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Literature summary for 3.2.1.37 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

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

KM Value [mM]

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

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Neocallimastix frontalis
-
-

Metals/Ions

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
beta-1,4-xylan + H2O Neocallimastix frontalis
-
beta-D-xylose + ?
-
?
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

Organism UniProt Comment Textmining
Neocallimastix frontalis
-
-
-

Purification (Commentary)

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

Source Tissue

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

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.3
-
-
Neocallimastix frontalis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
beta-1,4-xylan + H2O
-
Neocallimastix frontalis beta-D-xylose + ?
-
?
p-nitrophenyl beta-D-xylopyranoside + H2O
-
Neocallimastix frontalis p-nitrophenol + beta-D-xylopyranose
-
?
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

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

Temperature Optimum [°C]

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

Temperature Stability [°C]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6 6.5
-
Neocallimastix frontalis

pH Stability

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