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Literature summary for 3.2.1.37 extracted from

  • Saxena, S.; Fierobe, H.P.; Gaudin, C.; Guerlesquin, F.; Belaich, J.P.
    Biochemical properties of a beta-xylosidase from Clostridium cellulolyticum (1995), Appl. Environ. Microbiol., 61, 3509-3512.
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.4
-
p-nitrophenyl beta-D-xyloside
-
Ruminiclostridium cellulolyticum

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
43000
-
SDS-PAGE Ruminiclostridium cellulolyticum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
xylan + H2O Ruminiclostridium cellulolyticum low activity beta-D-xylose + ?
-
?
xylan + H2O Ruminiclostridium cellulolyticum 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 + ?
-
?
xylobiose + H2O Ruminiclostridium cellulolyticum
-
beta-D-xylose + D-xylose
-
?

Organism

Organism UniProt Comment Textmining
Ruminiclostridium cellulolyticum
-
-
-

Purification (Commentary)

Purification (Comment) Organism
to homogeneity by 3step chromatography techniques Ruminiclostridium cellulolyticum

Source Tissue

Source Tissue Comment Organism Textmining
cell culture enzyme production most induced in xylan medium Ruminiclostridium cellulolyticum
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
15.1
-
-
Ruminiclostridium cellulolyticum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
p-nitrophenyl alpha-L-arabinofuranoside + H2O low activity Ruminiclostridium cellulolyticum p-nitrophenol + alpha-L-arabinofuranose
-
?
p-nitrophenyl beta-D-xylopyranoside + H2O
-
Ruminiclostridium cellulolyticum p-nitrophenol + beta-D-xylopyranose
-
?
xylan + H2O low activity Ruminiclostridium cellulolyticum beta-D-xylose + ?
-
?
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 Ruminiclostridium cellulolyticum beta-D-xylose + ?
-
?
xylobiose + H2O
-
Ruminiclostridium cellulolyticum beta-D-xylose + D-xylose
-
?
xylopentaose + H2O extend of hydrolysis varies with chain length of the substrate Ruminiclostridium cellulolyticum beta-D-xylose + ?
-
?
xylotetraose + H2O acts by inverting the anomeric configuration Ruminiclostridium cellulolyticum xylotriose + beta-D-xylose
-
?
xylotriose + H2O
-
Ruminiclostridium cellulolyticum beta-D-xylose + xylobiose
-
?

Subunits

Subunits Comment Organism
monomer 1 * 43000, SDS-PAGE Ruminiclostridium cellulolyticum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
35
-
-
Ruminiclostridium cellulolyticum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
Ruminiclostridium cellulolyticum

pH Stability

pH Stability pH Stability Maximum Comment Organism
6
-
no activity below Ruminiclostridium cellulolyticum