Literature summary for 4.1.1.102 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.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
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.

Crystallization (Comment)

Organism

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

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

KM Value [mM]

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

Organism

Organism	UniProt	Comment	Textmining
Enterobacter sp.	C6F3U5	-	-
Enterobacter sp. Px6-4	C6F3U5	-	-

Substrates and Products (Substrate)

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

Turnover Number [1/s]

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

kcat/KM [mM/s]

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