Any feedback?
Information on EC 3.2.1.146 - beta-galactofuranosidase
for references in articles please use BRENDA:EC3.2.1.146Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.2.1.146 beta-galactofuranosidaseIUBMB Comments
The enzyme from Helminthosporium sacchari detoxifies helminthosporoside, a bis(digalactosyl)terpene produced by this fungus, by releasing its four molecules of bound galactose.
Specify your search results
Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
beta-galactofuranosidase, galf-ase, exo-beta-d-galactofuranosidase, beta-d-galactofuranosidase, exo beta-d-galactofuranosidase, orf1110, galf-specific galf-ase, orf0643, beta-d-galactofuranoside hydrolase, galf-specific hydrolase, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
ORF0232
ORF1110
ORF2125
ORF2812
additional information
beta-D-galactofuranosidase
-
-
-
-
exo-beta-D-galactofuranosidase
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
beta-D-(1->5) galactofuranose tetramer + H2O = beta-D-(1->5) galactofuranose trimer + D-galactose
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis
hydrolysis of O-glycosyl bond
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
52357-57-0
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
1-O-(p-nitrophenyl)-beta-D-galactofuranoside + H2O
p-nitrophenol + beta-D-galactofuranose
-
-
-
-
?
1-O-methyl-beta-D-galactofuranoside + H2O
methanol + beta-D-galactofuranose
-
-
-
-
?
4-nitrophenyl 5-deoxy-beta-D-galactofuranoside + H2O
?
-
substrate with low affinity
-
-
?
beta-D-(1->5) galactofuranose tetramer + H2O
beta-D-(1->5) galactofuranose trimer + D-galactose
-
-
-
?
Helminthosporium sacchari toxin + H2O
Helminthosporium sacchari toxin + D-galactose
Helminthosporium saccharii
-
enzyme cleaves only the terminal unit of galactose
-
?
methyl beta-D-galactofuranoside + H2O
?
-
tritium-labeled, synthesized from D-galacturonic acid
-
-
?
methyl beta-D-galactofuranoside + H2O
methanol + beta-D-galactofuranose
-
-
-
-
?
methyl-beta-D-galactofuranoside + H2O
methanol + D-galactose
-
-
-
?
p-nitrophenyl-beta-D-galactofuranoside + H2O
p-nitrophenol + beta-D-galactofuranose
-
-
-
-
?
peptidophosphogalactomannan + H2O
peptidophosphogalactomannan + D-galactose
-
-
-
?
peptidophosphogalactomannan pP2GM + H2O
beta-D-galactofuranose
-
-
-
-
?
tri-beta-D-(1,5)-galactofuranooligosaccharide + tetra-beta-D-(1,5)-galactofuranooligosaccharide + H2O
beta-D-galactofuranose
-
a mixture of tri-beta-D-(1,5)-galactofuranooligosaccharide and tetra-beta-D-(1,5)-galactofuranooligosaccharide
-
-
?
4-nitrophenyl beta-D-galactofuranoside + H2O
4-nitrophenol + beta-D-galactofuranose
-
-
-
-
?
4-nitrophenyl beta-D-galactofuranoside + H2O
4-nitrophenol + beta-D-galactofuranose
-
-
-
-
?
4-nitrophenyl beta-D-galactofuranoside + H2O
4-nitrophenol + beta-D-galactofuranose
-
-
-
-
?
4-nitrophenyl beta-D-galactofuranoside + H2O
4-nitrophenol + D-galactofuranose
-
-
-
-
?
4-nitrophenyl beta-D-galactofuranoside + H2O
4-nitrophenol + D-galactofuranose
-
NaOAc buffer, pH 4.9, 37°C
-
-
?
4-nitrophenyl beta-D-galactofuranoside + H2O
4-nitrophenol + D-galactofuranose
-
-
-
?
4-nitrophenyl beta-D-galactofuranoside + H2O
4-nitrophenol + D-galactofuranose
Streptomyces chartreusis JHA19
-
-
-
?
4-nitrophenyl beta-D-galactofuranoside + H2O
4-nitrophenol + D-galactofuranose
-
-
-
?
4-nitrophenyl beta-D-galactofuranoside + H2O
4-nitrophenol + D-galactofuranose
-
-
-
?
4-nitrophenyl beta-D-galactofuranoside + H2O
4-nitrophenol + D-galactofuranose
Streptomyces sp. JHA19 NRRL F-5140
-
-
-
?
4-nitrophenyl beta-D-galactofuranoside + H2O
4-nitrophenol + D-galactofuranose
-
-
-
?
4-nitrophenyl beta-D-galactofuranoside + H2O
4-nitrophenol + D-galactofuranose
-
-
-
?
