Background:The C5-hydroxylation reaction of coenzyme Q biosynthesis in Escherichia coli is catalyzed by an unknown enzyme. Results: The UbiI protein is responsible for the C5-hydroxylation reaction.
Conclusion:The three monooxygenases involved in aerobic Q biosynthesis are now identified. Significance: We report the characterization of a gene of unknown function and the first crystal structure of a monooxygenase involved in Q biosynthesis.
Background: A deamination reaction is necessary for yeast to synthesize coenzyme Q from para-aminobenzoic acid. Results: The deamination requires dioxygen and an active Coq6 enzyme. Conclusion: The flavin monooxygenase Coq6 is responsible for the substitution of the amino group with a hydroxyl group. Significance: Coq6 hydroxylates two positions of its amino substrate and partly determines whether an organism can synthesize coenzyme Q from para-aminobenzoic acid.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.