4.1.1.102: phenacrylate decarboxylase

This is an abbreviated version!
For detailed information about phenacrylate decarboxylase, go to the full flat file.

Reaction

Synonyms

FADase, Fdc, FDC1, ferulic acid decarboxylase, PAD, PAD1, phenolic acid decarboxylase, ubiD, YDR539W

ECTree

     4 Lyases

         4.1 Carbon-carbon lyases

             4.1.1 Carboxy-lyases

                4.1.1.102 phenacrylate decarboxylase

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Results	in table
4	Activating Compound
738	AA Sequence
9	Application
13	Cloned(Commentary)
2	Cofactor
3	Crystallization (Commentary)
5	General Information
8	Inhibitors
22	kcat/KM [mM/s]
11	KM Value [mM]
2	Localization
8	Metals/Ions
8	Molecular Weight [Da]
4	Natural Substrates/ Products (Substrates)
36	Organism
2	Pathway
53	PDB ID
5	pH Optimum
4	pH Range
2	pH Stability
1	pI Value
43	Protein Variants
4	Purification (Commentary)
3	Reaction
24	Reference
3	Specific Activity [micromol/min/mg]
47	Substrates and Products (Substrate)
7	Subunits
26	Synonyms
1	Systematic Name
5	Temperature Optimum [°C]
3	Temperature Range [°C]
1	Temperature Stability [°C]
9	Turnover Number [1/s]

Crystallization

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Crystallization on EC 4.1.1.102 - phenacrylate decarboxylase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

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.

C6F3U5

735040

modeling of structure based on PDB entry 2GC9. Residue Met57 is located at the entrance of the pocket and in the immediate vicinity of possible catalytic residues Arg60 and Glu82. Residue Met103 is spatially more distant from the two catalytic residues and located deeper in the active-site pocket

Meyerozyma guilliermondii

G3XHW5

733069

to 2.45 A resolution. The conformational flexibility of the beta2e-alpha5 loop allows access to the active site. The structure implicates Glu285 as the general base. An about 30-A-long pocket adjacent to the catalytic site may accommodate the isoprenoid tail of the substrate needed for ubiquinone biosynthesis in yeast

Saccharomyces cerevisiae

Q03034

733178