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Literature summary extracted from

  • Bhuiya, M.W.; Lee, S.G.; Jez, J.M.; Yu, O.
    Structure and mechanism of ferulic acid decarboxylase (FDC1) from Saccharomyces cerevisiae (2015), Appl. Environ. Microbiol., 81, 4216-4223.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.1.102 expression in Escherichia coli Saccharomyces cerevisiae

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.1.1.102 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

Protein Variants

EC Number Protein Variants Comment Organism
4.1.1.102 E285A loss of catalytic activity Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.1.102 0.79
-
 4-coumarate pH 6.5, 30°C Saccharomyces cerevisiae
4.1.1.102 0.92
-
 ferulate pH 6.5, 30°C Saccharomyces cerevisiae

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.102 Saccharomyces cerevisiae Q03034
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.102 4-coumarate
-
 Saccharomyces cerevisiae 4-vinylphenol + CO2
-
 ?
4.1.1.102 ferulate
-
 Saccharomyces cerevisiae 4-vinylguaiacol + CO2
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.1.1.102 FDC1
-
 Saccharomyces cerevisiae
4.1.1.102 ubiD
-
 Saccharomyces cerevisiae