Information on EC 1.3.1.82 - (-)-isopiperitenone reductase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.3.1.82
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RECOMMENDED NAME
GeneOntology No.
(-)-isopiperitenone reductase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(+)-cis-isopulegone + NADP+ = (-)-isopiperitenone + NADPH + H+
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
menthol biosynthesis
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Monoterpenoid biosynthesis
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Biosynthesis of secondary metabolites
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SYSTEMATIC NAME
IUBMB Comments
(+)-cis-isopulegone:NADP+ oxidoreductase
The reaction occurs in the opposite direction to that shown above. The enzyme participates in the menthol-biosynthesis pathway of Mentha plants. (+)-Pulegone, (+)-cis-isopulegone and (-)-menthone are not substrates. The enzyme has a preference for NADPH as the reductant, with NADH being a poor substitute [2]. The enzyme is highly regioselective for the reduction of the endocyclic 1,2-double bond, and is stereoselective, producing only the 1R-configured product. It is a member of the short-chain dehydrogenase/reductase superfamily.
CAS REGISTRY NUMBER
COMMENTARY hide
138066-94-1
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
endophyte isolated from rhizomes of Picrorhiza kurroa, the ITS1-5.8S-ITS2 ribosomal gene sequence shows highest similarity of 99% with Diaporthe phaseolorum followed by 98% with Phomopsis liquidambari, strain PR4 is taxonomically placed under the species, Diaporthe phaseolorum
UniProt
Manually annotated by BRENDA team
endophyte isolated from rhizomes of Picrorhiza kurroa, the ITS1-5.8S-ITS2 ribosomal gene sequence shows highest similarity of 99% with Diaporthe phaseolorum followed by 98% with Phomopsis liquidambari, strain PR4 is taxonomically placed under the species, Diaporthe phaseolorum
UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the enzyme belongs to the short-chain dehydrogenases/reductases SDR superfamily. A sequence alignment of the three ketoreductases MMR, MNMR, and salutaridine reductase (45-49% homology to Mentha enzymes) from Papaver somniferum with Mentha pipertita enzyme IPR shows each enzyme contains typical SDR-like motifs, such as those involved in central beta-sheet stabilization, and a TGxxxGhG motif
metabolism
physiological function
additional information
the catalytic acid residue in enzyme IPR is Glu238, analysis of its role in reaction mechanism
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(-)-isopiperitenone + NADPH + H+
(+)-cis-isopulegone + NADP+
show the reaction diagram
(2S,5R)-5-methyl-2-(propan-2-yl)cyclohexan-1-one + NADP+
(2S,5R)-5-methyl-2-(propan-2-yl)cyclohexan-1-ol + (1S,2R,5R)-5-methyl-2-(propan-2-yl)cyclohexan-1-ol + NADPH + H+
show the reaction diagram
reaction of enzyme mutant E238Y, not of the wild-type enzyme
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-
?
2,6,6-trimethyl-4-oxocyclohex-2-ene-1-carbaldehyde + NADP+
2,2,6-trimethyl-4-oxocyclohexane-1-carbaldehyde + NADPH + H+
show the reaction diagram
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-
-
?
3,5,5-trimethyl-4-(propan-2-yl)cyclohex-2-en-1-one + NADP+
3,3,5-trimethyl-4-(propan-2-yl)cyclohexan-1-one + NADPH + H+
show the reaction diagram
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-
-
?
3,5,5-trimethylcyclohex-2-en-1-one + NADP+
3,3,5-trimethylcyclohexan-1-one + NADPH + H+
show the reaction diagram
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?
3,5-dimethylcyclohex-2-en-1-one + NADP+
3,5-dimethylcyclohexan-1-one + NADPH + H+
show the reaction diagram
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-
-
?
3-methyl-6-(prop-1-en-2-yl)cyclohex-2-en-1-one + NADP+
5-methyl-2-(prop-1-en-2-yl)cyclohexan-1-one + NADPH + H+
show the reaction diagram
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-
-
?
3-methyl-6-(propan-2-yl)cyclohex-2-en-1-one + NADP+
5-methyl-2-(propan-2-yl)cyclohexan-1-one + NADPH + H+
show the reaction diagram
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-
-
?
additional information
?
