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Literature summary extracted from

  • Soren, D.; Jana, M.; Sengupta, S.; Ghosh, A.K.
    Purification and characterization of a low molecular weight endo-xylanase from mushroom Termitomyces clypeatus (2009), Appl. Biochem. Biotechnol., 162, 373-389.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.8 1-Fluoro-2,4-dinitrobenzene
-
Termitomyces clypeatus
3.2.1.8 Ag+ strong inhibition Termitomyces clypeatus
3.2.1.8 carbodiimide
-
Termitomyces clypeatus
3.2.1.8 EDTA
-
Termitomyces clypeatus
3.2.1.8 EGTA
-
Termitomyces clypeatus
3.2.1.8 Fe2+ strong inhibition Termitomyces clypeatus
3.2.1.8 HgCl2 strong inhibition Termitomyces clypeatus
3.2.1.8 iminodiborane
-
Termitomyces clypeatus
3.2.1.8 additional information CuSO4, NaN3, MgSO4, and iodoacetic acid do not show any inhibitory effect Termitomyces clypeatus
3.2.1.8 N-bromosuccimide
-
Termitomyces clypeatus
3.2.1.8 N-bromosuccinimide strong inhibition Termitomyces clypeatus
3.2.1.8 PCMB
-
Termitomyces clypeatus
3.2.1.8 trans-1,2-diaminocyclohexane-N',N',N',N'-tetraacetic acid strong inhibition Termitomyces clypeatus

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 Termitomyces clypeatus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.8 12000
-
gel filtration Termitomyces clypeatus

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.8 Termitomyces clypeatus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.8 native enzyme 28.8fold by ammonium sulfate fractionation and gel filtration to homogeneity Termitomyces clypeatus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.2.1.8 mycelium grown in submerged medium with oat spelt xylan Termitomyces clypeatus
-

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 6917
-
purified enzyme Termitomyces clypeatus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.8 beta-1,4-xylan + H2O best substrate is oat spelt xylan Termitomyces clypeatus ?
-
?
3.2.1.8 additional information substrate specificity, active with arabinoxylan and arabinogalactan, least specificity towards amylopectin and guar gum, overview Termitomyces clypeatus ?
-
?

Subunits

EC Number Subunits Comment Organism
3.2.1.8 monomer 1 x * 12000, SDS-PAGE Termitomyces clypeatus

Synonyms

EC Number Synonyms Comment Organism
3.2.1.8 endo-xylanase
-
Termitomyces clypeatus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.8 50
-
-
Termitomyces clypeatus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.8 5
-
-
Termitomyces clypeatus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.2.1.8 3 10 profile, overview Termitomyces clypeatus

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.2.1.8 6.5
-
purified enzyme, most stable at Termitomyces clypeatus