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Information on EC 3.2.1.146 - beta-galactofuranosidase
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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.
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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, 
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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
ORF0232
ORF1110
ORF2125
ORF2812
additional information
beta-D-galactofuranosidase
-
-
-
-
exo-beta-D-galactofuranosidase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
beta-D-(1->5) galactofuranose tetramer + H2O = beta-D-(1->5) galactofuranose trimer + D-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
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
-
-
?
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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
-
-
?
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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
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
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 4
3 - 6
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enzyme from Penicillium fellutanum, sharp drop at pH 8.0 or above
4 - 4.5
5.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enzyme is induced in the presence of galactofuranoside containing glycoconjugates
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brenda
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brenda
isolated from soil in Kagawa University, Japan
UniProt
brenda
isolated from soil in Kagawa University, Japan
UniProt
brenda