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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
(-)-isopiperitenone + NADPH + H+
(+)-cis-isopulegone + NADP+
show the reaction diagram
(2S,5R)-5-methyl-2-(propan-2-yl)cyclohexan-1-one + NADP+
(2S,5R)-5-methyl-2-(propan-2-yl)cyclohexan-1-ol + (1S,2R,5R)-5-methyl-2-(propan-2-yl)cyclohexan-1-ol + NADPH + H+
show the reaction diagram
Q6WAU1
reaction of enzyme mutant E238Y, not of the wild-type enzyme
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-
?
2,6,6-trimethyl-4-oxocyclohex-2-ene-1-carbaldehyde + NADP+
2,2,6-trimethyl-4-oxocyclohexane-1-carbaldehyde + NADPH + H+
show the reaction diagram
Q6WAU1
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-
-
?
3,5,5-trimethyl-4-(propan-2-yl)cyclohex-2-en-1-one + NADP+
3,3,5-trimethyl-4-(propan-2-yl)cyclohexan-1-one + NADPH + H+
show the reaction diagram
Q6WAU1
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-
-
?
3,5,5-trimethylcyclohex-2-en-1-one + NADP+
3,3,5-trimethylcyclohexan-1-one + NADPH + H+
show the reaction diagram
Q6WAU1
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?
3,5-dimethylcyclohex-2-en-1-one + NADP+
3,5-dimethylcyclohexan-1-one + NADPH + H+
show the reaction diagram
Q6WAU1
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-
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?
3-methyl-6-(prop-1-en-2-yl)cyclohex-2-en-1-one + NADP+
5-methyl-2-(prop-1-en-2-yl)cyclohexan-1-one + NADPH + H+
show the reaction diagram
Q6WAU1
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-
-
?
3-methyl-6-(propan-2-yl)cyclohex-2-en-1-one + NADP+
5-methyl-2-(propan-2-yl)cyclohexan-1-one + NADPH + H+
show the reaction diagram
Q6WAU1
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?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.001
(-)-isopiperitenone
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pH 5.5, recombinant enzyme
0.0022
NADPH
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pH 5.5, recombinant enzyme
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.3
(-)-isopiperitenone
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pH 5.5, recombinant enzyme
1.3
NADPH
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pH 5.5, recombinant enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
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wild-type enzyme
6.5
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truncated mutant enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 7.5
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50% of maximal activity within this range, wild-type enzyme
5 - 8
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50% of maximal activity within this range, deletion mutant enzyme
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
Mentha piperita;
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
34409
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2 * 34409, sequence calculation, 2 * 38000, SDS-PAGE
38000
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2 * 34409, sequence calculation, 2 * 38000, SDS-PAGE
60000
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about, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 34409, sequence calculation, 2 * 38000, SDS-PAGE
additional information
enzyme three-dimensional structure analysis, overview
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
enzyme IPR in apoform and in complex with NADP+, alkene 3-methyl-6-(prop-1-en-2-yl)cyclohex-2-en-1-one, and beta-cyclocitral, X-ray diffraction structure determination and analysis using using SalR crystal structure, PDB ID 3O26, at 1.2 and 1.7 A resolution, respectively, via molecular replacement, PDB ID 5LCX
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type enzyme from Escherichia coli strain BL21(DE3) to over 60% homogeneity, and to over 90% purity for the truncated mutant enzyme
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, functional expression of wild-type enzyme in Escherichia coli strain BL21(DE3), expression of a mutant cloning artifact that has a seven residue deletion at the C-terminus and bores an additional 33 vector-derived residues
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gene ipr, DNA and amino acid sequence determination and analysis, sequence comparisons
gene iPR, sequence comparisons, semi-quantitative RT-PCR enzyme exxpression analysis
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
penconazole and drought stresses alter the essential oil composition of the plant, the amount of (+)-cis-isopulegone is about 2fold increased. Penconazole and drought stress upregulates the iPR enzyme expression
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E238Y
site-directed mutagenesis, the mutant shows highly altered substrate specificity compared to the wild-type enzyme