|
type |
Journal Article |
authors |
Hedges JB, Kuatsjah E, Du YL, Eltis LD, Ryan KS. |
title |
Snapshots of the catalytic cycle of an O2, pyridoxal phosphate-dependent hydroxylase. |
journal |
ACS Chem Biol |
Activity |
mppp |
Family |
mppp |
sel |
selected |
ui |
29466666 |
year |
(2018) |
volume |
13 |
number |
4 |
pages |
965-974 |
| |
abstract |
Enzymes that catalyze hydroxylation of unactivated carbons normally contain heme- and non-heme iron cofactors. By contrast, how a pyridoxal phosphate (PLP)-dependent enzyme could catalyze such a hydroxylation was unknown. Here, we investigate RohP, a PLP-dependent enzyme that converts L-arginine to (S)-4-hydroxy-2-ketoarginine. We determine that the RohP reaction consumes oxygen, with stoichiometric release of H2O2. To understand this unusual chemistry, we obtain ~1.5 Å resolution structures that capture intermediates along the catalytic cycle. Our data suggest that RohP carries out a four-electron oxidation and a stereospecific alkene hydration to give the (S)-configured product. Together with our earlier studies on an O2, PLP-dependent L-arginine oxidase, our work suggests that there is a shared pathway leading to both oxidized and hydroxylated products from L-arginine.
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last changed |
2018/10/05 11:50 |
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