Literature summary for 4.1.1.98 extracted from

Marshall, S.; Fisher, K.; Cheallaigh, A.; White, M.; Payne, K.; Parker, D.; Rigby, S.; Leys, D.
Oxidative maturation and structural characterization of prenylated FMN binding by UbiD, a decarboxylase involved in bacterial ubiquinone biosynthesis (2017), J. Biol. Chem., 292, 4623-4637 .

Search for more literature for 4.1.1.98

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
structures of holoUbiD reveal a relatively open active site potentially occluded from solvent through domain motion	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0AAB4	-	-

Purification (Commentary)

Purification (Comment)	Organism
UbiD cannot be isolated in an active holoenzyme form. Formation of holoUbiD requires reconstitution in vitro of the apoUbiD with reduced prenylated FMN. The apoenzyme can be readily reconstituted and activated, but in vitro oxidation to the mature prenylated FMN cofactor stalls at formation of a radical prenylated FMN species in holoUbiD	Escherichia coli

Synonyms

Synonyms	Comment	Organism
3-octaprenyl-4-hydroxybenzoate carboxy-lyase	-	Escherichia coli
ubiD	-	Escherichia coli

Cofactor

Cofactor	Comment	Organism	Structure
FMN	enzyme uses a prenylated FMN cofactor. Formation of holoUbiD requires reconstitution in vitro of the apoUbiD with reduced prenylated FMN. A proton-coupled electron transfer may precede formation of the fully oxidized prenylated FMN	Escherichia coli

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)