phosphate hydrolase
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Vacuolar invertase
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additional information
the enzyme belongs to glycoside hydrolase family GH-32
additional information
the enzyme belongs to the glycoside hydrolase family GH32
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hydrolysis of terminal non-reducing beta-D-fructofuranoside residues in beta-D-fructofuranosides
hydrolysis of terminal non-reducing beta-D-fructofuranoside residues in beta-D-fructofuranosides
double-displacement reaction mechanism, cleavage of beta-fructopyranosidic linkages involving a nucleophilic aspartate and a catalytic glutamic acid acting as general acid/base, structure of the active site substrate binding pocket possessing three binding subsites
hydrolysis of terminal non-reducing beta-D-fructofuranoside residues in beta-D-fructofuranosides
the enzyme reaction mechanism with retention of the anomeric configuration at the site of cleavage, active site structure
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hydrolysis of O-glycosyl bond
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beta-D-fructofuranoside fructohydrolase
Substrates include sucrose; also catalyses fructotransferase reactions.
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inulin + H2O
D-fructose + ?
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raffinose + H2O
alpha-D-galactosyl-1,6-alpha-D-glucose + D-fructose
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sucrose + H2O
D-glucose + D-fructose
inulin + H2O
fructose + ?
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raffinose + H2O
fructose + melibiose
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sucrose + H2O
D-fructose + D-glucose
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sucrose + H2O
D-glucose + D-fructose
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sucrose + H2O
D-glucose + D-fructose
best substrate
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?
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sucrose + H2O
D-glucose + D-fructose
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?
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additional information
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high substrate concentrations and also high levels of the cleavage products glucose and fructose do not severly inhibit sucrose inversion
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4.2 - 7.1
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more than 50% of maximal activity between pH 4.2 and pH 7.1
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60 - 98
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60°C: about 35% of maximal activity, 98°C: about 20% of maximal activity
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SwissProt
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additional information
three-dimensional structure analysis
additional information
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three-dimensional structure analysis
additional information
the enzyme is bimodular with a five bladed beta-propeller catalytic domain linked to a beta-sandwich, three-dimensional structure, overview
additional information
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the enzyme is bimodular with a five bladed beta-propeller catalytic domain linked to a beta-sandwich, three-dimensional structure, overview
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purified recombinant His-tagged wild-type and selenomethionine-labeled enzyme, vapour diffusion method, 11 mg/ml wild-type enzyme in 15% PEG 1000, 150 mM Li2SO4, and 100 mM sodium citrate, pH 4.2, 3 days, 20°C, conditions for the selenomethionine-labeled enzyme: 8 mg/ml protein in 17% PEG 1000, 50 mM Li2SO4, 1% isopropanol, and 100 mM sodium citrate, pH 4.2, X-ray diffraction structure determination and analysis at 2.0-2.2 A resolution
purified recombinant inactivated mutant enzyme E190D in complex with substrate raffinose, hanging drop vapour diffusion method, 11 mg/ml protein in 15-17% PEG 1000, 150 mM Li2SO4, and 100 mM sodium citrate, pH 4.2, soaking of crystals in 5 mM substrate solution, flash freezing at -173°C, X-ray diffraction structure determination and analysis at a.87 A resolution, structure modelling, no successful crystal structure analysis with crystals of wild-type enzyme and mutant E190A built by the same method
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E190A
site-directed mutagenesis, inactivated mutant
E190D
site-directed mutagenesis, inactivated mutant
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60
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14 days, 59% loss of activity
70
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14 days, 76% loss of activity
80
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5 h, retains at least 85% of its initial activity
85
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5 h, 15% loss of activity
90
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5 h, substantial loss of activity
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recombinant His-tagged wild-type and selenomethionine-labeled enzyme from Escherichia coli strain BL21(DE3)
recombinant His-tagged wild-type enzyme and mutants E190A and E190D from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
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DNA and amino acid sequence determination, expression of His-tagged wild-type and selenomethionine-labeled enzyme in Escherichia coli strain BL21(DE3)
expression of His-tagged wild-type enzyme and mutants E190A and E190D in Escherichia coli strain BL21(DE3)
expression in Escherichia coli
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Liebl, W.; Brem, D.; Gotschlich, A.
Analysis of the gene for beta-fructosidase (invertase, inulinase) of the hyperthermophilic bacterium Thermotoga maritima, and characterization of the enzyme expressed in Escherichia coli
Appl. Microbiol. Biotechnol.
50
55-64
1998
Thermotoga maritima, Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
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Alberto, F.; Jordi, E.; Henrissat, B.; Czjzek, M.
Crystal structure of inactivated Thermotoga maritima invertase in complex with the trisaccharide substrate raffinose
Biochem. J.
395
457-462
2006
Thermotoga maritima (O33833), Thermotoga maritima
brenda
Alberto, F.; Bignon, C.; Sulzenbacher, G.; Henrissat, B.; Czjzek, M.
The three-dimensional structure of invertase (beta-fructosidase) from Thermotoga maritima reveals a bimodular arrangement and an evolutionary relationship between retaining and inverting glycosidases
J. Biol. Chem.
279
18903-18910
2004
Thermotoga maritima (O33833), Thermotoga maritima, Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589 (O33833)
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