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Literature summary for 3.1.1.73 extracted from

  • Dodd, D.; Kocherginskaya, S.A.; Spies, M.A.; Beery, K.E.; Abbas, C.A.; Mackie, R.I.; Cann, I.K.
    Biochemical analysis of a beta-D-xylosidase and a bifunctional xylanase-ferulic acid esterase from a xylanolytic gene cluster in Prevotella ruminicola 23 (2009), J. Bacteriol., 191, 3328-3338.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
Xyn10D-Fae1A amplicons cloned into the pGEM-T vector via TA cloning and subcloned in frame with the hexahistidine-encoding sequence of a modified pET-28a expression vector by replacing the NdeI-XhoI polylinker, expressed in Escherichia coli BL-21 CodonPlus (DE3) RIL competent cells Prevotella ruminicola

Protein Variants

Protein Variants Comment Organism
E280S the ferulic acid esterase activity increases 3fold. Capacity for Xyn10D-Fae1A to depolymerize oat spelt xylan is attenuated Prevotella ruminicola
S629A the ferulic acid esterase activity for Xyn10D-Fae1A is attenuated. Depolymerizes xylan to an extent similar to the that of wild-type Prevotella ruminicola

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
84000
-
1 * 84000, hexahistidine fusion protein, SDS-PAGE, exists either as monomer or homodimer in solution Prevotella ruminicola
84000
-
2 * 84000, gel filtration, exists either as monomer or homodimer in solution Prevotella ruminicola
124000
-
gel filtration Prevotella ruminicola

Organism

Organism UniProt Comment Textmining
Prevotella ruminicola
-
-
-
Prevotella ruminicola 23
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Xyn10D-Fae1A purified by metal affinity chromatography and gel filtration Prevotella ruminicola

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1-naphthyl butyrate + H2O esterase activity Prevotella ruminicola butyric acid + 1-naphthol
-
?
1-naphthyl butyrate + H2O esterase activity Prevotella ruminicola 23 butyric acid + 1-naphthol
-
?
feruloyl xylooligosaccharide + H2O degrees of polymerization (X3 to X6) are hydrolyzed mostly to xylobiose, with some xylose also being released Prevotella ruminicola ferulic acid + xylooligosaccharide
-
?
feruloyl xylooligosaccharide + H2O degrees of polymerization (X3 to X6) are hydrolyzed mostly to xylobiose, with some xylose also being released Prevotella ruminicola 23 ferulic acid + xylooligosaccharide
-
?
feruloylated oat spelt xylan + H2O xylanase activity Prevotella ruminicola ferulic acid + ?
-
?
feruloylated oat spelt xylan + H2O xylanase activity Prevotella ruminicola 23 ferulic acid + ?
-
?
methyl ferulate + H2O
-
Prevotella ruminicola ferulic acid + methanol
-
?
methyl ferulate + H2O
-
Prevotella ruminicola 23 ferulic acid + methanol
-
?
additional information no xylobiose hydrolysis to xylose Prevotella ruminicola ?
-
?
additional information no xylobiose hydrolysis to xylose Prevotella ruminicola 23 ?
-
?

Subunits

Subunits Comment Organism
homodimer 2 * 84000, gel filtration, exists either as monomer or homodimer in solution Prevotella ruminicola
monomer 1 * 84000, hexahistidine fusion protein, SDS-PAGE, exists either as monomer or homodimer in solution Prevotella ruminicola

Synonyms

Synonyms Comment Organism
xylanase-ferulic acid esterase
-
Prevotella ruminicola
Xyn10D-Fae1A
-
Prevotella ruminicola

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
-
Prevotella ruminicola

General Information

General Information Comment Organism
physiological function Xyn10D-Fae1A possesses both endo-beta-1,4-xylanase and ferulic acid esterase activities, Glu280 is an important residue for xylanase activity and Ser629 is an important residue for ferulic acid esterase activity. When incubated in combination with Xyn10D-Fae1A, the beta-D-glucosidase Xyl3A improves the release of xylose monomers from a hemicellulosic xylan substrate, thus these two enzymes function synergistically to depolymerize xylan. Two catalytic domains for Xyn10D-Fae1A are functionally coupled Prevotella ruminicola