4-nitrophenyl beta-D-galactofuranoside + H2O
4-nitrophenol + D-galactofuranose
-
-
-
?
4-nitrophenyl beta-D-galactofuranoside + H2O
4-nitrophenol + D-galactofuranose
-
-
-
?
galactomannan + H2O
?
release of galactose residue, galactomannan prepared from Aspergillus fumigatus
-
-
?
galactomannan + H2O
?
Streptomyces chartreusis JHA19
release of galactose residue, galactomannan prepared from Aspergillus fumigatus
-
-
?
galactomannan + H2O
?
release of galactose residue, galactomannan prepared from Aspergillus fumigatus
-
-
?
galactomannan + H2O
?
release of galactose residue, galactomannan prepared from Aspergillus fumigatus
-
-
?
galactomannan + H2O
?
Streptomyces sp. JHA19 NRRL F-5140
release of galactose residue, galactomannan prepared from Aspergillus fumigatus
-
-
?
galactomannan + H2O
?
release of galactose residue, galactomannan prepared from Aspergillus fumigatus
-
-
?
galactomannan + H2O
?
release of galactose residue, galactomannan prepared from Aspergillus fumigatus
-
-
?
galactomannan + H2O
?
release of galactose residue, galactomannan prepared from Aspergillus fumigatus
-
-
?
p-nitrophenyl beta-D-galactofuranoside + H2O
p-nitrophenol + D-galactose
-
-
-
?
p-nitrophenyl beta-D-galactofuranoside + H2O
p-nitrophenol + D-galactose
-
-
-
?
p-nitrophenyl beta-D-galactofuranoside + H2O
p-nitrophenol + D-galactose
-
-
-
?
p-nitrophenyl beta-D-galactofuranoside + H2O
p-nitrophenol + D-galactose
-
-
-
?
p-nitrophenyl beta-D-galactofuranoside + H2O
p-nitrophenol + D-galactose
-
-
-
?
p-nitrophenyl beta-D-galactofuranoside + H2O
p-nitrophenol + D-galactose
-
-
-
?
p-nitrophenyl beta-D-galactofuranoside + H2O
p-nitrophenol + D-galactose
-
-
-
?
p-nitrophenyl beta-D-galactofuranoside + H2O
p-nitrophenol + D-galactose
-
-
-
?
p-nitrophenyl beta-D-galactofuranoside + H2O
p-nitrophenol + D-galactose
-
-
-
?
p-nitrophenyl beta-D-galactofuranoside + H2O
p-nitrophenol + D-galactose
-
-
-
?
p-nitrophenyl beta-D-galactofuranoside + H2O
p-nitrophenol + D-galactose
-
-
-
?
p-nitrophenyl beta-D-galactofuranoside + H2O
p-nitrophenol + D-galactose
-
-
-
?
p-nitrophenyl beta-D-galactofuranoside + H2O
p-nitrophenol + D-galactose
-
-
-
?
p-nitrophenyl beta-D-galactofuranoside + H2O
p-nitrophenol + D-galactose
-
-
-
?
p-nitrophenyl beta-D-galactofuranoside + H2O
p-nitrophenol + D-galactose
-
-
-
?
p-nitrophenyl beta-D-galactofuranoside + H2O
p-nitrophenol + D-galactose
-
-
-
?
p-nitrophenyl beta-D-galactofuranoside + H2O
p-nitrophenol + D-galactose
-
-
-
?
p-nitrophenyl beta-D-galactofuranoside + H2O
p-nitrophenol + D-galactose
-
4-nitrophenyl beta-D-fucofuranoside is not hydrolyzed
-
-
?
p-nitrophenyl beta-D-galactofuranoside + H2O
p-nitrophenol + D-galactose
-
-
-
?
p-nitrophenyl beta-D-galactofuranoside + H2O
p-nitrophenol + D-galactose
-
-
-
?
p-nitrophenyl beta-D-galactofuranoside + H2O
p-nitrophenol + D-galactose
-
-
-
?
p-nitrophenyl beta-D-galactofuranoside + H2O
p-nitrophenol + D-galactose
-
-
-
?
p-nitrophenyl beta-D-galactofuranoside + H2O
p-nitrophenol + D-galactose
-
-
-
?
p-nitrophenyl beta-D-galactofuranoside + H2O
p-nitrophenol + D-galactose
-
-
-
?
p-nitrophenyl beta-D-galactofuranoside + H2O
p-nitrophenol + D-galactose
-
-
-
?
p-nitrophenyl beta-D-galactofuranoside + H2O
p-nitrophenol + D-galactose
-
-
-
?
p-nitrophenyl beta-D-galactofuranoside + H2O
p-nitrophenol + D-galactose
-
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
no hydrolysis of 4-methylumbelliferyl beta-D-galactofuranoside and methyl 5-deoxy-alpha-L-arabino-hexofuranoside
-
-
?
additional information
?
