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Literature summary extracted from

  • Hassan, S.; Hugouvieux-Cotte-Pattat, N.
    Identification of two feruloyl esterases in Dickeya dadantii 3937 and induction of the major feruloyl esterase and of pectate lyases by ferulic acid (2011), J. Bacteriol., 193, 963-970.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.1.1.73 ferulic acid strong activation of FaeD and FaeT resulting in 15fold and 4fold increase of the FaeD and FaeT activities, respectively, at 0.5 mM Dickeya dadantii

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.1.73 genes faeT and faeD, DNA and amino acid sequence determination and analysis, overexpression in Escherichia coli strain BL21(DE3) Dickeya dadantii

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.1.73 cytoplasm feruloyl esterase FaeT Dickeya dadantii 5737
-
3.1.1.73 extracellular feruloyl esterase FaeD, which is an extracellular protein secreted by the Out system Dickeya dadantii
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.1.73 additional information no difference in enzymatic activity through addition of cations Ca2+, Cu2+, Fe2+, Mg2+, or Mn2+ at 0.1-1 mM or 10 mM EDTA Dickeya dadantii

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.73 Dickeya dadantii
-
formerly Erwinia chrysanthemi, genes faeT and faeD
-
3.1.1.73 Dickeya dadantii 3937
-
formerly Erwinia chrysanthemi, genes faeT and faeD
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.1.1.73 0.005
-
about, recombinant feruoyl esterase FaeD, pH 7.5, 37°C, substrate 4-nitrophenyl acetate Dickeya dadantii
3.1.1.73 0.0083
-
about, recombinant feruoyl esterase FaeT, pH 7.5, 37°C, substrate 4-nitrophenyl acetate Dickeya dadantii
3.1.1.73 0.0267
-
about, recombinant feruoyl esterase FaeD, pH 7.5, 37°C, substrate 4-nitrophenyl acetate, in presence of 0.5 mM ferulic acid Dickeya dadantii
3.1.1.73 0.033
-
about, recombinant feruoyl esterase FaeT, pH 7.5, 37°C, substrate 4-nitrophenyl acetate, in presence of 0.5 mM ferulic acid Dickeya dadantii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.73 4-nitrophenyl acetate + H2O
-
Dickeya dadantii 4-nitrophenol + acetate
-
?
3.1.1.73 4-nitrophenyl acetate + H2O
-
Dickeya dadantii 3937 4-nitrophenol + acetate
-
?

Synonyms

EC Number Synonyms Comment Organism
3.1.1.73 FaeD
-
Dickeya dadantii
3.1.1.73 FaeT
-
Dickeya dadantii
3.1.1.73 More FaeD and FaeT belong to the carbohydrate esterase family CE10 Dickeya dadantii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.1.73 37
-
assay at Dickeya dadantii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.73 6.5
-
assay at Dickeya dadantii

Expression

EC Number Organism Comment Expression
3.1.1.73 Dickeya dadantii expression of genes faeT and faeD is not significantly affected by the addition of acetosyringone, benzoic acid, cinnamic acid, p-coumaric acid, vanillic acid, arabinogalactan, arabinose, galactose, galacturonate, mannose, pectin, polygalacturonate, rhamnose, salicine, xylose, or xylan additional information
3.1.1.73 Dickeya dadantii feruoyl esterases FaeD and FaeT are induced by ferulic acid. The product of the adjacent gene faeR is involved in the positive control of faeD in response to ferulic acid. Moreover, ferulic acid acts in synergy with polygalacturonate to induce pectate lyases, the main virulence determinant of soft rot disease up

General Information

EC Number General Information Comment Organism
3.1.1.73 malfunction when gene faeT is inactivated, the size of the esterase halo clearly decreased. When gene faeD is inactivated, only very low residual feruoyl esterase activity is detected, as observed in the faeD faeT double mutant Dickeya dadantii
3.1.1.73 physiological function the two feruloyl esterases, FaeD and FaeT, cleave the ester link between ferulate and the pectic or xylan chains. FaeD is an extracellular protein secreted by the Out system, responsible for pectinase secretion. Feruloyl esterases dissociate internal cross-links in the polysaccharide network of the plant cell wall, suppress the polysaccharide esterifications, and liberate ferulic acid, which contributes to the induction of pectate lyases. Together, these effects of feruloyl esterases could facilitate soft rot disease caused by pectinolytic bacteria. FaeD appears to be responsible for most feruloyl esterase activity in Dickeya dadantii Dickeya dadantii