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Information on EC 3.2.1.146 - beta-galactofuranosidase
for references in articles please use BRENDA:EC3.2.1.146
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EC Tree 3 Hydrolases
3.2 Glycosylases
3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
3.2.1.146 beta-galactofuranosidase
IUBMB Comments
The enzyme from Helminthosporium sacchari detoxifies helminthosporoside, a bis(digalactosyl)terpene produced by this fungus, by releasing its four molecules of bound galactose.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
showSynonyms
beta-galactofuranosidase, galf-ase, exo-beta-d-galactofuranosidase, beta-d-galactofuranosidase, orf1110, exo beta-d-galactofuranosidase, galf-specific galf-ase, orf0643, araf-ase, beta-d-galactofuranoside hydrolase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Araf-ase
beta-D-galactofuranosidase
beta-D-galactofuranosidase 1
beta-D-galactofuranosidase 3
beta-D-galactofuranosidase 4
exo beta-D-galactofuranosidase
exo-beta-D-galactofuranosidase
exo-beta-galactofuranosidase
-
-
-
-
galactofuranose-specific beta-D-galactofuranosidase
Galf-ase
Galf-specific Galf-ase
Galf-specific hydrolase
GfgA
GfgB
ORF0232
ORF1110
ORF2125
ORF2812
additional information
beta-D-galactofuranosidase
-
-
-
-
exo-beta-D-galactofuranosidase
-
-
-
-
galactofuranose-specific beta-D-galactofuranosidase
Streptomyces sp. JHA19 NRRL F-5140
A0A0K2SRV3
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hydrolysis of terminal non-reducing beta-D-galactofuranosides, releasing galactose
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis
hydrolysis of O-glycosyl bond
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
beta-D-galactofuranoside hydrolase
The enzyme from Helminthosporium sacchari detoxifies helminthosporoside, a bis(digalactosyl)terpene produced by this fungus, by releasing its four molecules of bound galactose.
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CAS REGISTRY NUMBER
COMMENTARY
52357-57-0
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-O-(p-nitrophenyl)-beta-D-galactofuranoside + H2O
p-nitrophenol + beta-D-galactofuranose
-
Substrates: -
Products: -
Products: -
?
1-O-methyl-beta-D-galactofuranoside + H2O
methanol + beta-D-galactofuranose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl 5-deoxy-beta-D-galactofuranoside + H2O
?
-
Substrates: substrate with low affinity
Products: -
Products: -
?
beta-D-(1->5) galactofuranose tetramer + H2O
beta-D-(1->5) galactofuranose trimer + D-galactose
-
Substrates: -
Products: -
Products: -
?
Helminthosporium sacchari toxin + H2O
Helminthosporium sacchari toxin + D-galactose
Helminthosporium saccharii
-
Substrates: enzyme cleaves only the terminal unit of galactose
Products: -
Products: -
?
methyl beta-D-galactofuranoside + H2O
?
-
Substrates: tritium-labeled, synthesized from D-galacturonic acid
Products: -
Products: -
?
methyl beta-D-galactofuranoside + H2O
methanol + beta-D-galactofuranose
-
Substrates: -
Products: -
Products: -
?
methyl-beta-D-galactofuranoside + H2O
methanol + D-galactose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-beta-D-galactofuranoside + H2O
p-nitrophenol + beta-D-galactofuranose
-
Substrates: -
Products: -
Products: -
?
peptidophosphogalactomannan + H2O
peptidophosphogalactomannan + D-galactose
-
Substrates: -
Products: -
Products: -
?
peptidophosphogalactomannan pP2GM + H2O
beta-D-galactofuranose
-
Substrates: -
Products: -
Products: -
?
tri-beta-D-(1,5)-galactofuranooligosaccharide + tetra-beta-D-(1,5)-galactofuranooligosaccharide + H2O
beta-D-galactofuranose
-
Substrates: a mixture of tri-beta-D-(1,5)-galactofuranooligosaccharide and tetra-beta-D-(1,5)-galactofuranooligosaccharide
Products: -
Products: -
?
4-nitrophenyl beta-D-galactofuranoside + H2O
4-nitrophenol + beta-D-galactofuranose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-galactofuranoside + H2O
4-nitrophenol + beta-D-galactofuranose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-galactofuranoside + H2O
4-nitrophenol + beta-D-galactofuranose
Aspergillus nidulans AKU89
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-galactofuranoside + H2O
4-nitrophenol + beta-D-galactofuranose
Substrates: maximum activity
Products: -
Products: -
?
4-nitrophenyl beta-D-galactofuranoside + H2O
4-nitrophenol + beta-D-galactofuranose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-galactofuranoside + H2O
4-nitrophenol + beta-D-galactofuranose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-galactofuranoside + H2O
4-nitrophenol + beta-D-galactofuranose
Streptomyces sp. JHA 19
-
Substrates: exclusive substrate specificity
Products: -
Products: -
?
4-nitrophenyl beta-D-galactofuranoside + H2O
4-nitrophenol + beta-D-galactofuranose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-galactofuranoside + H2O
4-nitrophenol + D-galactofuranose
-
Substrates: NaOAc buffer, pH 4.9, 37°C
Products: -
Products: -
?
4-nitrophenyl beta-D-galactofuranoside + H2O
4-nitrophenol + D-galactofuranose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-galactofuranoside + H2O
4-nitrophenol + D-galactofuranose
A0A0K2SQX3
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-galactofuranoside + H2O
4-nitrophenol + D-galactofuranose
Streptomyces chartreusis JHA19
A0A0K2SQX3
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-galactofuranoside + H2O
4-nitrophenol + D-galactofuranose
A0A0K2SQZ9
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-galactofuranoside + H2O
4-nitrophenol + D-galactofuranose
A0A0K2SRV3
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-galactofuranoside + H2O
4-nitrophenol + D-galactofuranose
Streptomyces sp. JHA19 NRRL F-5140
A0A0K2SRV3
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-galactofuranoside + H2O
4-nitrophenol + D-galactofuranose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-galactofuranoside + H2O
4-nitrophenol + D-galactofuranose
A0A0K2SQZ9
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-galactofuranoside + H2O
4-nitrophenol + D-galactofuranose
A0A0K2SQX4
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-galactofuranoside + H2O
4-nitrophenol + D-galactofuranose
A0A0K2SQX4
Substrates: -
Products: -
Products: -
?
beta-(1,5)-Galf3-PA + H2O
Gal-PA
Substrates: isoform GfgB
Products: -
Products: -
?
beta-(1,5)-Galf3-PA + H2O
Gal-PA + ?