-
-
the enzyme activity is highly dependent on the glycone and also the aglycone structure
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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 active as alpha-L-arabinofuranosidases (Araf-ases, EC 3.2.1.55) and also as beta-D-galactofuranosidases
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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)
-
-
?
additional information
?
-
Streptomyces sp. JHA19 NRRL F-5140
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)
-
-
?
additional information
?
-
the enzyme is active with a galactofuranose-containing oligosaccharide termed GM
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
the enzyme could be important for the processing of parasite glycoconjugates and thus for regulation of the interaction with the triatomine vector
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
peptidophosphogalactomannan + H2O
peptidophosphogalactomannan + D-galactose
-
-
-
?
additional information
?
-
-
the enzyme could be important for the processing of parasite glycoconjugates and thus for regulation of the interaction with the triatomine vector
-
-
?
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
4.4
4-nitrophenyl beta-D-galactofuranoside
pH 5.5, 37°C, recombinant enzyme
6.8
4-nitrophenyl beta-D-galactofuranoside
pH 4.5, 37°C, recombinant enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1
-
extracellular polysaccharides of Penicillium digitatum as substrate
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
5.5
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enzyme is induced in the presence of galactofuranoside containing glycoconjugates
-
-
brenda
-
-
-
brenda
isolated from soil in Kagawa University, Japan
UniProt
brenda
isolated from soil in Kagawa University, Japan
UniProt
brenda
isolated from soil in Kagawa University, Japan
UniProt
brenda
isolated from soil in Kagawa University, Japan
UniProt
brenda
isolated from soil in Kagawa University, Japan
UniProt
brenda
isolated from soil in Kagawa University, Japan
UniProt
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
filtered medium of stationary Penicillium fellutanum culture as source for substrate and enzyme
brenda
Please 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
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
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)
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)
-
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)
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
150000
55000
70000
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D183A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D201A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
D330A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
D336A
site-directed mutagenesis, the mutant shows equal activity as the wild-type enzyme
D372A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D386A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D414A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D423A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
D482A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D500A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
D508A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D590A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D602A
site-directed mutagenesis, the mutant shows slightly increased activity compared to the wild-type enzyme
E405A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
E464A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
E530A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
E592A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E594A
site-directed mutagenesis, the mutant shows highly 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
-
D386A
Streptomyces sp. JHA19 NRRL F-5140
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
-
E464A
Streptomyces sp. JHA19 NRRL F-5140
-
site-directed mutagenesis, the mutant shows highly 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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
purified recombinant detagged enzyme, pH 5.5, 10 min, stable up to, unstable above
50
purified recombinant detagged enzyme, pH 5.5, 10 min, stable up to
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
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
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-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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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
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
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
176-182
1999
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.
174
6096-6102
1992
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
J. Appl. Bacteriol.
66
311-317
1989
Aspergillus fumigatus, Aspergillus nidulans, Aspergillus niger, Aspergillus parasiticus, Aspergillus tamarii, Aspergillus versicolor, Penicillium expansum, Talaromyces funiculosus, Penicillium implicatum, Talaromyces islandicus, Penicillium palitans, Talaromyces purpureogenus, Penicillium simplicissimum, Penicillium tardum, Penicillium verrucosum, Penicillium viridicatum
brenda
Varela, O.; Marino, C.; de Lederkremer, R.M.
Synthesis of p-nitrophenyl beta-D-galactofuranoside. A convenient substrate for beta-galactofuranosidase
Carbohydr. Res.
155
247-251
1986
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
1983
Bipolaris zeicola, Bipolaris maydis, Helminthosporium saccharii, Exserohilum turcicum, Bipolaris victoriae
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
1977
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
2119-2126
2002
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
85-88
2003
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
J. Clin. Microbiol.
44
1711-1718
2006
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
2703-2711
2009
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
1863-1869
2008
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 viridochromogenes (A0A0K2SQX4), Streptomyces sp. (A0A0K2SQZ9), Streptomyces sp. JHA19 (A0A0K2SRV3), Streptomyces chartreusis JHA19 (A0A0K2SQX3), Streptomyces sp. JHA19 NRRL F-5140 (A0A0K2SRV3), Streptomyces viridochromogenes JHA19 (A0A0K2SQX4), Streptomyces sp. NRRL F-5140 (A0A0K2SQZ9)
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
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 3.2.1.146)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
