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Literature summary extracted from

  • Hebraud, M.; Fevre, M.
    Purification and characterization of an extracellular beta-xylosidase from rumen anaerobic fungus Neocallimastix frontalis (1990), FEMS Microbiol. Lett., 72, 11-16.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.37 Cu2+ 50% inhibition Neocallimastix frontalis
3.2.1.37 Hg2+ complete inhibition Neocallimastix frontalis
3.2.1.37 p-chloromercuribenzoate complete inhibition Neocallimastix frontalis
3.2.1.37 SDS complete inhibition Neocallimastix frontalis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.37 122
-
 p-nitrophenyl beta-D-xylopyranoside
-
 Neocallimastix frontalis

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.2.1.37 extracellular
-
 Neocallimastix frontalis
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.37 Ca2+
-
 Neocallimastix frontalis
3.2.1.37 Co2+
-
 Neocallimastix frontalis
3.2.1.37 Mg2+
-
 Neocallimastix frontalis
3.2.1.37 Mn2+ considerable increase of activity Neocallimastix frontalis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.37 90000
-
 2 * 90000, SDS-PAGE Neocallimastix frontalis
3.2.1.37 180000
-
 gel filtration, SDS-PAGE Neocallimastix frontalis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.37 beta-1,4-xylan + H2O Neocallimastix frontalis
-
 beta-D-xylose + ?
-
 ?
3.2.1.37 xylan + H2O Neocallimastix frontalis complete degration of xylan requires synergistic action of two types of enzyme, endo-1,4-xylanase to form xylooligosaccharides and beta-D-xylosidase, which hydrolyses xylooligosaccharides to xylose beta-D-xylose + ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.37 Neocallimastix frontalis
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.37 to homogeneity by 2step chromatography and isoelectric focusing Neocallimastix frontalis

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.2.1.37 zoospore zoospore culture, induction of enzyme production highest in cellubiose/xylan medium Neocallimastix frontalis
-

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 4.3
-
-
 Neocallimastix frontalis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.37 beta-1,4-xylan + H2O
-
 Neocallimastix frontalis beta-D-xylose + ?
-
 ?
3.2.1.37 p-nitrophenyl beta-D-xylopyranoside + H2O
-
 Neocallimastix frontalis p-nitrophenol + beta-D-xylopyranose
-
 ?
3.2.1.37 xylan + H2O complete degration of xylan requires synergistic action of two types of enzyme, endo-1,4-xylanase to form xylooligosaccharides and beta-D-xylosidase, which hydrolyses xylooligosaccharides to xylose Neocallimastix frontalis beta-D-xylose + ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.37 dimer 2 * 90000, SDS-PAGE Neocallimastix frontalis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.37 35
-
-
 Neocallimastix frontalis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.37 35
-
 rapid decrease of activity above and below Neocallimastix frontalis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.37 6 6.5
-
 Neocallimastix frontalis

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.2.1.37 6 6.5 stable during 1 h at 20°C Neocallimastix frontalis