BRENDA - Enzyme Database show
show all sequences of 1.3.1.81

Monoterpene double-bond reductases of the (-)-menthol biosynthetic pathway: isolation and characterization of cDNAs encoding (-)-isopiperitenone reductase and (+)-pulegone reductase of peppermint

Ringer, K.L.; McConkey, M.E.; Davis, E.M.; Rushing, G.W.; Croteau, R.; Arch. Biochem. Biophys. 418, 80-92 (2003)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
DNA and amino acid sequence determination and analysis, functional expression in Escherichia coli strain BL21(DE3)
Mentha x piperita
General Stability
General Stability
Organism
neither protease inhibitors nor flavins improve the activity or stability of the purified native enzyme, and the addition of glycerol to the buffers leads to rapid loss of activity upon storage
Mentha x piperita
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0023
-
(+)-pulegone
pH 5.0, recombinant enzyme
Mentha x piperita
0.0069
-
NADPH
pH 5.0, recombinant enzyme
Mentha x piperita
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
37914
-
1 x * 43000, SDS-PAGE, 1 * 37914, sequence calculation
Mentha x piperita
43000
-
1 x * 43000, SDS-PAGE, 1 * 37914, sequence calculation
Mentha x piperita
45000
-
gel filtration
Mentha x piperita
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2 (+)-pulegone + 2 NADPH + 2 H+
Mentha x piperita
pathways of monoterpene biosynthesis, overview
(-)-menthone + (+)-isomenthone + 2 NADP+
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Mentha x piperita
-
cv. Black Mitcham
-
Purification (Commentary)
Commentary
Organism
recombinant enzyme from Escherichia coli strain BL21(DE3), native enzyme by oil gland secretory cell isolation procedure, two steps of anion exchange chromatography, hydroxyapatite chromatography, and beta-NADPH affinity chromatography, the activity is rapidly lost during purification on each matrix, 10fold purification accompanied by loss of over 98% of starting activity
Mentha x piperita
Source Tissue
Source Tissue
Commentary
Organism
Textmining
epidermis
-
Mentha x piperita
-
leaf
-
Mentha x piperita
-
secretory cell
-
Mentha x piperita
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2 (+)-pulegone + 2 NADPH + 2 H+
pathways of monoterpene biosynthesis, overview
684664
Mentha x piperita
(-)-menthone + (+)-isomenthone + 2 NADP+
-
-
-
?
2 (+)-pulegone + 2 NADPH + 2 H+
the reductase catalyzes the reduction of the 4(8)-double bond of (+)-pulegone to produce both (-)-menthone and (+)-isomenthone in a 70:30 ratio, product analysis by GC-MS, stereospecific reductase
684664
Mentha x piperita
(-)-menthone + (+)-isomenthone + 2 NADP+
-
-
-
?
Subunits
Subunits
Commentary
Organism
monomer
1 x * 43000, SDS-PAGE, 1 * 37914, sequence calculation
Mentha x piperita
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1.8
-
NADPH
pH 5.0, recombinant enzyme
Mentha x piperita
1.8
-
(+)-pulegone
pH 5.0, recombinant enzyme
Mentha x piperita
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
5
-
-
Mentha x piperita
pH Range
pH Minimum
pH Maximum
Commentary
Organism
4.5
6.5
70% of maximal activity within this range
Mentha x piperita
Cofactor
Cofactor
Commentary
Organism
Structure
NADPH
dependent on
Mentha x piperita
pI Value
Organism
Commentary
pI Value Maximum
pI Value
Mentha x piperita
about, isoelectric focusing
-
5.2
Cloned(Commentary) (protein specific)
Commentary
Organism
DNA and amino acid sequence determination and analysis, functional expression in Escherichia coli strain BL21(DE3)
Mentha x piperita
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADPH
dependent on
Mentha x piperita
General Stability (protein specific)
General Stability
Organism
neither protease inhibitors nor flavins improve the activity or stability of the purified native enzyme, and the addition of glycerol to the buffers leads to rapid loss of activity upon storage
Mentha x piperita
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0023
-
(+)-pulegone
pH 5.0, recombinant enzyme
Mentha x piperita
0.0069
-
NADPH
pH 5.0, recombinant enzyme
Mentha x piperita
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
37914
-
1 x * 43000, SDS-PAGE, 1 * 37914, sequence calculation
Mentha x piperita
43000
-
1 x * 43000, SDS-PAGE, 1 * 37914, sequence calculation
Mentha x piperita
45000
-
gel filtration
Mentha x piperita
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2 (+)-pulegone + 2 NADPH + 2 H+
Mentha x piperita
pathways of monoterpene biosynthesis, overview
(-)-menthone + (+)-isomenthone + 2 NADP+
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant enzyme from Escherichia coli strain BL21(DE3), native enzyme by oil gland secretory cell isolation procedure, two steps of anion exchange chromatography, hydroxyapatite chromatography, and beta-NADPH affinity chromatography, the activity is rapidly lost during purification on each matrix, 10fold purification accompanied by loss of over 98% of starting activity
Mentha x piperita
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
epidermis
-
Mentha x piperita
-
leaf
-
Mentha x piperita
-
secretory cell
-
Mentha x piperita
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2 (+)-pulegone + 2 NADPH + 2 H+
pathways of monoterpene biosynthesis, overview
684664
Mentha x piperita
(-)-menthone + (+)-isomenthone + 2 NADP+
-
-
-
?
