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Literature summary for 3.2.1.37 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
Search for more literature for 3.2.1.37

Activating Compound

Activating Compound Comment Organism Structure
Ba2+ 1.7fold activation of xylan-inducible enzyme, 1.1fold of xylose-inducible enzyme, at 0.25 mM Aspergillus versicolor
Ca2+ 2.2fold activation of xylan-inducible enzyme, 1.4fold of xylose-inducible enzyme, at 0.25 mM Aspergillus versicolor
Co2+ 1.4fold activation of xylan-inducible enzyme, 1.2fold of xylose-inducible enzyme, at 1 mM Aspergillus versicolor
Mg2+ 1.65fold activation of xylan-inducible enzyme, 1.2fold of xylose-inducible enzyme, at 0.25 mM Aspergillus versicolor
Mn2+ 1.2fold activation of xylan-inducible enzyme, 1.2fold of xylose-inducible enzyme, at 1 mM Aspergillus versicolor
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
Zn2+ 1.2fold activation of xylan-inducible enzyme, 1.3fold of xylose-inducible enzyme, at 1 mM Aspergillus versicolor

Inhibitors

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

KM Value [mM]

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

Metals/Ions

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Aspergillus versicolor
-
 two enzyme forms
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein O-linked sugars Aspergillus versicolor

Purification (Commentary)

Purification (Comment) Organism
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

Source Tissue Comment Organism Textmining
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]

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
-
 ?
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
-
 ?
4-nitrophenyl beta-D-xylopyranoside + H2O preferred substrate, specific for, xylan-inducible enzyme and xylose-inducible enzyme Aspergillus versicolor 4-nitrophenol + beta-D-xylose
-
 ?
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

Synonyms Comment Organism
beta-xylosidase
-
 Aspergillus versicolor

Temperature Optimum [°C]

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

Temperature Stability [°C]

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

pH Optimum

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

Ki Value [mM]

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

pI Value

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