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Information on EC 3.2.1.26 - beta-fructofuranosidase and Organism(s) Thermotoga maritima and UniProt Accession O33833
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3.2.1.26 beta-fructofuranosidaseIUBMB Comments
Substrates include sucrose; also catalyses fructotransferase reactions.
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Word Map
- 3.2.1.26
- maltase
- fructose
- border
-
brush
- disaccharidase
- starch
- mucosal
- jejunal
- urease
- villus
- catalase
- enterocytes
-
crypt
- aminopeptidase
-
sink
- biomass
- ileum
- potato
- amylase
- trehalase
- isomaltase
- apoplastic
- inulin
- fructans
-
brush-border
- alpha-glucosidase
-
suckling
- raffinose
- glucoamylase
- tuber
- duodenum
- bowel
-
rhizosphere
- phloem
- cellulase
- hexoses
- levan
- fructosyltransferase
-
small-intestinal
- acarbose
- fructooligosaccharides
- molasses
- fructokinase
-
carbohydrases
- microvillus
- inulinase
- synthesis
- stachyose
- nutrition
- biochars
- food industry
- industry
- agriculture
- pharmacology
- analysis
- biofuel production
-
photosynthate
- adp-glucose
The taxonomic range for the selected organisms is: Thermotoga maritima
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
invertase, sucrase, acid invertase, vacuolar invertase, cell wall invertase, yeast invertase, beta-fructofuranosidase, neutral invertase, beta-fructosidase, soluble acid invertase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acid invertase
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-
-
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Acid sucrose-6-phosphate hydrolase
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-
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alkaline invertase
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-
-
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beta-FFase
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-
-
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beta-fructofuranosidase
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-
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beta-fructosidase
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-
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beta-h-fructosidase
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-
-
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fructofuranosidase, beta-
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-
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fructosylinvertase
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glucosucrase
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-
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invertase
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-
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Invertase E1
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-
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invertin
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-
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maxinvert L 1000
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-
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Protein B46
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-
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saccharase
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-
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sucrase
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-
-
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Sucrase E1
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-
-
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Sucrose-6-phosphate hydrolase
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-
-
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Vacuolar invertase
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-
-
-
additional information
additional information
the enzyme belongs to glycoside hydrolase family GH-32
additional information
the enzyme belongs to the glycoside hydrolase family GH32
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
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PATHWAY SOURCE
PATHWAYS
BRENDA
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-, -, -
SYSTEMATIC NAME
IUBMB Comments
beta-D-fructofuranoside fructohydrolase
Substrates include sucrose; also catalyses fructotransferase reactions.
CAS REGISTRY NUMBER
COMMENTARY
9001-57-4
-
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
raffinose + H2O
alpha-D-galactosyl-1,6-alpha-D-glucose + D-fructose
-
-
-
?
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
high substrate concentrations and also high levels of the cleavage products glucose and fructose do not severly inhibit sucrose inversion
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60 - 98
-
60°C: about 35% of maximal activity, 98°C: about 20% of maximal activity
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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
-
the enzyme is bimodular with a five bladed beta-propeller catalytic domain linked to a beta-sandwich, three-dimensional structure, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
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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