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Literature summary for 1.1.1.236 extracted from
- Biochemical characterization reveals the functional divergence of two tropinone reductases from Przewalskia tangutica (2019), Biotechnol. Appl. Biochem., 66, 597-606 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| TRII, DNA and amino acid sequence determiation and analysis, phylogenetic analysis and tree, quantitative real-time PCR expression level analysis, recombinant epression in Escherichia coli strain Rosetta (DE3) | Przewalskia tangutica |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Michaelis-Menten kinetics | Przewalskia tangutica | |
| 0.087 | - |
tropinone | pH 6.4, 30°C, enzyme TRII | Przewalskia tangutica |  |
| 0.87 | - |
tropinone | pH 6.4, 30°C | Przewalskia tangutica | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| pseudotropine + NADP+ | Przewalskia tangutica | - |
tropinone + NADPH + H+ | - |
r | |
| tropinone + NADPH + H+ | Przewalskia tangutica | direction of biosynthesis | pseudotropine + NADP+ | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Przewalskia tangutica | A0A6B7HD48 | - |
- |
| Przewalskia tangutica | A0A6B7HD48 | isoform tropinone reductase II | - |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| leaf | - |
Przewalskia tangutica | - |
| leaf | low expression level | Przewalskia tangutica | - |
| additional information | PtTRII is expressed in the roots and stems at higher levels than in the leaves, tissue profiling analysis of PtTRII | Przewalskia tangutica | - |
| root | - |
Przewalskia tangutica | - |
| root | high expression level | Przewalskia tangutica | - |
| stem | - |
Przewalskia tangutica | - |
| stem | about half of the expression in root | Przewalskia tangutica | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| pseudotropine + NADP+ | - |
Przewalskia tangutica | tropinone + NADPH + H+ | - |
r | |
| tropinone + NADPH + H+ | - |
Przewalskia tangutica | pseudotropine + NADP+ | - |
? | |
| tropinone + NADPH + H+ | direction of biosynthesis | Przewalskia tangutica | pseudotropine + NADP+ | - |
r | |
| tropinone + NADPH + H+ | stereospecific reduction of the 3-carbonyl group of tropinone to hydroxyl group (pseudotropine) with distinct stereospecific configuration, product identification by GC-MS analysis | Przewalskia tangutica | pseudotropine + NADP+ | - |
r | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 29100, calculated from sequence and SDS-PAGE | Przewalskia tangutica |
| ? | x * 29100, recombinant enzyme, SDS-PAGE | Przewalskia tangutica |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| pseudotropine reductase II | - |
Przewalskia tangutica |
| TRII | - |
Przewalskia tangutica |
| tropinone reductase II | - |
Przewalskia tangutica |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Przewalskia tangutica |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 10.26 | - |
tropinone | pH 6.4, 30°C, enzyme TRI | Przewalskia tangutica | |
| 116.9 | - |
tropinone | pH 6.4, 30°C | Przewalskia tangutica | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6.8 | - |
- |
Przewalskia tangutica |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NADP+ | - |
Przewalskia tangutica | |
| NADPH | the enzyme has a NADPH-binding site with a typical sequence characterized by the GXXXGXG motif | Przewalskia tangutica | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | both PtTRI and PtTRII have a conserved NADPH-binding site with a typical sequence characterized by the GXXXGXG motif. There are also two conserved domains in the amino acid sequence: the NNAG domain that is unique to the short-chain dehydrogenase family and the S-Y-K structure which is unique to TRs | Przewalskia tangutica |
| metabolism | two tropinone reductases (TRs) with a similar amino acid sequence constitute a branching point in TA metabolism. