Crystallization (Comment) | Organism |
---|---|
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 | Mentha x piperita |
Protein Variants | Comment | Organism |
---|---|---|
E238Y | site-directed mutagenesis, the mutant shows highly altered substrate specificity compared to the wild-type enzyme | Mentha x piperita |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
(2S,5R)-5-methyl-2-(propan-2-yl)cyclohexan-1-one + NADP+ | Mentha x piperita | reaction of enzyme mutant E238Y, not of the wild-type enzyme | (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+ | - |
? | |
2,6,6-trimethyl-4-oxocyclohex-2-ene-1-carbaldehyde + NADP+ | Mentha x piperita | - |
2,2,6-trimethyl-4-oxocyclohexane-1-carbaldehyde + NADPH + H+ | - |
? | |
3,5,5-trimethyl-4-(propan-2-yl)cyclohex-2-en-1-one + NADP+ | Mentha x piperita | - |
3,3,5-trimethyl-4-(propan-2-yl)cyclohexan-1-one + NADPH + H+ | - |
? | |
3,5,5-trimethylcyclohex-2-en-1-one + NADP+ | Mentha x piperita | - |
3,3,5-trimethylcyclohexan-1-one + NADPH + H+ | - |
? | |
3,5-dimethylcyclohex-2-en-1-one + NADP+ | Mentha x piperita | - |
3,5-dimethylcyclohexan-1-one + NADPH + H+ | - |
? | |
3-methyl-6-(prop-1-en-2-yl)cyclohex-2-en-1-one + NADP+ | Mentha x piperita | - |
5-methyl-2-(prop-1-en-2-yl)cyclohexan-1-one + NADPH + H+ | - |
? | |
3-methyl-6-(propan-2-yl)cyclohex-2-en-1-one + NADP+ | Mentha x piperita | - |
5-methyl-2-(propan-2-yl)cyclohexan-1-one + NADPH + H+ | - |
? | |
additional information | Mentha x piperita | compound analysis by GS-MS. 3-methyl-6-(prop-1-en-2-yl)cyclohex-2-en-1-one is a poor substrate for enzyme mutant E238Y. Substrate specificity of wild-type and mutant enzymes and ligand binding structure analysis, overview | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mentha x piperita | Q6WAU1 | - |
- |
Source Tissue | Comment | Organism | Textmining |
---|
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(2S,5R)-5-methyl-2-(propan-2-yl)cyclohexan-1-one + NADP+ | reaction of enzyme mutant E238Y, not of the wild-type enzyme | Mentha x piperita | (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+ | - |
? | |
2,6,6-trimethyl-4-oxocyclohex-2-ene-1-carbaldehyde + NADP+ | - |
Mentha x piperita | 2,2,6-trimethyl-4-oxocyclohexane-1-carbaldehyde + NADPH + H+ | - |
? | |
3,5,5-trimethyl-4-(propan-2-yl)cyclohex-2-en-1-one + NADP+ | - |
Mentha x piperita | 3,3,5-trimethyl-4-(propan-2-yl)cyclohexan-1-one + NADPH + H+ | - |
? | |
3,5,5-trimethylcyclohex-2-en-1-one + NADP+ | - |
Mentha x piperita | 3,3,5-trimethylcyclohexan-1-one + NADPH + H+ | - |
? | |
3,5-dimethylcyclohex-2-en-1-one + NADP+ | - |
Mentha x piperita | 3,5-dimethylcyclohexan-1-one + NADPH + H+ | - |
? | |
3-methyl-6-(prop-1-en-2-yl)cyclohex-2-en-1-one + NADP+ | - |
Mentha x piperita | 5-methyl-2-(prop-1-en-2-yl)cyclohexan-1-one + NADPH + H+ | - |
? | |
3-methyl-6-(propan-2-yl)cyclohex-2-en-1-one + NADP+ | - |
Mentha x piperita | 5-methyl-2-(propan-2-yl)cyclohexan-1-one + NADPH + H+ | - |
? | |
additional information | compound analysis by GS-MS. 3-methyl-6-(prop-1-en-2-yl)cyclohex-2-en-1-one is a poor substrate for enzyme mutant E238Y. Substrate specificity of wild-type and mutant enzymes and ligand binding structure analysis, overview | Mentha x piperita | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | enzyme three-dimensional structure analysis, overview | Mentha x piperita |
Synonyms | Comment | Organism |
---|---|---|
IPR | - |
Mentha x piperita |
isopiperitenone reductase | - |
Mentha x piperita |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Mentha x piperita |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6 | - |
assay at | Mentha x piperita |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADP+ | - |
Mentha x piperita |
General Information | Comment | Organism |
---|---|---|
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 | Mentha x piperita |
additional information | the catalytic acid residue in enzyme IPR is Glu238, analysis of its role in reaction mechanism | Mentha x piperita |