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Literature summary 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)

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

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.8 Ag+
-
 Ruminococcus flavefaciens
3.2.1.8 Cu2+
-
 Ruminococcus flavefaciens
3.2.1.8 Zn2+
-
 Ruminococcus flavefaciens

Metals/Ions

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

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.8 Ruminococcus flavefaciens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.8
-
 Ruminococcus flavefaciens

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.8 260
-
-
 Ruminococcus flavefaciens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.8 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 ?
3.2.1.8 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 ?
-
 ?
3.2.1.8 xyloheptaose + H2O
-
 Ruminococcus flavefaciens xylobiose + xylotriose + xylotetraose
-
 ?
3.2.1.8 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 ?
3.2.1.8 xylooctaose + H2O
-
 Ruminococcus flavefaciens xylobiose + xylotriose + xylotetraose
-
 ?
3.2.1.8 xylopentaose + H2O
-
 Ruminococcus flavefaciens additional information xylobiose + xylotriose ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.8 50
-
 catalytic domains XYL-A and XYL-C Ruminococcus flavefaciens

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.8 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