Structural and Biochemical Analysis Reveals a Distinct Catalytic Site of Salicylate 5-Monooxygenase NagGH from Rieske Dioxygenases
Yanjie Hou, Yuan Guo, De‐Feng Li, Ning‐Yi Zhou
Abstract
Rieske oxygenases are involved in the degradation of various aromatic compounds. These dioxygenases usually carry out hydroxylation of hydrophobic aromatic compounds and supply substrates with hydroxyl groups for extradiol/intradiol dioxygenases to cleave rings, and have been extensively studied. Salicylate 5-hydroxylase NagGH is a novel Rieske monooxygenase with high similarity to Rieske dioxygenases, and also shares reductase and ferredoxin similarity with a Rieske dioxygenase naphthalene 1,2-dioxygenase (NagAcAd) in Ralstonia sp. strain U2.
Topics & Concepts
DioxygenaseHydroxylationMonooxygenaseChemistryOxygenaseFerredoxinPrenyltransferaseStereochemistryBiochemistryEnzymeCytochrome P450PrenylationMicrobial bioremediation and biosurfactantsMicrobial metabolism and enzyme functionMetal-Catalyzed Oxygenation Mechanisms