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Literature summary extracted from

  • Gu, W.; Yang, J.; Lou, Z.; Liang, L.; Sun, Y.; Huang, J.; Li, X.; Cao, Y.; Meng, Z.; Zhang, K.Q.
    Structural basis of enzymatic activity for the ferulic acid decarboxylase (FADase) from Enterobacter sp. Px6-4 (2011), PLoS ONE, 6, e16262.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.1.1.102 crystal structures in complex with substrate analogues. FADase possesses a half-opened bottom beta-barrel with the catalytic pocket located between the middle of the core beta-barrel and the helical bottom. Its structure shared a high degree of similarity with members of the phenolic acid decarboxylase (PAD) superfamily. FADase catalyzed reactions by an open-closed mechanism involving a pocket on the surface of the enzyme. During decarboxylation of ferulic acid by FADase, Trp25 and Tyr27 are required for the entering and proper orientation of the substrate while Glu134 and Asn23 participate in proton transfer Enterobacter sp.

Protein Variants

EC Number Protein Variants Comment Organism
4.1.1.102 E134A mutation decreases the enzyme activity by more than 60% Enterobacter sp.
4.1.1.102 W25A mutation decreases the enzyme activity by more than 95% Enterobacter sp.
4.1.1.102 Y21A mutation abolishes the enzyme activity completely Enterobacter sp.
4.1.1.102 Y27A mutation abolishes the enzyme activity completely Enterobacter sp.

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.1.102 0.73
-
 ferulate mutant W25A, pH 4.0, 28°C Enterobacter sp.
4.1.1.102 2.36
-
 ferulate wild-type, pH 4.0, 28°C Enterobacter sp.
4.1.1.102 3.52
-
 ferulate mutant E134A, pH 4.0, 28°C Enterobacter sp.

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.102 Enterobacter sp. C6F3U5
-
-
4.1.1.102 Enterobacter sp. Px6-4 C6F3U5
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.102 ferulate
-
 Enterobacter sp. 4-vinylguaiacol + CO2
-
 ?
4.1.1.102 ferulate
-
 Enterobacter sp. Px6-4 4-vinylguaiacol + CO2
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.1.1.102 0.02
-
 ferulate mutant W25A, pH 4.0, 28°C Enterobacter sp.
4.1.1.102 0.99
-
 ferulate mutant E134A, pH 4.0, 28°C Enterobacter sp.
4.1.1.102 2.15
-
 ferulate wild-type, pH 4.0, 28°C Enterobacter sp.

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
4.1.1.102 0.02
-
 ferulate mutant W25A, pH 4.0, 28°C Enterobacter sp.
4.1.1.102 0.28
-
 ferulate mutant E134A, pH 4.0, 28°C Enterobacter sp.
4.1.1.102 0.91
-
 ferulate wild-type, pH 4.0, 28°C Enterobacter sp.