Substrates: isoform GfgA
Products: -
Products: -
?
beta-(1,5)-Galf3-PA + H2O
Gal-PA + ?
Aspergillus nidulans AKU89
Substrates: isoform GfgA
Products: -
Products: -
?
beta-(1,6)-Galf3-PA + H2O
?
Substrates: isoform GfgB does not act efficiently on beta-(1,6)-Galf3-PA
Products: -
Products: -
?
beta-(1,6)-Galf3-PA + H2O
?
Aspergillus nidulans AKU89
Substrates: isoform GfgB does not act efficiently on beta-(1,6)-Galf3-PA
Products: -
Products: -
?
beta-(1,6)-Galf3-PA + H2O
Gal-PA
Substrates: isoform GfgA
Products: -
Products: -
?
galactomannan + H2O
?
A0A0K2SQX3
Substrates: release of galactose residue, galactomannan prepared from Aspergillus fumigatus
Products: -
Products: -
?
galactomannan + H2O
?
Streptomyces chartreusis JHA19
A0A0K2SQX3
Substrates: release of galactose residue, galactomannan prepared from Aspergillus fumigatus
Products: -
Products: -
?
galactomannan + H2O
?
A0A0K2SQZ9
Substrates: release of galactose residue, galactomannan prepared from Aspergillus fumigatus
Products: -
Products: -
?
galactomannan + H2O
?
A0A0K2SRV3
Substrates: release of galactose residue, galactomannan prepared from Aspergillus fumigatus
Products: -
Products: -
?
galactomannan + H2O
?
Streptomyces sp. JHA19 NRRL F-5140
A0A0K2SRV3
Substrates: release of galactose residue, galactomannan prepared from Aspergillus fumigatus
Products: -
Products: -
?
galactomannan + H2O
?
A0A0K2SQZ9
Substrates: release of galactose residue, galactomannan prepared from Aspergillus fumigatus
Products: -
Products: -
?
galactomannan + H2O
?
A0A0K2SQX4
Substrates: release of galactose residue, galactomannan prepared from Aspergillus fumigatus
Products: -
Products: -
?
galactomannan + H2O
?
A0A0K2SQX4
Substrates: release of galactose residue, galactomannan prepared from Aspergillus fumigatus
Products: -
Products: -
?
Galf3-PA + H2O
Galf2-PA + D-galactose
Substrates: -
Products: -
Products: -
?
p-nitrophenyl beta-D-galactofuranoside + H2O
p-nitrophenol + D-galactose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl beta-D-galactofuranoside + H2O
p-nitrophenol + D-galactose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl beta-D-galactofuranoside + H2O
p-nitrophenol + D-galactose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl beta-D-galactofuranoside + H2O
p-nitrophenol + D-galactose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl beta-D-galactofuranoside + H2O
p-nitrophenol + D-galactose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl beta-D-galactofuranoside + H2O
p-nitrophenol + D-galactose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl beta-D-galactofuranoside + H2O
p-nitrophenol + D-galactose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl beta-D-galactofuranoside + H2O
p-nitrophenol + D-galactose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl beta-D-galactofuranoside + H2O
p-nitrophenol + D-galactose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl beta-D-galactofuranoside + H2O
p-nitrophenol + D-galactose
-
Substrates: 4-nitrophenyl beta-D-fucofuranoside is not hydrolyzed
Products: -
Products: -
?
p-nitrophenyl beta-D-galactofuranoside + H2O
p-nitrophenol + D-galactose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl beta-D-galactofuranoside + H2O
p-nitrophenol + D-galactose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl beta-D-galactofuranoside + H2O
p-nitrophenol + D-galactose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl beta-D-galactofuranoside + H2O
p-nitrophenol + D-galactose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl beta-D-galactofuranoside + H2O
p-nitrophenol + D-galactose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl beta-D-galactofuranoside + H2O
p-nitrophenol + D-galactose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl beta-D-galactofuranoside + H2O
p-nitrophenol + D-galactose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl beta-D-galactofuranoside + H2O
p-nitrophenol + D-galactose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl beta-D-galactofuranoside + H2O
p-nitrophenol + D-galactose
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with alpha-L-arabinofuranoside, 4-nitrophenyl alpha-D-galactopyranoside, 4-nitrophenyl alpha-L-mannopyranoside, 4-nitrophenyl beta-mannopyranoside 4-nitrophenyl N-acetyl-D-glucosaminide, 4-nitrophenyl N-acetyl-D-galactosaminide, 4-nitrophenyl alpha-L-xylopyranoside, 4-nitrophenyl beta-D-xylopyranoside and 4-nitrophenyl beta-D-glucuronide
Products: -
Products: -
-
additional information
?
-
Substrates: no activity with alpha-L-arabinofuranoside, 4-nitrophenyl alpha-D-galactopyranoside, 4-nitrophenyl alpha-L-mannopyranoside, 4-nitrophenyl beta-mannopyranoside 4-nitrophenyl N-acetyl-D-glucosaminide, 4-nitrophenyl N-acetyl-D-galactosaminide, 4-nitrophenyl alpha-L-xylopyranoside, 4-nitrophenyl beta-D-xylopyranoside and 4-nitrophenyl beta-D-glucuronide
Products: -
Products: -
-
additional information
?
-
Aspergillus nidulans AKU89
Substrates: no activity with alpha-L-arabinofuranoside, 4-nitrophenyl alpha-D-galactopyranoside, 4-nitrophenyl alpha-L-mannopyranoside, 4-nitrophenyl beta-mannopyranoside 4-nitrophenyl N-acetyl-D-glucosaminide, 4-nitrophenyl N-acetyl-D-galactosaminide, 4-nitrophenyl alpha-L-xylopyranoside, 4-nitrophenyl beta-D-xylopyranoside and 4-nitrophenyl beta-D-glucuronide
Products: -
Products: -
-
additional information
?
-
Aspergillus nidulans AKU89
Substrates: no activity with alpha-L-arabinofuranoside, 4-nitrophenyl alpha-D-galactopyranoside, 4-nitrophenyl alpha-L-mannopyranoside, 4-nitrophenyl beta-mannopyranoside 4-nitrophenyl N-acetyl-D-glucosaminide, 4-nitrophenyl N-acetyl-D-galactosaminide, 4-nitrophenyl alpha-L-xylopyranoside, 4-nitrophenyl beta-D-xylopyranoside and 4-nitrophenyl beta-D-glucuronide
Products: -
Products: -
-
additional information
?
