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Literature summary for 3.2.1.8 extracted from

  • Garcia-Campayo, V.; McCrae, S.I.; Zhang, J.X.; Flint, H.J.; Wood, T.M.
    Mode of action, kinetic properties and physicochemical characterization of two different domains of a bifunctional (1->4)-beta-D-xylanase from Ruminococcus flavefaciens expressed separately in Escherichia coli (1993), Biochem. J., 296, 235-243.
No PubMed abstract available

Cloned(Commentary)

Cloned (Comment) Organism
two catalytic domains XYLA-A and XYL-C, expressed separately as truncated gene products from lacZ fusion in Escherichia coli Ruminococcus flavefaciens

Inhibitors

Inhibitors Comment Organism Structure
Ag+
-
Ruminococcus flavefaciens
Cu2+
-
Ruminococcus flavefaciens
Zn2+
-
Ruminococcus flavefaciens

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ slightly enhances activity of the catalytic domain XYLA-C2, no effect on activity of the catalytic domain XYLA-A1 Ruminococcus flavefaciens
Mg2+ slightly enhances activity of the catalytic domain XYLA-C2, no effect on activity of the catalytic domain XYLA-A1 Ruminococcus flavefaciens

Organism

Organism UniProt Comment Textmining
Ruminococcus flavefaciens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Ruminococcus flavefaciens

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
260
-
-
Ruminococcus flavefaciens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1,4-beta-D-xylan + H2O oat spelt xylan Ruminococcus flavefaciens additional information with oat spelt xylan activity of the catalytic domain XYL-A1 is restricted to regions where xylopyranosyl residues do not carry arabinofuranosyl substituents, catalytic domain XYLA-C2 is able to release heterooligosaccharides carrying arabinofuranosyl residues ?
additional information neither the catalytic domain XYLA-A1 nor XYLA-C2 can hydrolyze oligomers of DP 4 and lower. Except in the case of xylohexaose the rate of attack of different xylooligosaccharides by XYLA-A1 is higher than that shown by XYLA-C2 Ruminococcus flavefaciens ?
-
?
xyloheptaose + H2O
-
Ruminococcus flavefaciens xylobiose + xylotriose + xylotetraose
-
?
xylohexaose + H2O
-
Ruminococcus flavefaciens additional information xylotriose is produced by the catalytic domain XYLA-A1, xylobiose, xylotriose and xylotetraose are produced by the catalytic domain XYLA-A1 ?
xylooctaose + H2O
-
Ruminococcus flavefaciens xylobiose + xylotriose + xylotetraose
-
?
xylopentaose + H2O
-
Ruminococcus flavefaciens additional information xylobiose + xylotriose ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
catalytic domains XYL-A and XYL-C Ruminococcus flavefaciens

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
55
-
half-life of the catalytic domain XYLA-A1 is 20 min, half-life of the catalytic domain XYLA-C2 is 50 min Ruminococcus flavefaciens