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Literature summary extracted from

  • Katsuyama, Y.; Harmrolfs, K.; Pistorius, D.; Li, Y. and Muller, R.
    A semipinacol rearrangement directed by an enzymatic system featuring dual-function FAD-dependent monooxygenase (2012), Angew. Chem. Int. Ed. Engl., 51, 9437-9440.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.394 gene auaH, recombinant expression of the C-terminally His6-tagged enzyme in Escherichia coli Stigmatella aurantiaca
1.14.13.222 expressed in Escherichia coli Stigmatella aurantiaca
1.14.13.222 expression in Escherichia coli Stigmatella aurantiaca

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.14.13.222 41290
-
 calculated from amino acid sequence Stigmatella aurantiaca

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.394 3,4-dihydroxy-2-methyl-4-[(2E,6E)-farnesyl]-3,4-dihydroquinoline 1-oxide + NAD+ Stigmatella aurantiaca
-
 4-hydroxy-2-methyl-3-oxo-4-[(2E,6E)-farnesyl]-3,4-dihydroquinoline 1-oxide + NADH + H+ i.e aurachin B ?
1.1.1.394 3,4-dihydroxy-2-methyl-4-[(2E,6E)-farnesyl]-3,4-dihydroquinoline 1-oxide + NAD+ Stigmatella aurantiaca Sg a15
-
 4-hydroxy-2-methyl-3-oxo-4-[(2E,6E)-farnesyl]-3,4-dihydroquinoline 1-oxide + NADH + H+ i.e aurachin B ?
1.14.13.222 aurachin C + NADH + O2 Stigmatella aurantiaca
-
 4-hydroxy-2-methyl-3-oxo-4-farnesyl-3,4-dihydroquinoline-1-oxide + NAD+ + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.394 Stigmatella aurantiaca H1ZZB0 gene auaH
-
1.1.1.394 Stigmatella aurantiaca Sg a15 H1ZZB0 gene auaH
-
1.14.13.222 Stigmatella aurantiaca H1ZZA4
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.394 recombinant C-terminally HIs6-tagged enzyme from Escherichia coli by nickel affinity chromatography Stigmatella aurantiaca

Reaction

EC Number Reaction Comment Organism Reaction ID
1.1.1.394 aurachin B + NAD+ + H2O = 4-[(2E,6E)-farnesyl]-4-hydroxy-2-methyl-3-oxo-3,4-dihydroquinoline 1-oxide + NADH + H+ reaction mechanism, overview Stigmatella aurantiaca
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.394 3,4-dihydroxy-2-methyl-4-[(2E,6E)-farnesyl]-3,4-dihydroquinoline 1-oxide + NAD+
-
 Stigmatella aurantiaca 4-hydroxy-2-methyl-3-oxo-4-[(2E,6E)-farnesyl]-3,4-dihydroquinoline 1-oxide + NADH + H+ i.e aurachin B ?
1.1.1.394 3,4-dihydroxy-2-methyl-4-[(2E,6E)-farnesyl]-3,4-dihydroquinoline 1-oxide + NAD+
-
 Stigmatella aurantiaca Sg a15 4-hydroxy-2-methyl-3-oxo-4-[(2E,6E)-farnesyl]-3,4-dihydroquinoline 1-oxide + NADH + H+ i.e aurachin B ?
1.14.13.222 aurachin C + NAD(P)H + H+ + O2
-
 Stigmatella aurantiaca 4-hydroxy-2-methyl-3-oxo-4-[(2E,6E)-farnesyl]-3,4-dihydroquinoline 1-oxide + NAD(P)+ + H2O overall reaction, the product of AuaG is highly unstable and rapidly isomerizes in 0.1 M CHES (pH 9.5)/methanol ?
1.14.13.222 aurachin C + NADH + H+ + O2
-
 Stigmatella aurantiaca 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 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 ?
1.14.13.222 aurachin C + NADH + O2
-
 Stigmatella aurantiaca 4-hydroxy-2-methyl-3-oxo-4-farnesyl-3,4-dihydroquinoline-1-oxide + NAD+ + H2O
-
 ?
1.14.13.222 aurachin C + NADH + O2 first step in the conversion of aurachin C to aurachin. The FAD-dependent monooxygenase catalyses the epoxidation of the C2-C3 double bond of aurachin C, this is followed by a semipinacol rearrangement, causing migration of the farnesyl group from C3 to C4 Stigmatella aurantiaca 4-hydroxy-2-methyl-3-oxo-4-farnesyl-3,4-dihydroquinoline-1-oxide + NAD+ + H2O
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.1.394 additional information the enzyme possesses a Rossman fold, and both the conserved TGxxxGxG motif for NAD(P)H binding and the catalytic centers important for ketoreduction activity (YxxxK motif and the catalytic Ser residue) Stigmatella aurantiaca

Synonyms

EC Number Synonyms Comment Organism
1.1.1.394 AuaH
-
 Stigmatella aurantiaca
1.14.13.222 auaG
-
 Stigmatella aurantiaca

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.394 NAD+
-
 Stigmatella aurantiaca
1.14.13.222 FAD contains an FAD binding domain Stigmatella aurantiaca
1.14.13.222 FAD AuaG purifies as a slightly yellow protein and the binding cofactor is flavin–adenine dinucleotide Stigmatella aurantiaca
1.14.13.222 NADH preferred over NADPH Stigmatella aurantiaca
1.14.13.222 NADH NADH is preferred over NADPH Stigmatella aurantiaca
1.14.13.222 NADPH NADH is preferred over NADPH Stigmatella aurantiaca

General Information

EC Number General Information Comment Organism
1.1.1.394 metabolism the enzyme catalyzes the second step in the biosynthetic pathway from aurachin C to aurachin B. Aurachin C is first converted to 3,4-dihydroxy-2-methy-4-[(2E,6E)-farnesyl]-3,4-dihydroquinoline 1-oxide by enzyme AuaG, which is then reduced to aurachin B. The pathway involves the migration of the prenyl group from position C3 to C4, probably via a pinacol type rearrangement. The equilibrium state of AuaG and the instability of 3,4-dihydroxy-2-methy-4-[(2E,6E)-farnesyl]-3,4-dihydroquinoline 1-oxide suggests the requirement of immediate reduction catalyzed by AuaH to fix the farnesyl group at the position C4 and prevent the degradation of the intermediate Stigmatella aurantiaca
1.1.1.394 additional information the enzyme possesses a Rossman fold, and both the conserved TGxxxGxG motif for NAD(P)H binding and the catalytic centers important for ketoreduction activity (YxxxK motif and the catalytic Ser residue) Stigmatella aurantiaca