-
Substrates: no hydrolysis is detected of 4-nitrophenyl beta-Galp, 4-nitrophenyl beta-(1,5)-Galf3, 4-nitrophenyl alpha-arabinofuranoside, 4-nitrophenyl beta-D-glucoside, 4-nitrophenyl alpha-D-glucoside, 4-nitrophenyl beta-D-xyloside, 4-nitrophenyl beta-D-xylobioside, 4-nitrophenyl N-acetyl-beta-D-glucosaminide, 4-nitrophenyl beta-D-lactoside, 4-methylumbelliferyl-Galf3, 4-methylumbelliferyl-Galf4, 4-methylumbelliferyl-Galf5, 4-methylumbelliferyl-Galf6, octyl beta-D-galactofuranosyl-(1,6)-beta-D-galactofuranosyl-(1,5)-beta-D-galactofuranoside, octyl beta-D-galactofuranosyl-(1,5)-beta-D-galactofuranosyl-(1,6)-beta-D-galactofuranoside, and Galf-alpha-(1,2)-Man-alpha-(1,3)-Man-alpha-(1,6)-Man-beta-(1,4)-GlcNAc-beta-(1,4)-GlcNAc
Products: -
Products: -
-
additional information
?
-
-
Substrates: no hydrolysis of: 1-O-(p-nitrophenyl)-beta-D-galactopyranoside, 1-O-(p-nitrophenyl)-alpha-D-galactopyranoside,1-O-(p-nitrophenyl)-beta-N-acetyl-D-glucopyranosylamine, p-nitrophenyl-phosphocholine, p-nitrophenyl-phosphate, or bis-(p-nitrophenyl)-phosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: hydroxyl groups at C-2, C-3 and C-6 of the galactofuranoside are essential for interaction with the exo beta-D-galactofuranosidase. Methyl-2-deoxy-beta-D-lyxo-hexafuranoside is not hydrolyzed
Products: -
Products: -
?
additional information
?
-
-
Substrates: no hydrolysis of 4-methylumbelliferyl beta-D-galactofuranoside and methyl 5-deoxy-alpha-L-arabino-hexofuranoside
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme activity is highly dependent on the glycone and also the aglycone structure
Products: -
Products: -
?
additional information
?
-
A0A0K2SQX3
Substrates: four genes in Streptomyces sp. JHA19 encode Galf-ases. One enzyme (beta-D-galactofuranosidase 2) is a Galf-specific hydrolase, that shows no activity with alpha-L-arabinofuranosides, while the other three (beta-D-galactofuranosidases 1, 3, and 4) are active as alpha-L-arabinofuranosidases (Araf-ases, EC 3.2.1.55) and also as beta-D-galactofuranosidases
Products: -
Products: -
?
additional information
?
-
Streptomyces chartreusis JHA19
A0A0K2SQX3
Substrates: four genes in Streptomyces sp. JHA19 encode Galf-ases. One enzyme (beta-D-galactofuranosidase 2) is a Galf-specific hydrolase, that shows no activity with alpha-L-arabinofuranosides, while the other three (beta-D-galactofuranosidases 1, 3, and 4) are active as alpha-L-arabinofuranosidases (Araf-ases, EC 3.2.1.55) and also as beta-D-galactofuranosidases
Products: -
Products: -
?
additional information
?
-
A0A0K2SQZ9
Substrates: four genes in Streptomyces sp. JHA19 encode Galf-ases. One enzyme (beta-D-galactofuranosidase 2) is a Galf-specific hydrolase, that shows no activity with alpha-L-arabinofuranosides, while the other three (beta-D-galactofuranosidases 1, 3, and 4) are active as alpha-L-arabinofuranosidases (Araf-ases, EC 3.2.1.55) and also as beta-D-galactofuranosidases
Products: -
Products: -
?
additional information
?
-
Streptomyces sp. JHA 19
-
Substrates: no activity with 4-nitrophenyl alpha-L-arabinofuranoside, 4-nitrophenyl alpha-L-glucoside, 4-nitrophenyl beta-D-glucoside, 4-nitrophenyl beta-D-mannoside, 4-nitrophenyl beta-D-galactoside, 4-nitrophenyl N-acetylglucosamine, 4-nitrophenyl beta-D-xyloside, 4-nitrophenyl alpha-L-fucoside, 4-nitrophenyl alpha-L-arabinoside, 4-nitrophenyl alpha-L-rhamnoside, 4-nitrophenyl N-acetylgalactosamine, 4-nitrophenyl beta-D-glucuronic acid, and 4-nitrophenyl beta-D-ribofuranoside
Products: -
Products: -
-
additional information
?
-
A0A0K2SRV3
Substrates: four genes in Streptomyces sp. JHA19 encode Galf-ases. The beta-D-galactofuranosidase 2 enzyme is a Galf-specific hydrolase, that shows no activity with alpha-L-arabinofuranosides, while the other three are also active as alpha-L-arabinofuranosidases (Araf-ases, EC 3.2.1.55)
Products: -
Products: -
?
additional information
?
-
Streptomyces sp. JHA19 NRRL F-5140
A0A0K2SRV3
Substrates: four genes in Streptomyces sp. JHA19 encode Galf-ases. The beta-D-galactofuranosidase 2 enzyme is a Galf-specific hydrolase, that shows no activity with alpha-L-arabinofuranosides, while the other three are also active as alpha-L-arabinofuranosidases (Araf-ases, EC 3.2.1.55)
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is active with a galactofuranose-containing oligosaccharide termed GM
Products: -
Products: -
?
additional information
?
-
A0A0K2SQZ9
Substrates: four genes in Streptomyces sp. JHA19 encode Galf-ases. One enzyme (beta-D-galactofuranosidase 2) is a Galf-specific hydrolase, that shows no activity with alpha-L-arabinofuranosides, while the other three (beta-D-galactofuranosidases 1, 3, and 4) are active as alpha-L-arabinofuranosidases (Araf-ases, EC 3.2.1.55) and also as beta-D-galactofuranosidases
Products: -
Products: -
?
additional information
?
