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Literature summary 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)

EC Number Cloned (Comment) Organism
3.1.1.73 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
3.2.1.37 ecxpression in Escherichia coli Prevotella ruminicola

Protein Variants

EC Number Protein Variants Comment Organism
3.1.1.73 E280S the ferulic acid esterase activity increases 3fold. Capacity for Xyn10D-Fae1A to depolymerize oat spelt xylan is attenuated Prevotella ruminicola
3.1.1.73 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
3.2.1.37 D269A no catalytic activity Prevotella ruminicola
3.2.1.37 D269N no catalytic activity Prevotella ruminicola
3.2.1.37 E594Q activity similar to wild-type Prevotella ruminicola
3.2.1.37 E616A about 5% of wild-type activity Prevotella ruminicola
3.2.1.37 R149L no catalytic activity Prevotella ruminicola
3.2.1.37 Y237F less than 10% of wild-type activity Prevotella ruminicola

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.37 1.8
-
 4-nitrophenyl-beta-D-xylopyranoside wild-type, pH 5.0, 37°C Prevotella ruminicola
3.2.1.37 2
-
 4-nitrophenyl-beta-D-xylopyranoside mutant E594Q, pH 5.0, 37°C Prevotella ruminicola
3.2.1.37 3.9
-
 4-nitrophenyl-beta-D-xylopyranoside mutant Y237F, pH 5.0, 37°C Prevotella ruminicola
3.2.1.37 18
-
 4-nitrophenyl-beta-D-xylopyranoside mutant E616A, pH 5.0, 37°C Prevotella ruminicola

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.1.73 84000
-
 1 * 84000, hexahistidine fusion protein, SDS-PAGE, exists either as monomer or homodimer in solution Prevotella ruminicola
3.1.1.73 84000
-
 2 * 84000, gel filtration, exists either as monomer or homodimer in solution Prevotella ruminicola
3.1.1.73 124000
-
 gel filtration Prevotella ruminicola

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.73 Prevotella ruminicola
-
-
-
3.1.1.73 Prevotella ruminicola 23
-
-
-
3.2.1.37 Prevotella ruminicola D5EY15 isoform Xyl3A
-

Purification (Commentary)

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.73 1-naphthyl butyrate + H2O esterase activity Prevotella ruminicola butyric acid + 1-naphthol
-
 ?
3.1.1.73 1-naphthyl butyrate + H2O esterase activity Prevotella ruminicola 23 butyric acid + 1-naphthol
-
 ?
3.1.1.73 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
-
 ?
3.1.1.73 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
-
 ?
3.1.1.73 feruloylated oat spelt xylan + H2O xylanase activity Prevotella ruminicola ferulic acid + ?
-
 ?
3.1.1.73 feruloylated oat spelt xylan + H2O xylanase activity Prevotella ruminicola 23 ferulic acid + ?
-
 ?
3.1.1.73 methyl ferulate + H2O
-
 Prevotella ruminicola ferulic acid + methanol
-
 ?
3.1.1.73 methyl ferulate + H2O
-
 Prevotella ruminicola 23 ferulic acid + methanol
-
 ?
3.1.1.73 additional information no xylobiose hydrolysis to xylose Prevotella ruminicola ?
-
 ?
3.1.1.73 additional information no xylobiose hydrolysis to xylose Prevotella ruminicola 23 ?
-
 ?
3.2.1.37 4-nitrophenyl alpha-L-arabinofuranoside + H2O poor substrate Prevotella ruminicola 4-nitrophenol + alpha-L-arabinofuranose
-
 ?
3.2.1.37 4-nitrophenyl beta-D-xylopyranoside + H2O
-
 Prevotella ruminicola 4-nitrophenol + beta-D-xylose
-
 ?
3.2.1.37 additional information no substrate: 4-nitrophenly-beta-D-glucopyranoside. When incubated in combination with bifunctional xylanase-ferulic acid esterase Xyn10D-Fae1A, Xyl3A improves the release of xylose monomers from a hemicellulosic xylan substrate, suggesting that these two enzymes function synergistically to depolymerize xylan Prevotella ruminicola ?
-
 ?
3.2.1.37 xylobiose + H2O
-
 Prevotella ruminicola 2 D-xylose
-
 ?
3.2.1.37 xylohexaose + H2O sole products released are xylose monomers Prevotella ruminicola 6 D-xylose
-
 ?
3.2.1.37 xylopentaose + H2O sole products released are xylose monomers Prevotella ruminicola 5 D-xylose
-
 ?
3.2.1.37 xylotetraose + 3 H2O
-
 Prevotella ruminicola 4 D-xylose
-
 ?
3.2.1.37 xylotriose + H2O
-
 Prevotella ruminicola 3 D-xylose
-
 ?

Subunits

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

Synonyms

EC Number Synonyms Comment Organism
3.1.1.73 xylanase-ferulic acid esterase
-
 Prevotella ruminicola
3.1.1.73 Xyn10D-Fae1A
-
 Prevotella ruminicola
3.2.1.37 Xyl3A
-
 Prevotella ruminicola

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.2.1.37 1.6
-
 4-nitrophenyl-beta-D-xylopyranoside mutant Y237F, pH 5.0, 37°C Prevotella ruminicola
3.2.1.37 3.3
-
 4-nitrophenyl-beta-D-xylopyranoside mutant E616A, pH 5.0, 37°C Prevotella ruminicola
3.2.1.37 9.7
-
 4-nitrophenyl-beta-D-xylopyranoside wild-type, pH 5.0, 37°C Prevotella ruminicola
3.2.1.37 10
-
 4-nitrophenyl-beta-D-xylopyranoside mutant E594Q, pH 5.0, 37°C Prevotella ruminicola

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.73 5
-
-
 Prevotella ruminicola

General Information

EC Number General Information Comment Organism
3.1.1.73 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
3.2.1.37 physiological function when incubated in combination with bifunctional xylanase-ferulic acid esterase Xyn10D-Fae1A, Xyl3A improves the release of xylose monomers from a hemicellulosic xylan substrate, suggesting that these two enzymes function synergistically to depolymerize xylan Prevotella ruminicola

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.2.1.37 0.2
-
 4-nitrophenyl-beta-D-xylopyranoside mutant E616A, pH 5.0, 37°C Prevotella ruminicola
3.2.1.37 0.41
-
 4-nitrophenyl-beta-D-xylopyranoside mutant Y237F, pH 5.0, 37°C Prevotella ruminicola
3.2.1.37 5
-
 4-nitrophenyl-beta-D-xylopyranoside mutant E594Q, pH 5.0, 37°C Prevotella ruminicola
3.2.1.37 5.4
-
 4-nitrophenyl-beta-D-xylopyranoside wild-type, pH 5.0, 37°C Prevotella ruminicola