1.14.15.37: luteothin monooxygenase
This is an abbreviated version!
For detailed information about luteothin monooxygenase, go to the full flat file.
Reaction
Synonyms
AurH, More, multifunctional cytochrome P450 monooxygenase, NorH
ECTree
1.14.15.37 luteothin monooxygenaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 1.14.15.37 - luteothin monooxygenase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(7R)-7-hydroxyluteothin + O2 + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
aureothin + 2 H2O + 2 oxidized ferredoxin [iron-sulfur] cluster
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-
?
deoxyneoaureothin + 2 O2 + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+
neoaureothin + 3 H2O + 4 oxidized ferredoxin [iron-sulfur] cluster
luteothin + 2 O2 + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+
aureothin + 3 H2O + 4 oxidized ferredoxin [iron-sulfur] cluster
luteothin + O2 + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
(7R)-7-hydroxyluteothin + H2O + 2 oxidized ferredoxin [iron-sulfur] cluster
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-
-
?
deoxyneoaureothin + 2 O2 + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+
neoaureothin + 3 H2O + 4 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
deoxyneoaureothin + 2 O2 + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+
neoaureothin + 3 H2O + 4 oxidized ferredoxin [iron-sulfur] cluster
Streptomyces orinoci HKI-0260
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-
?
luteothin + 2 O2 + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+
aureothin + 3 H2O + 4 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
luteothin + 2 O2 + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+
aureothin + 3 H2O + 4 oxidized ferredoxin [iron-sulfur] cluster
luteothin i.e. deoxyaureothin
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-
?
additional information
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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
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additional information
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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
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additional information
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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
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