-
A0A0K2SQX4
Substrates: four genes in Streptomyces sp. JHA19 encode Galf-ases. One enzyme (beta-D-galactofuranosidase 2) is a Galf-specific hydrolase, that shows no activity with alpha-L-arabinofuranosides, while the other three (beta-D-galactofuranosidases 1, 3, and 4) are active as alpha-L-arabinofuranosidases (Araf-ases, EC 3.2.1.55) and also as beta-D-galactofuranosidases
Products: -
Products: -
?
additional information
?
-
A0A0K2SQX4
Substrates: four genes in Streptomyces sp. JHA19 encode Galf-ases. One enzyme (beta-D-galactofuranosidase 2) is a Galf-specific hydrolase, that shows no activity with alpha-L-arabinofuranosides, while the other three (beta-D-galactofuranosidases 1, 3, and 4) are active as alpha-L-arabinofuranosidases (Araf-ases, EC 3.2.1.55) and also as beta-D-galactofuranosidases
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme could be important for the processing of parasite glycoconjugates and thus for regulation of the interaction with the triatomine vector
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
peptidophosphogalactomannan + H2O
peptidophosphogalactomannan + D-galactose
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme could be important for the processing of parasite glycoconjugates and thus for regulation of the interaction with the triatomine vector
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,2:3,4-di-O-isopropylidene-6-S-(D-galactofuranosyl)-6-thio-alpha-D-galactopyranose
-
pH 4.9, 37°C, 80% enzyme activity at 0.3 mM, beyond that about 75% enzyme activity, 0.2-1.0 mM inhibitor
2-propyl 3-deoxy-4-S-(beta-D-galactofuranosyl)-4-thio-alpha-D-xylo-hexopyranoside
-
pH 4.9, 37°C, weak inhibitory activity, about 85% enzyme activity at 1 mM, 0.2-1.0 mM inhibitor
4-methylphenyl 1-thio-beta-D-galactofuranoside
-
low inhibitory activity with 30% inhibition at 0.25 mM
methyl 5-S-(beta-D-galactofuranosyl)-6-deoxy-5-thio-alpha-L-altrofuranoside
-
competitive inhibitor
methyl 5-S-(beta-D-galactofuranosyl)-6-deoxy-5-thio-beta-D-galactofuranoside
-
competitive inhibitor
methyl 6-S-(alpha-L-arabinofuranosyl)-6-thio-alpha-D-galactopyranoside
-
pH 4.9, 37°C, 80% enzyme activity at 0.3 mM, beyond that about 75% enzyme activity, 0.2-1.0 mM inhibitor
methyl 6-S-(beta-D-galactofuranosyl)-6-thio-alpha-D-galactopyranoside
-
pH 4.9, 37°C, 80% enzyme activity at 0.3 mM, beyond that about 65% enzyme activity, 0.2-1.0 mM inhibitor
methyl 6-S-(beta-D-galactofuranosyl)-6-thio-alpha-D-glucopyranoside
-
pH 4.9, 37°C, weak inhibitory activity, about 85% enzyme activity at 1 mM, 0.2-1.0 mM inhibitor
methyl 6-S-(beta-D-galactofuranosyl)-6-thio-beta-D-galactofuranoside
-
a (1->6)-linked thiodisaccharide formed by two galactofuranosyl units, synthesis and conformational analysis, overview. A competitive inhibitor of the beta-galactofuranosidase
D-galactono-1,4-lactone
-
competitive inhibition, 50% inhibition in the presence of 1 mM ZnCl2, CaCl2, NiCl2 or AgNO3
D-galactono-1,4-lactone
-
pH 4.9, 37°C, strong inhibitor, about 40% enzyme activity at 0.1 mM, 10% enzyme activity at 0.2 mM, less than 10% beyond 0.2 mM
D-galactono-1,4-lactone
-
resembles the transition state of the hydrolysis
additional information
-
no inhibitory activity at 0.2-1.0 mM of methyl 6-S-(alpha-L-arabinofuranosyl)-6-thio-alpha-D-glucopyranoside, pH 4.9, 37°C
-
additional information
-
no inhibition at concentrations up to 2.5 mM 4-methylphenyl 5-deoxy-1-thio-beta-D-galactofuranoside
-
additional information
-
synthesis of enantiomeric polyhydroxyalkylpyrrolidines from 1,3-dipolar cycloadducts by the 1,3-dipolar cycloaddition of sugar enones with azomethine ylides derived from natural amino acids, and evaluation as inhibitors of a beta-galactofuranosidase, overview. Reduction of the ketone carbonyl group of the cycloadducts, which possess a basic structure of bicyclic 6-(menthyloxy)hexahydropyrano[4,3-c]pyrrol-7(6H)one, affords a number of pyrrolidine-based bicyclic systems. The unprotected products are isolated as pyrrolidinium trifluoroacetates. Because of the furanose-like nature of the target trihydroxyalkyl pyrrolidines, these molecules are evaluated as inhibitors of the beta-galactofuranosidase from Penicillium fellutanum. The compounds ((2R,3S,3aR,6aS)-1-[(tert-butyloxy)carbonyl]-3-(1'(S),2'-diacetoxyethyl)-6-acetoxy-2-phenylhexahydro-1H-furo[3,4-b]pyrrole, (2S,3R,3aS,6aR)-1-[(tert-butyloxy)carbonyl]-3-(1'(R),2'-diacetoxyethyl)-6-acetoxy-2-phenylhexahydro-1H-furo[3,4-b]pyrrole, (2S,3R,4S,5R)-4-(1'(S),2'-diacetoxyethyl)-2,3-bis(acetoxymethyl)-1-[(tert-butyloxy)carbonyl]-5-phenylpyrrolidine, (2R,3S,4R,5S)-4-(1'(R),2'-diacetoxyethyl)-2,3-bis(acetoxymethyl)- 1-[(tert-butyloxy)carbonyl]-5-phenylpyrrolidine, (2S,3R,4S,5R)-4-(1'(S),2'-dihydroxyethyl)-2,3-bis(hydroxymethyl)-5-phenylpyrrolidinium trifluoroacetate, (2R,3S,4R,5S)-4-(1'(R),2'-dihydroxyethyl)-2,3-bis(hydroxymethyl)-5-phenylpyrrolidinium trifluoroacetate, (1R,3aR,4S,6R,6aS)-5-[(tert-butyloxy)carbonyl]-4-(hydroxymethyl)-6-phenylhexahydro-1H-furo[3,4-c]pyrrol-1-ol, (1S,3aS,4R,6S,6aR)-5-[(tert-butyloxy)carbonyl]-4-(hydroxymethyl)-6-phenylhexahydro-1H-furo[3,4-c]pyrrol-1-ol, (2S,3R,4S,5R)-1-[(tert-butyloxy)carbonyl]-2,3,4-tris-(hydroxymethyl)-5-phenylpyrrolidine, (2R,3S,4R,5S)-1-[(tert-butyloxy)carbony l]-2,3,4-tris-(hydroxymethyl)-5-phenylpyrrolidine, (2S,3R,4S,5R)-2,3,4-tris(hydroxymethyl)-5-phenylpyrrolidinium trifluoroacetate, and (2R,3S,4R,5S)-2,3,4-tris(hydroxymethyl)-5-phenylpyrrolidinium trifluoroacetate) show practically no inhibitory activity for concentration of pyrrolidines in the range of 0.1-1.6 mM. NMR structure analysis
-
additional information
-
synthesis of galactofuranosyl-(1->5)-thiodisaccharide glycomimetics as inhibitors of a beta-D-galactofuranosidase, NMR spectrometric structure determination and analysis, overview
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.29
4-nitrophenyl 5-deoxy-beta-D-galactofuranoside
-
in 66 mM NaOAc buffer (pH 4.9), at 37°C
0.31
4-nitrophenyl beta-D-galactofuranoside
-
in 66 mM NaOAc buffer (pH 4.9), at 37°C
1.2
4-nitrophenyl beta-D-galactofuranoside
isoform GfgB, at pH 5.0 and 37°C
4.4
4-nitrophenyl beta-D-galactofuranoside
A0A0K2SRV3
pH 5.5, 37°C, recombinant enzyme
5.2
4-nitrophenyl beta-D-galactofuranoside
isoform GfgA, at pH 5.0 and 37°C
6.8
4-nitrophenyl beta-D-galactofuranoside
pH 4.5, 37°C, recombinant enzyme
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
21.9
4-nitrophenyl beta-D-galactofuranoside
isoform GfgB, at pH 5.0 and 37°C
70.8
4-nitrophenyl beta-D-galactofuranoside
isoform GfgA, at pH 5.0 and 37°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
13.6
4-nitrophenyl beta-D-galactofuranoside
isoform GfgA, at pH 5.0 and 37°C
18.2
4-nitrophenyl beta-D-galactofuranoside
isoform GfgB, at pH 5.0 and 37°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.5
1H-benzimidazol-2-yl 1-thio-alpha-D-galactofuranoside
Streptomyces sp. JHA 19
-
at pH 4.5 and 37°C
2.23
methyl 5-S-(beta-D-galactofuranosyl)-6-deoxy-5-thio-alpha-L-altrofuranoside
-
pH 4.6, 37°C
0.15
methyl 5-S-(beta-D-galactofuranosyl)-6-deoxy-5-thio-beta-D-galactofuranoside
-
pH 4.6, 37°C
3.62
methyl 6-S-(beta-D-galactofuranosyl)-6-thio-beta-D-galactofuranoside
-
pH 4.6, 37°C
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3
1H-benzimidazol-2-yl 1-thio-alpha-D-galactofuranoside
Streptomyces sp. JHA 19
-
at pH 4.5 and 37°C
0.8
4-methylphenyl 1-thio-alpha-D-galactofuranoside
Streptomyces sp. JHA 19
-
at pH 4.5 and 37°C
5
pyrimidin-2-yl 1-thio-alpha-D-galactofuranoside
Streptomyces sp. JHA 19
-
at pH 4.5 and 37°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.23
with 4-nitrophenyl beta-D-galactofuranoside as substrate, at pH 5.0 and 25°C
1
-
extracellular polysaccharides of Penicillium digitatum as substrate
80.5
isoform GfgB, with 4-nitrophenyl beta-D-galactofuranoside as substrate, at pH 7.0 and 37°C
94.4
isoform GfgA, with 4-nitrophenyl beta-D-galactofuranoside as substrate, at pH 5.0 and 37°C
additional information
-
enzyme activity is low during logarithmic growth of a culture medium of Aspergillus fumigatus (about 0.2 to 0.4 U/liter) and increases during the lytical phase. Maximal activity is the lowest at higher pHs, being 1.4 U/liter at pH 7.1 to 7.4 and 2.6 U/liter at pH 7.4 and higher at low pHs, being 5.4 U/liter at pH 3.6 to 4.4 and 4.9 U/liter at pH 5.0. Activity is even higher when grown on 25 mM of glucose at pH 5.0, being 11.6 U/liter
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 4
3 - 6
-
enzyme from Penicillium fellutanum, sharp drop at pH 8.0 or above
4 - 4.5
4.5
5.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.5 - 5
Streptomyces sp. JHA 19
-
the optimum pH is comprised in a narrow range between 3.5 and 5, significantly decreasing above pH 5.0
4 - 5
highest activity between pH 4.0 and 5.0, substantial decrease in activity observed after incubation at pH 5.5 or higher
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
60
Streptomyces sp. JHA 19
-
for 20 min reactions, the optimal temperature is 60°C with a clear peak of activity. Temperatures above the optimum value result in dramatic loss of activity
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 40
substantial decrease in activity observed after incubation at temperatures greater than 30°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
isolated from soil in Kagawa University, Japan
A0A0K2SQX3
UniProt
brenda
Streptomyces chartreusis JHA19
isolated from soil in Kagawa University, Japan
A0A0K2SQX3
UniProt
brenda
isolated from soil in Kagawa University, Japan
A0A0K2SRV3
UniProt
brenda
Streptomyces sp. JHA19 NRRL F-5140
isolated from soil in Kagawa University, Japan
A0A0K2SRV3
UniProt
brenda
isolated from soil in Kagawa University, Japan
UniProt
brenda
isolated from soil in Kagawa University, Japan
A0A0K2SQZ9
UniProt
brenda
isolated from soil in Kagawa University, Japan
A0A0K2SQX4
UniProt
brenda
isolated from soil in Kagawa University, Japan
A0A0K2SQX4
UniProt
brenda
enzyme is induced in the presence of galactofuranoside containing glycoconjugates
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
filtered medium of stationary Penicillium fellutanum culture as source for substrate and enzyme
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
additional information
ORF0643 contains PA14, glycosyl hydro 2 N, glycosyl hydro and glycosyl hydro 2C domains
evolution
A0A0K2SQZ9
four genes in Streptomyces sp. JHA19 encode beta-D-galactofuranosidase (Galf-ases). One enzyme (beta-D-galactofuranosidase 2) is a Galf-specific hydrolase, that shows no activity with alpha-L-arabinofuranosides, while the other three (beta-D-galactofuranosidases 1, 3, and 4) are also active as alpha-L-arabinofuranosidases (Araf-ases, EC 3.2.1.55)
evolution
A0A0K2SQX3
four genes in Streptomyces sp. JHA19 encode Galf-ases. One enzyme (beta-D-galactofuranosidase 2) is a Galf-specific hydrolase, that shows no activity with alpha-L-arabinofuranosides, while the other three (beta-D-galactofuranosidases 1, 3, and 4) are also active as alpha-L-arabinofuranosidases (Araf-ases, EC 3.2.1.55)
evolution
A0A0K2SQX4
four genes in Streptomyces sp. JHA19 encode Galf-ases. One enzyme (beta-D-galactofuranosidase 2) is a Galf-specific hydrolase, that shows no activity with alpha-L-arabinofuranosides, while the other three (beta-D-galactofuranosidases 1, 3, and 4) are also active as alpha-L-arabinofuranosidases (Araf-ases, EC 3.2.1.55)
