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Literature summary for 3.2.1.8 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

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

Inhibitors

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

KM Value [mM]

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

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Penicillium sclerotiorum
-
-

Metals/Ions

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

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

Organism

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

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein xylanase I and xylanase II Penicillium sclerotiorum

Purification (Commentary)

Purification (Comment) Organism
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]

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
beta-1,4-xylan + H2O
-
Penicillium sclerotiorum ?
-
?
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 ?
-
?
additional information specificities of xylanases against birchwood xylan, oat spelt xylan, carboxymethylcellulose, Overview Penicillium sclerotiorum ?
-
?

Subunits

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

Synonyms

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

Temperature Optimum [°C]

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

Temperature Stability [°C]

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

pH Optimum

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

pH Range

pH Minimum pH Maximum Comment Organism
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
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

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