2 (+)-pulegone + 2 NADPH + 2 H+
the reductase catalyzes the reduction of the 4(8)-double bond of (+)-pulegone to produce both (-)-menthone and (+)-isomenthone in a 70:30 ratio, product analysis by GC-MS, stereospecific reductase
684664
Mentha x piperita
(-)-menthone + (+)-isomenthone + 2 NADP+
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
monomer
1 x * 43000, SDS-PAGE, 1 * 37914, sequence calculation
Mentha x piperita
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1.8
-
NADPH
pH 5.0, recombinant enzyme
Mentha x piperita
1.8
-
(+)-pulegone
pH 5.0, recombinant enzyme
Mentha x piperita
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
5
-
-
Mentha x piperita
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
4.5
6.5
70% of maximal activity within this range
Mentha x piperita
pI Value (protein specific)
Organism
Commentary
pI Value Maximum
pI Value
Mentha x piperita
about, isoelectric focusing
-
5.2
Other publictions for EC 1.3.1.81
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)
746411
Li
MAPK-mediated regulation of g ...
Mentha x piperita
Protoplasma
253
1541-1556
2016
-
-
-
-
-
-
-
-
-
-
-
1
-
3
-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
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-
-
-
-
-
-
-
1
-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
-
-
-
-
2
2
-
-
-
712853
Dolzhenko
UV-B modulates the interplay b ...
Mentha x piperita
J. Photochem. Photobiol. B Biol.
100
67-75
2010
-
-
1
-
-
-
-
-
-
-
-
1
-
2
-
-
-
-
-
1
-
-
1
-
-
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-
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2
-
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-
1
2
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-
1
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1
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-
1
-
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-
-
-
-
-
-
-
1
1
1
1
-
-
713312
Rios-Estepa
Mathematical modeling-guided e ...
Mentha x piperita
Plant Physiol.
152
2105-2119
2010
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
3
-
-
2
-
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-
-
-
-
-
-
2
-
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-
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-
-
2
-
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-
1
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3
-
-
2
-
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-
-
-
-
-
-
-
-
2
2
-
-
-
725777
Dolzhenko
UV-B modulates the interplay b ...
Mentha x piperita
J. Photochem. Photobiol. B
100
67-75
2010
-
-
-
-
-
-
1
-
-
-
-
-
-
2
-
-
-
-
-
1
-
-
-
-
-
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1
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1
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-
-
1
-
-
1
-
-
689800
Rios-Estepa
A systems biology approach ide ...
Mentha x piperita
Proc. Natl. Acad. Sci. USA
105
2818-2823
2008
-
-
-
-
-
-
1
2
-
-
-
2
-
2
-
-
1
-
-
2
-
-
3
-
-
-
-
-
1
-
-
1
1
-
1
-
-
-
1
-
-
-
1
1
1
2
-
-
-
2
-
-
-
1
-
2
-
-
3
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
670589
Ringer
Monoterpene metabolism. Clonin ...
Mentha spicata, Mentha x piperita
Plant Physiol.
137
863-872
2005
-
-
-
-
-
-
-
-
-
-
-
2
-
2
-
-
-
-
-
-
-
-
4
-
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2
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2
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2
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-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
660251
Turner
Organization of monoterpene bi ...
Mentha x piperita
Plant Physiol.
136
4215-4227
2004
-
-
1
-
-
-
-
-
1
-
1
1
-
4
-
-
1
-
-
1
-
-
2
1
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
1
-
1
1
-
-
-
1
-
1
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
684664
Ringer
Monoterpene double-bond reduct ...
Mentha x piperita
Arch. Biochem. Biophys.
418
80-92
2003
-
-
1
-
-
1
-
2
-
-
3
1
-
3
-
-
1
-
-
3
-
-
2
1
-
-
-
2
1
1
-
1
-
1
-
-
-
1
1
-
-
1
-
-
-
2
-
-
3
1
-
-
-
1
-
3
-
-
2
1
-
-
-
2
1
1
-
1
-
-
-
-
-
-
689735
Mahmoud
Menthofuran regulates essentia ...
Mentha x piperita
Proc. Natl. Acad. Sci. USA
100
14481-14486
2003
-
-
-
-
-
-
1
-
1
-
-
2
-
3
-
-
-
-
-
1
1
-
3
-
-
-
-
-
-
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-
1
-
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-
-
-
-
1
-
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1
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1
-
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2
-
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1
1
-
3
-
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