evolution
-
four genes in Streptomyces sp. JHA19 encode beta-D-galactofuranosidase (Galf-ases). One enzyme (beta-D-galactofuranosidase 2) is a Galf-specific hydrolase, that shows no activity with alpha-L-arabinofuranosides, while the other three (beta-D-galactofuranosidases 1, 3, and 4) are also active as alpha-L-arabinofuranosidases (Araf-ases, EC 3.2.1.55)
-
evolution
Streptomyces chartreusis JHA19
-
four genes in Streptomyces sp. JHA19 encode Galf-ases. One enzyme (beta-D-galactofuranosidase 2) is a Galf-specific hydrolase, that shows no activity with alpha-L-arabinofuranosides, while the other three (beta-D-galactofuranosidases 1, 3, and 4) are also active as alpha-L-arabinofuranosidases (Araf-ases, EC 3.2.1.55)
-
evolution
-
four genes in Streptomyces sp. JHA19 encode Galf-ases. One enzyme (beta-D-galactofuranosidase 2) is a Galf-specific hydrolase, that shows no activity with alpha-L-arabinofuranosides, while the other three (beta-D-galactofuranosidases 1, 3, and 4) are also active as alpha-L-arabinofuranosidases (Araf-ases, EC 3.2.1.55)
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). BDGF_ASPNC
Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
340
0
37999
Swiss-Prot
-
Q5B8D0_EMENI
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139)
645
0
72102
TrEMBL
-
Q5BAN5_EMENI
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139)
613
0
68506
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
150000
55000
70000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
-
stains with Schiff-reagent, binds to Concanavalin A-Sepharose, 17% carbohydrate content
glycoprotein
-
enzyme contains approximately 60 mannosyl residues per mol of enzyme, based on a MW of 70000 Da
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D183A
A0A0K2SRV3
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D201A
A0A0K2SRV3
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
D330A
A0A0K2SRV3
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
D336A
A0A0K2SRV3
site-directed mutagenesis, the mutant shows equal activity as the wild-type enzyme
D372A
A0A0K2SRV3
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D386A
A0A0K2SRV3
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D414A
A0A0K2SRV3
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D423A
A0A0K2SRV3
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
D482A
A0A0K2SRV3
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D500A
A0A0K2SRV3
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
D508A
A0A0K2SRV3
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D590A
A0A0K2SRV3
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D602A
A0A0K2SRV3
site-directed mutagenesis, the mutant shows slightly increased activity compared to the wild-type enzyme
E405A
A0A0K2SRV3
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
E464A
A0A0K2SRV3
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
E530A
A0A0K2SRV3
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
E592A
A0A0K2SRV3
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E594A
A0A0K2SRV3
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
D183A
Streptomyces sp. JHA19 NRRL F-5140
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
-
D201A
Streptomyces sp. JHA19 NRRL F-5140
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
-
D330A
Streptomyces sp. JHA19 NRRL F-5140
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
-
D336A
Streptomyces sp. JHA19 NRRL F-5140
-
site-directed mutagenesis, the mutant shows equal activity as the wild-type enzyme
-
D372A
Streptomyces sp. JHA19 NRRL F-5140
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
-
additional information
truncation of the PA14 domain of the enzyme (N-terminal 179 amino acid residues), ORF0643 Galf-ase lacking the PA14 domain exhibits about half activity compared with full-length ORF0643
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
40
purified recombinant detagged enzyme, pH 5.5, 10 min, stable up to, unstable above
50
60
Streptomyces sp. JHA 19
-
the enzyme is stable to temperature up to 60°C and to at least 4 freeze-thaw's cycles
30
isoform GfgB shows stable activity at temperatures less 30°C
30
the temperature stability of the enzyme decreases when incubated above 30°C for 1 h
50
A0A0K2SRV3
purified recombinant detagged enzyme, pH 5.5, 10 min, stable up to
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
culture filtrate of Penicillium fellutanum, DEAE-Sepharose, 4-aminophenyl 1-thio-beta-D-galactofuranoside-Sepharose
-
dialysed culture filtrate, Sepharose-Q, NeobarAQ-1, Neobar AQ-2, Superose-12, GNA-agarose
-
Ni-NTA resin column chromatography and HiTrap Q anion exchange chromatography
purified from Glucanex, a crude enzyme preparation isolated from Trichoderma harzianum
-
recombinant N-termially 2 x His6- and Nus-tagged enzyme from Escherichia coli strain BL21(DE3)CodonPlus, by nickel affinity chromatography, tag cleavage by HRV3C protease, followed by nickel affinity chromatography and ultrafiltration
recombinant N-terminally 2 x His6- and Nus-tagged enzyme from Escherichia coli strain BL21(DE3)CodonPlus, by nickel affinity chromatography, tag cleavage by HRV3C protease, followed by nickel affinity chromatography and ultrafiltration
recombinant N-termially 2 x His6- and Nus-tagged enzyme from Escherichia coli strain BL21(DE3)CodonPlus, by nickel affinity chromatography, tag cleavage by HRV3C protease, followed by nickel affinity chromatography and ultrafiltration
A0A0K2SQX3
recombinant N-termially 2 x His6- and Nus-tagged enzyme from Escherichia coli strain BL21(DE3)CodonPlus, by nickel affinity chromatography, tag cleavage by HRV3C protease, followed by nickel affinity chromatography and ultrafiltration
