Literature summary for 4.1.1.102 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.

Search for more literature for 4.1.1.102

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Saccharomyces cerevisiae

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Protein Variants	Comment	Organism
E285A	loss of catalytic activity	Saccharomyces cerevisiae

KM Value [mM]

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

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	Q03034	-	-

Substrates and Products (Substrate)

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

Synonyms

Synonyms	Comment	Organism
FDC1	-	Saccharomyces cerevisiae
ubiD	-	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)