BRENDA - Enzyme Database show
show all sequences of 1.1.1.394

A semipinacol rearrangement directed by an enzymatic system featuring dual-function FAD-dependent monooxygenase

Katsuyama, Y.; Harmrolfs, K.; Pistorius, D.; Li, Y. and Muller, R.; Angew. Chem. Int. Ed. Engl. 51, 9437-9440 (2012)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene auaH, recombinant expression of the C-terminally His6-tagged enzyme in Escherichia coli
Stigmatella aurantiaca
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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
-
?
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
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Stigmatella aurantiaca
H1ZZB0
gene auaH
-
Stigmatella aurantiaca Sg a15
H1ZZB0
gene auaH
-
Purification (Commentary)
Commentary
Organism
recombinant C-terminally HIs6-tagged enzyme from Escherichia coli by nickel affinity chromatography
Stigmatella aurantiaca
Reaction
Reaction
Commentary
Organism
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
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3,4-dihydroxy-2-methyl-4-[(2E,6E)-farnesyl]-3,4-dihydroquinoline 1-oxide + NAD+
-
733094
Stigmatella aurantiaca
4-hydroxy-2-methyl-3-oxo-4-[(2E,6E)-farnesyl]-3,4-dihydroquinoline 1-oxide + NADH + H+
i.e aurachin B
-
-
?
3,4-dihydroxy-2-methyl-4-[(2E,6E)-farnesyl]-3,4-dihydroquinoline 1-oxide + NAD+
-
733094
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
-
-
?
Subunits
Subunits
Commentary
Organism
More
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
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
-
Stigmatella aurantiaca
Cloned(Commentary) (protein specific)
Commentary
Organism
gene auaH, recombinant expression of the C-terminally His6-tagged enzyme in Escherichia coli
Stigmatella aurantiaca
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
-
Stigmatella aurantiaca
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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
-
?
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
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant C-terminally HIs6-tagged enzyme from Escherichia coli by nickel affinity chromatography
Stigmatella aurantiaca
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3,4-dihydroxy-2-methyl-4-[(2E,6E)-farnesyl]-3,4-dihydroquinoline 1-oxide + NAD+
-
733094
Stigmatella aurantiaca
4-hydroxy-2-methyl-3-oxo-4-[(2E,6E)-farnesyl]-3,4-dihydroquinoline 1-oxide + NADH + H+
i.e aurachin B
-
-
?
3,4-dihydroxy-2-methyl-4-[(2E,6E)-farnesyl]-3,4-dihydroquinoline 1-oxide + NAD+
-
733094
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
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
More
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
General Information
General Information
Commentary
Organism
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
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
General Information (protein specific)
General Information
Commentary
Organism
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
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
Other publictions for EC 1.1.1.394
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
733094
Katsuyama
A semipinacol rearrangement di ...
Stigmatella aurantiaca, Stigmatella aurantiaca Sg a15
Angew. Chem. Int. Ed. Engl.
51
9437-9440
2012
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