A0A0K2SQZ9
recombinant N-terminally 2 x His6- and Nus-tagged enzyme from Escherichia coli strain BL21(DE3)CodonPlus, by nickel affinity chromatography, tag cleavage by HRV3C protease, followed by nickel affinity chromatography and ultrafiltration
A0A0K2SRV3
recombinant N-terminally 2 x His6- and Nus-tagged enzyme from Escherichia coli strain BL21(DE3)CodonPlus, by nickel affinity chromatography, tag cleavage by HRV3C protease, followed by nickel affinity chromatography and ultrafiltration
recombinant N-terminally 2 x His6- and Nus-tagged enzyme from Escherichia coli strain BL21(DE3)CodonPlus, by nickel affinity chromatography, tag cleavage by HRV3C protease, followed by nickel affinity chromatography and ultrafiltration
A0A0K2SQX4
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli Rosetta (DE3) cells
orf0232, DNA and amino acid sequence determination and analysis, recombinant expression of N-terminally 2 x His6- and Nus-tagged enzyme in Escherichia coli strain BL21(DE3)CodonPlus
A0A0K2SQX4
orf0643, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of N-terminally 2 x His6- and Nus-tagged enzyme in Escherichia coli strain BL21(DE3)CodonPlus
orf1110, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, recombinant expression of N-terminally 2 x His6- and Nus-tagged enzyme in Escherichia coli strain BL21(DE3)CodonPlus
A0A0K2SRV3
orf2125, DNA and amino acid sequence determination and analysis, recombinant expression of N-termially 2 x His6- and Nus-tagged enzyme in Escherichia coli strain BL21(DE3)CodonPlus
A0A0K2SQX3
orf2812, DNA and amino acid sequence determination and analysis, recombinant expression of N-termially 2 x His6- and Nus-tagged enzyme in Escherichia coli strain BL21(DE3)CodonPlus
A0A0K2SQZ9
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
beta-galactofuranosidase activity is about 20fold decreased in the Aspergillus fumigatus mutant strain lacking calcineurin A after 96 h of growth
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
molecular biology
-
labeled substrate to detect galactofuranosidase activity, galactofuranose metabolism is a potential target for chemotherapeutic agents to fight microbial infections
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wallis, G.L.F.; Hemming, F.W.; Peberdy, J.F.
An extracellular beta-galactofuranosidase from Aspergillus niger and its use as a tool for glycoconjugate analysis
Biochim. Biophys. Acta
1525
19-28
2001
Aspergillus fumigatus, Aspergillus nidulans, Aspergillus niger, Aspergillus parasiticus, Aspergillus tamarii, Aspergillus versicolor
brenda
Chiocconi, A.; Marino, C.; de Lederkremer, R.M.
Synthesis of 4-nitrophenyl beta-D-fucofuranoside and beta-D-fucofuranosyl-(1->3)-D-mannopyranose: modified substrates for studies on catalytic requirements of beta-D-galactofuranosidase
Carbohydr. Res.
323
7-13
2000
Penicillium fellutanum
brenda
Miletti, L.C.; Marino, C.; Marino, K.; de Lederkremer, R.M.; Colli, W.; Alves, M.J.M.
Immobilized 4-aminophenyl 1-thio-beta-D-galactofuranoside as a matrix for affinity purification of an exo-beta-D-galactofuranosidase
Carbohydr. Res.
320
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Penicillium fellutanum
brenda
Van Bruggen van der Lugt, A.W.; Kamphuis, H.J.; de Ruiter, G.A.; Mischnik, P.; van Boom, J.H.; Rombouts, F.M.
New structural features of the antigenic extracellular polysaccharides of Penicillium and Aspergillus species revealed with exo-beta-D-galactofuranosidase
J. Bacteriol.
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Trichoderma harzianum
brenda
Cousin, M.A.; Notermans, S.; Hoogerhout, P; van Boom, J.H.
Detection of beta-galactofuranosidase production by Penicillium and Aspergillus species using 4-nitrophenyl beta-D-galactofuranosidase
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Aspergillus fumigatus, Aspergillus nidulans, Aspergillus niger, Aspergillus parasiticus, Aspergillus tamarii, Aspergillus versicolor, Penicillium expansum, Penicillium implicatum, Penicillium palitans, Penicillium simplicissimum, Penicillium tardum, Penicillium verrucosum, Penicillium viridicatum, Talaromyces funiculosus, Talaromyces islandicus, Talaromyces purpureogenus
brenda
Varela, O.; Marino, C.; de Lederkremer, R.M.
Synthesis of p-nitrophenyl beta-D-galactofuranoside. A convenient substrate for beta-galactofuranosidase
Carbohydr. Res.
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Penicillium fellutanum
brenda
Livingston, R.S.; Scheffer, R.P.
Conversion of Helminthosporium sacchari toxin to toxoids by beta-galactofuranosidase from Helminthosporium
Plant Physiol.
72
530-534
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Bipolaris maydis, Bipolaris victoriae, Bipolaris zeicola, Exserohilum turcicum, Helminthosporium saccharii
brenda
Rietschel-Berst, M.; Jentoft, N.H.; Rick, P.D.; Pletcher, C.; Fang, F.; Gander, J.E.
Extracellular exo-beta-galactofuranosidase from Penicillium charlesii
J. Biol. Chem.
252
3219-3226
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Penicillium charlesii
brenda
Gander, J.E; Fang, F.
Influence of 2-deoxy-D-Glucose on galactofuranosidase and peptidophosphogalactomannan synthesis in Penicillium charlesii
Biochem. Biophys. Res. Commun.
58
368-374
1974
Penicillium charlesii
brenda
Tuekam, B.A.; Park, Y.I.; Unkefer, C.J.; Gander, J.E.
Relationship of exo-beta-D-galactofuranosidase kinetic parameters to the number of phosphodiesters in Penicillium fellutanum peptidophosphogalactomannan: enzyme purification and kinetics of glycopeptide and galactofuran chain hydrolysis
Appl. Environ. Microbiol.
