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Literature summary extracted from

  • Knob, A.; Carmona, E.C.
    Purification and characterization of two extracellular xylanases from Penicillium sclerotiorum: a novel acidophilic xylanase (2009), Appl. Biochem. Biotechnol., 162, 429-443.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.2.1.8 2-mercaptoethanol
-
Penicillium sclerotiorum
3.2.1.8 dithiothreitol
-
Penicillium sclerotiorum
3.2.1.8 Pb(CH3COO)2 activates xylanase II and inhibits xylanase I at 10 mM Penicillium sclerotiorum
3.2.1.8 PMSF activates xylanase I, inhibits xylanase II Penicillium sclerotiorum
3.2.1.8 Sodium citrate activates Penicillium sclerotiorum

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.8 Co2+ complete inhibition of xylanase II at 10 mM, 50% at 2 mM, no inhibition of xylanase I Penicillium sclerotiorum
3.2.1.8 Cu2+ strong inhibition of xylanase I and xylanase II Penicillium sclerotiorum
3.2.1.8 EDTA inhibition of xylanase I and xylanase II Penicillium sclerotiorum
3.2.1.8 Hg2+ strong inhibition of xylanase I and xylanase II Penicillium sclerotiorum
3.2.1.8 NH4Cl activates xylanase I, inhibits xylanase II Penicillium sclerotiorum
3.2.1.8 Pb(CH3COO)2 activates xylanase II and inhibits xylanase I at 10 mM Penicillium sclerotiorum
3.2.1.8 PMSF activates xylanase I, inhibits xylanase II Penicillium sclerotiorum
3.2.1.8 SDS strong inhibition of xylanase I and xylanase II, complete inhibition at 2 mM and 10 mM, respectively Penicillium sclerotiorum
3.2.1.8 Zn2+ inhibition of xylanase I and xylanase II Penicillium sclerotiorum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.8 additional information
-
additional information kinetics of isozymes xylanase I and xylanase II Penicillium sclerotiorum

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.2.1.8 extracellular
-
Penicillium sclerotiorum
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.8 Ba2+ activates xylanase I by 10-16% at 2-10 mM Penicillium sclerotiorum
3.2.1.8 Ca2+ activates both isozyme by about 20% at 2-10 mM Penicillium sclerotiorum
3.2.1.8 Mn2+ activates xylanase II by 2.25fold Penicillium sclerotiorum
3.2.1.8 additional information no effect by NaCl and MgSO4 at 10 mM Penicillium sclerotiorum
3.2.1.8 NH4Cl activates xylanase I, inhibits xylanase II Penicillium sclerotiorum

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.8 23800
-
xylanase I, gel filtration Penicillium sclerotiorum
3.2.1.8 23900
-
1 * 23900, xylanase I, SDS-PAGE, 1 * 33100, xylanase II, SDS-PAGE Penicillium sclerotiorum
3.2.1.8 30800
-
xylanase II, gel filtration Penicillium sclerotiorum
3.2.1.8 33100
-
1 * 23900, xylanase I, SDS-PAGE, 1 * 33100, xylanase II, SDS-PAGE Penicillium sclerotiorum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.8 beta-1,4-xylan + H2O Penicillium sclerotiorum
-
?
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.8 Penicillium sclerotiorum
-
isozymes xylanase I and II
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.2.1.8 glycoprotein xylanase I and xylanase II Penicillium sclerotiorum

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.8 native xylanase I and xylanase II 2.4-2.5fold by anion exchange chromatography and gel filtration to homogeneity Penicillium sclerotiorum

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.8 240.9
-
purified isozyme xylanase II Penicillium sclerotiorum
3.2.1.8 249.1
-
purified isozyme xylanase I Penicillium sclerotiorum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.8 beta-1,4-xylan + H2O
-
Penicillium sclerotiorum ?
-
?
3.2.1.8 beta-1,4-xylan + H2O the enzyme cleaves the internal beta-1,4-bonds in the xylan backbone at non-modified residues, yielding different chain-length-substituted xylooligosaccharides Penicillium sclerotiorum ?
-
?
3.2.1.8 additional information specificities of xylanases against birchwood xylan, oat spelt xylan, carboxymethylcellulose, Overview Penicillium sclerotiorum ?
-
?

Subunits

EC Number Subunits Comment Organism
3.2.1.8 monomer 1 * 23900, xylanase I, SDS-PAGE, 1 * 33100, xylanase II, SDS-PAGE Penicillium sclerotiorum

Synonyms

EC Number Synonyms Comment Organism
3.2.1.8 endo-beta-(1,4)-xylanase
-
Penicillium sclerotiorum
3.2.1.8 xylanase I
-
Penicillium sclerotiorum
3.2.1.8 xylanase II
-
Penicillium sclerotiorum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.8 50
-
xylanase I Penicillium sclerotiorum
3.2.1.8 55
-
xylanase II Penicillium sclerotiorum

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.8 45
-
half-life of both isozymes is about 210 min Penicillium sclerotiorum
3.2.1.8 50
-
half-life of both isozymes is about 80 min Penicillium sclerotiorum
3.2.1.8 55
-
half-life of both isozymes is 50 min Penicillium sclerotiorum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.8 2.5
-
xylanase I Penicillium sclerotiorum
3.2.1.8 4.5
-
xylanase II Penicillium sclerotiorum

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.2.1.8 1.5 6.5 activity range, 80% of maximal activity by xylanase I at pH 1.6 and pH 3.0, inactive at pH 7.0, profile, overview Penicillium sclerotiorum
3.2.1.8 2.5 7.5 activity range, 60% of maximal activity by xylanase II at pH 3.5 and pH 7.0, 25% at pH 2.5, profile, overview Penicillium sclerotiorum

General Information

EC Number General Information Comment Organism
3.2.1.8 metabolism key enzyme in beta-1,4-xylan degradation, which involves several hydrolases, overview Penicillium sclerotiorum