| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-107 |
Sentence |
denotes |
Coq6 is responsible for the C4-deamination reaction in coenzyme Q biosynthesis in Saccharomyces cerevisiae. |
| T2 |
108-334 |
Sentence |
denotes |
The yeast Saccharomyces cerevisiae is able to use para-aminobenzoic acid (pABA) in addition to 4-hydroxybenzoic acid as a precursor of coenzyme Q, a redox lipid essential to the function of the mitochondrial respiratory chain. |
| T3 |
335-496 |
Sentence |
denotes |
The biosynthesis of coenzyme Q from pABA requires a deamination reaction at position C4 of the benzene ring to substitute the amino group with an hydroxyl group. |
| T4 |
497-710 |
Sentence |
denotes |
We show here that the FAD-dependent monooxygenase Coq6, which is known to hydroxylate position C5, also deaminates position C4 in a reaction implicating molecular oxygen, as demonstrated with labeling experiments. |
| T5 |
711-833 |
Sentence |
denotes |
We identify mutations in Coq6 that abrogate the C4-deamination activity, whereas preserving the C5-hydroxylation activity. |
| T6 |
834-964 |
Sentence |
denotes |
Several results support that the deletion of Coq9 impacts Coq6, thus explaining the C4-deamination defect observed in Δcoq9 cells. |
| T7 |
965-1081 |
Sentence |
denotes |
The vast majority of flavin monooxygenases catalyze hydroxylation reactions on a single position of their substrate. |
| T8 |
1082-1358 |
Sentence |
denotes |
Coq6 is thus a rare example of a flavin monooxygenase that is able to act on two different carbon atoms of its C4-aminated substrate, allowing its deamination and ultimately its conversion into coenzyme Q by the other proteins constituting the coenzyme Q biosynthetic pathway. |