67
4648-4656
2001
Penicillium fellutanum
brenda
Chiocconi, A.; Marino, C.; Otal, E.; de Lederkremer, R.M.
Photoinduced electron transfer and chemical alpha-deoxygenation of D-galactono-1,4-lactone. Synthesis of 2-deoxy-D-lyxo-hexofuranosides
Carbohydr. Res.
337
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Penicillium fellutanum
brenda
Miletti, L.C.; Marino, K.; Marino, C.; Colli, W.; Alves, M.J.; de Lederkremer, R.M.
Evidence for exo beta-D-galactofuranosidase in Trypanosoma cruzi
Mol. Biochem. Parasitol.
127
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Trypanosoma cruzi
brenda
Mennink-Kersten, M.A.; Ruegebrink, D.; Wasei, N.; Melchers, W.J.; Verweij, P.E.
In vitro release by Aspergillus fumigatus of galactofuranose antigens, 1,3-beta-D-glucan, and DNA, surrogate markers used for diagnosis of invasive aspergillosis
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44
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Aspergillus fumigatus
brenda
Repetto, E.; Marino, C.; Uhrig, M.L.; Varela, O.
Thiodisaccharides with galactofuranose or arabinofuranose as terminal units: synthesis and inhibitory activity of an exo beta-D-galactofuranosidase
Bioorg. Med. Chem.
17
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Penicillium fellutanum
brenda
Bordoni, A.; Lima, C.; Marino, K.; de Lederkremer, R.M.; Marino, C.
Facile synthesis of methyl alpha- and beta-D-[6-(3)H]galactofuranosides from D-galacturonic acid. Substrates for the detection of galactofuranosidases
Carbohydr. Res.
343
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Talaromyces varians
brenda
Bordoni, A.; de Lederkremer, R.M.; Marino, C.
Synthesis of 5-deoxy-beta-D-galactofuranosides as tools for the characterization of beta-D-galactofuranosidases
Bioorg. Med. Chem.
18
5339-5345
2010
Penicillium fellutanum
brenda
Mennink-Kersten, M.A.; Ruegebrink, D.; Verweij, P.E.; Steinbach, W.J.
Calcineurin-dependent galactomannan release in Aspergillus fumigatus
Eur. J. Clin. Microbiol. Infect. Dis.
30
551-553
2011
Aspergillus fumigatus
brenda
Repetto, E.; Marino, C.; Varela, O.
Synthesis of the (1->6)-linked thiodisaccharide of galactofuranose: inhibitory activity against a beta-galactofuranosidase
Bioorg. Med. Chem.
21
3327-3333
2013
Penicillium fellutanum
brenda
Matsunaga, E.; Higuchi, Y.; Mori, K.; Yairo, N.; Toyota, S.; Oka, T.; Tashiro, K.; Takegawa, K.
Characterization of a PA14 domain-containing galactofuranose-specific beta-D-galactofuranosidase from Streptomyces sp.
Biosci. Biotechnol. Biochem.
81
1314-1319
2017
Streptomyces sp. JHA26 (A0A1Q2U3E4)
brenda
Oliveira Udry, G.A.; Repetto, E.; Vega, D.R.; Varela, O.
Synthesis of enantiomeric polyhydroxyalkylpyrrolidines from 1,3-dipolar cycloadducts. Evaluation as inhibitors of a beta-galactofuranosidase
J. Org. Chem.
81
4179-4189
2016
Penicillium fellutanum
brenda
Matsunaga, E.; Higuchi, Y.; Mori, K.; Yairo, N.; Oka, T.; Shinozuka, S.; Tashiro, K.; Izumi, M.; Kuhara, S.; Takegawa, K.
Identification and characterization of a novel galactofuranose-specific beta-D-galactofuranosidase from Streptomyces species
PLoS ONE
10
e0137230
2015
Streptomyces chartreusis (A0A0K2SQX3), Streptomyces chartreusis JHA19 (A0A0K2SQX3), Streptomyces sp. (A0A0K2SQZ9), Streptomyces sp. JHA19 (A0A0K2SRV3), Streptomyces sp. JHA19 NRRL F-5140 (A0A0K2SRV3), Streptomyces sp. NRRL F-5140 (A0A0K2SQZ9), Streptomyces viridochromogenes (A0A0K2SQX4), Streptomyces viridochromogenes JHA19 (A0A0K2SQX4)
brenda
Lo Fiego, M.; Marino, C.; Varela, O.
Synthesis of galactofuranosyl-(1->5)-thiodisaccharide glycomimetics as inhibitors of a beta-D-galactofuranosidase
RSC Adv.
5
45631-45640
2015
Penicillium fellutanum
-
brenda
Ota, R.; Okamoto, Y.; Vavricka, C.; Oka, T.; Matsunaga, E.; Takegawa, K.; Kiyota, H.; Izumi, M.
Chemo-enzymatic synthesis of p-nitrophenyl beta-D-galactofuranosyl disaccharides from Aspergillus sp. fungal-type galactomannan
Carbohydr. Res.
473
99-103
2019
Streptomyces sp.
brenda
Senicar, M.; Legentil, L.; Ferrieres, V.; Eliseeva, S.V.; Petoud, S.; Takegawa, K.; Lafite, P.; Daniellou, R.
Galactofuranosidase from JHA 19 Streptomyces sp. subcloning and biochemical characterization
Carbohydr. Res.
480
35-41
2019
Streptomyces sp. JHA 19
brenda
Bulmer, G.S.; Yuen, F.W.; Begum, N.; Jones, B.S.; Flitsch, S.L.; van Munster, J.M.
Biochemical characterization of a glycoside hydrolase family 43 beta-D-galactofuranosidase from the fungus Aspergillus niger
Enzyme Microb. Technol.
164
110170
2023
Aspergillus niger (A2QVZ0)
brenda
Matsunaga, E.; Tanaka, Y.; Toyota, S.; Yamada, H.; Oka, T.; Higuchi, Y.; Takegawa, K.
Identification and characterization of beta-D-galactofuranosidases from Aspergillus nidulans and Aspergillus fumigatus
J. Biosci. Bioeng.
131
1-7
2021
Aspergillus nidulans (Q5B8D0), Aspergillus nidulans (Q5BAN5), Aspergillus nidulans AKU89 (Q5B8D0), Aspergillus nidulans AKU89 (Q5BAN5)
brenda
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