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Literature summary extracted from

  • Andrade, S.d.V.; Polizeli, M.d.; Terenzi, H.F.; Jorge, J.A.
    Effect of carbon source on the biochemical properties of beta-xylosidases produced by Aspergillus versicolor (2004), Process Biochem., 39, 1931-1938.
No PubMed abstract available

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.2.1.37 Ba2+ 1.7fold activation of xylan-inducible enzyme, 1.1fold of xylose-inducible enzyme, at 0.25 mM Aspergillus versicolor
3.2.1.37 Ca2+ 2.2fold activation of xylan-inducible enzyme, 1.4fold of xylose-inducible enzyme, at 0.25 mM Aspergillus versicolor
3.2.1.37 Co2+ 1.4fold activation of xylan-inducible enzyme, 1.2fold of xylose-inducible enzyme, at 1 mM Aspergillus versicolor
3.2.1.37 Mg2+ 1.65fold activation of xylan-inducible enzyme, 1.2fold of xylose-inducible enzyme, at 0.25 mM Aspergillus versicolor
3.2.1.37 Mn2+ 1.2fold activation of xylan-inducible enzyme, 1.2fold of xylose-inducible enzyme, at 1 mM Aspergillus versicolor
3.2.1.37 additional information xylose and xylan as only carbon source induce expression of enzyme form 1 and enzyme form 2, respectively, prevented by cycloheximide Aspergillus versicolor
3.2.1.37 Zn2+ 1.2fold activation of xylan-inducible enzyme, 1.3fold of xylose-inducible enzyme, at 1 mM Aspergillus versicolor

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.37 4-nitrophenyl-beta-D-xylopyranoside
-
Aspergillus versicolor
3.2.1.37 Al3+ 80% inhibition of xylan-inducible enzyme, 10% of xylose-inducible enzyme, at 1 mM Aspergillus versicolor
3.2.1.37 Cu2+ 64% inhibition of xylan-inducible enzyme, 79% of xylose-inducible enzyme, at 1 mM Aspergillus versicolor
3.2.1.37 D-xylose product inhibition Aspergillus versicolor
3.2.1.37 Hg2+ complete inhibition of xylan-inducible enzyme and xylose-inducible enzyme, at 1 mM Aspergillus versicolor
3.2.1.37 additional information addition of glucose to the growth medium suppresses enzyme expression Aspergillus versicolor

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.37 0.19
-
4-nitrophenyl-beta-D-xylopyranoside pH 6.5, 45°C, xylan-inducible enzyme Aspergillus versicolor
3.2.1.37 0.32
-
4-nitrophenyl-beta-D-xylopyranoside pH 5.6, 40°C, xylose-inducible enzyme Aspergillus versicolor

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.37 additional information no effect by 2-mercaptoethanol Aspergillus versicolor

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.37 60000
-
xylose-inducible enzyme, gel filtration Aspergillus versicolor
3.2.1.37 100000
-
xylan-inducible enzyme, gel filtration Aspergillus versicolor

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.37 Aspergillus versicolor
-
two enzyme forms
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.2.1.37 glycoprotein O-linked sugars Aspergillus versicolor

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.37 two forms of native enzyme from mycelium by ion exchange chromatography, xylose-inducible enzyme form 11.3fold, xylan.inducible enzyme form 12.3fold, ammonium sulfate, and gel filtration Aspergillus versicolor

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.2.1.37 mycelium xylose and xylan as only carbon source induce expression of enzyme form 1 and enzyme form 2, respectively, addition of glucose suppresses enzyme expression Aspergillus versicolor
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.37 additional information
-
the xylan-inducible enzyme shows higher catalytic efficiency than the xylose-inducible enzyme Aspergillus versicolor
3.2.1.37 51.3
-
purified xylan-inducible enzyme Aspergillus versicolor
3.2.1.37 59.6
-
purified xylose-inducible enzyme Aspergillus versicolor

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.37 4-nitrophenyl beta-D-galactopyranoside + H2O xylan-inducible enzyme shows 10% of activity with 4-nitrophenyl-beta-D-xylopyranoside, and xylose-inducible enzyme 2% Aspergillus versicolor 4-nitrophenol + beta-D-galactose
-
?
3.2.1.37 4-nitrophenyl beta-D-glucopyranoside + H2O xylan-inducible enzyme shows 18% of activity with 4-nitrophenyl-beta-D-xylopyranoside, and xylose-inducible enzyme 8% Aspergillus versicolor 4-nitrophenol + beta-D-glucose
-
?
3.2.1.37 4-nitrophenyl beta-D-xylopyranoside + H2O preferred substrate, specific for, xylan-inducible enzyme and xylose-inducible enzyme Aspergillus versicolor 4-nitrophenol + beta-D-xylose
-
?
3.2.1.37 4-nitrophenyl-alpha-L-arabinopyranoside + H2O xylan-inducible enzyme shows 18% of activity with 4-nitrophenyl-beta-D-xylopyranoside, and xylose-inducible enzyme 26% Aspergillus versicolor 4-nitrophenol + alpha-L-arabinose
-
?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.37 beta-xylosidase
-
Aspergillus versicolor

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.37 40
-
xylose-inducible enzyme Aspergillus versicolor
3.2.1.37 45
-
xylan-inducible enzyme Aspergillus versicolor

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.37 55
-
half-life of the xylan-inducible enzyme is 9 min, of the xylose-inducible enzyme 18 min Aspergillus versicolor

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.37 5.5
-
xylan-inducible enzyme Aspergillus versicolor
3.2.1.37 6
-
xylose-inducible enzyme Aspergillus versicolor

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.2.1.37 2
-
4-nitrophenyl-beta-D-xylopyranoside pH 6.5, 45°C, xylan-inducible enzyme Aspergillus versicolor
3.2.1.37 5.3
-
4-nitrophenyl-beta-D-xylopyranoside pH 5.6, 40°C, xylose-inducible enzyme Aspergillus versicolor

pI Value

EC Number Organism Comment pI Value Maximum pI Value
3.2.1.37 Aspergillus versicolor xylose-inducible enzyme, isoelectric focusing
-
5.6
3.2.1.37 Aspergillus versicolor xylan-inducible enzyme, isoelectric focusing
-
6.5