1.14.15.37	(7R)-7-hydroxyluteothin + O2 + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+	-	Streptomyces thioluteus	aureothin + 2 H2O + 2 oxidized ferredoxin [iron-sulfur] cluster	-	?	446483	
1.14.15.37	deoxyneoaureothin + 2 O2 + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+	-	Streptomyces orinoci	neoaureothin + 3 H2O + 4 oxidized ferredoxin [iron-sulfur] cluster	-	?	447405	
1.14.15.37	deoxyneoaureothin + 2 O2 + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+	-	Streptomyces orinoci HKI-0260	neoaureothin + 3 H2O + 4 oxidized ferredoxin [iron-sulfur] cluster	-	?	447405	
1.14.15.37	luteothin + 2 O2 + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+	-	Streptomyces thioluteus	aureothin + 3 H2O + 4 oxidized ferredoxin [iron-sulfur] cluster	-	?	447705	
1.14.15.37	luteothin + 2 O2 + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+	luteothin i.e. deoxyaureothin	Streptomyces thioluteus	aureothin + 3 H2O + 4 oxidized ferredoxin [iron-sulfur] cluster	-	?	447705	
1.14.15.37	luteothin + O2 + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+	-	Streptomyces thioluteus	(7R)-7-hydroxyluteothin + H2O + 2 oxidized ferredoxin [iron-sulfur] cluster	-	?	447706	
1.14.15.37	additional information	AurH is a unique cytochrome P450 monooxygenase catalyzing the stepwise formation of a homochiral oxygen heterocycle, a key structural and pharmacophoric component of the antibiotic aureothin. The enzymatic reaction involves a tandem oxygenation process including a regio- and stereospecific hydroxylation, followed by heterocyclization, overview	Streptomyces thioluteus	?	-	?	89	
1.14.15.37	additional information	AurH catalyzes an unprecedented tandem oxygenation process. First, AurH catalyzes an asymmetric hydroxylation of deoxyaureothin, yielding (7R)-7-hydroxydeoxyaureothin as an intermediate, thus setting the absolute configuration of the final product. Second, AurH mediates another C-O bond formation that leads to O-heterocyclization. Structure-function relationship analysis by computational docking, site-directed mutagenesis, and chemical analyses, overview	Streptomyces thioluteus	?	-	?	89	
1.14.15.37	additional information	the formation of the heterocycle is catalyzed by a single enzyme both in vivo and in vitro. The reaction is a sequential hydroxylation-heterocyclization sequence. The methylene position adjacent to the pyrone ring (C7) is attacked first, which defines the absolute configuration of the resulting heterocycle. The second allylic position (C9a) is then oxygenated by the adjacent hydroxymethyl group	Streptomyces thioluteus	?	-	?	89