Information on EC 1.14.13.222 - aurachin C monooxygenase/isomerase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.13.222
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RECOMMENDED NAME
GeneOntology No.
aurachin C monooxygenase/isomerase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2-hydroxy-1a-methyl-7a-[(2E,6E)-farnesyl]-1a,2-dihydrooxireno[2,3-b]quinolin-7(7aH)-one = 4-hydroxy-2-methyl-3-oxo-4-[(2E,6E)-farnesyl]-3,4-dihydroquinoline 1-oxide
show the reaction diagram
(1b)
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aurachin C + NAD(P)H + H+ + O2 = 2-hydroxy-1a-methyl-7a-[(2E,6E)-farnesyl]-1a,2-dihydrooxireno[2,3-b]quinolin-7(7aH)-one + NAD(P)+ + H2O
show the reaction diagram
(1a)
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aurachin C + NAD(P)H + H+ + O2 = 4-hydroxy-2-methyl-3-oxo-4-[(2E,6E)-farnesyl]-3,4-dihydroquinoline 1-oxide + NAD(P)+ + H2O
show the reaction diagram
overall reaction
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SYSTEMATIC NAME
IUBMB Comments
aurachin C:NAD(P)H:oxygen oxidoreductase (4-hydroxy-2-methyl-3-oxo-4-farnesyl-3,4-dihydroquinoline-1-oxide-forming)
The aurachin C monooxygenase from the bacterium Stigmatella aurantiaca accepts both NADH and NADPH as cofactor, but has a preference for NADH. It catalyses the initial steps in the conversion of aurachin C to aurachin B. The FAD-dependent monooxygenase catalyses the epoxidation of the C2-C3 double bond of aurachin C, which is followed by a semipinacol rearrangement, causing migration of the farnesyl group from C3 to C4.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
E9RFS9 i.e. oxygenase large subunit MimA, E9RFT0 i.e. reductase MimB, E9RFT1 i.e. oxygenase small subunit MimC, E9RFT2 i.e. coupling protein MimD
E9RFS9 and E9RFT0 and E9RFT1 and E9RFT2
UniProt
Manually annotated by BRENDA team
E9RFS9 i.e. oxygenase large subunit MimA, E9RFT0 i.e. reductase MimB, E9RFT1 i.e. oxygenase small subunit MimC, E9RFT2 i.e. coupling protein MimD
E9RFS9 and E9RFT0 and E9RFT1 and E9RFT2
UniProt
Manually annotated by BRENDA team
alpha subunit
UniProt
Manually annotated by BRENDA team
alpha subunit
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 2,3-dimethyl-4(1H)-quinolinone + NAD(P)H + H+ + O2
3-hydroxy-2-[(3-hydroxy-3-methyl-4-oxo-1,2,3,4-tetrahydroquinolin-2-yl)methyl]-3-methylquinolin-4(3H)-one + NAD(P)+ + H2O
show the reaction diagram
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methyl variant of aurachin D
product is formed by dimerization
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?
2-methyl-3-geranyl-4(1H)-quinolinone + NAD(P)H + H+ + O2
3-[(3,7-dimethylocta-1,6-dien-3-yl)oxy]-2-methyl-2,3-dihydroquinolin-4(1H)-one + NAD(P)+ + H2O
show the reaction diagram
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geranyl variant of aurachin D
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?
2-methyl-3-isoprenyl-4(1H)-quinolinone + NAD(P)H + H+ + O2
2-methyl-3-[(2-methylbut-3-en-2-yl)oxy]-2,3-dihydroquinolin-4(1H)-one + NAD(P)+ + H2O
show the reaction diagram
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isoprenyl variant of aurachin D
during the AuaG-catalysed transformation, the transient C2-C3 epoxide can be formed and opened to the tertiary alcoholate. The ether product is supposed to arise from rapid retro-[2,3]-Wittig rearrangement assisted by the presence of both carbonyl and iminium functions
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?
aurachin C + NAD(P)H + H+ + O2
4-hydroxy-2-methyl-3-oxo-4-[(2E,6E)-farnesyl]-3,4-dihydroquinoline 1-oxide + NAD(P)+ + H2O
show the reaction diagram
aurachin C + NADH + H+ + O2
4-hydroxy-2-methyl-4-[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]quinolin-3(4H)-one 1-oxide + NAD+ + H2O
show the reaction diagram
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formation of aurachin B requires the presence of AuaH. AuaG and AuaH act sequentially and conversion of aurachin C into aurachin B occurs by oxidation and subsequent reduction
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aurachin C + NADH + O2
4-hydroxy-2-methyl-3-oxo-4-farnesyl-3,4-dihydroquinoline-1-oxide + NAD+ + H2O
show the reaction diagram
additional information
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AuaG is able to oxidize short-chain analogues of aurachin D. A retro-[2,3]-Wittig rearrangement is observed with isoprenyl substrate analogues. Saturated-chain analogues of N-oxidized aurachin C are not transformed by the C3 to C4 semipinacol reaction
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
aurachin C + NADH + O2
4-hydroxy-2-methyl-3-oxo-4-farnesyl-3,4-dihydroquinoline-1-oxide + NAD+ + H2O
show the reaction diagram
H1ZZA4
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
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AuaG purifies as a slightly yellow protein and the binding cofactor is flavin–adenine dinucleotide; contains an FAD binding domain
NADH
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NADH is preferred over NADPH; preferred over NADPH
NADPH
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NADH is preferred over NADPH
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41290
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calculated from amino acid sequence
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli; expression in Escherichia coli
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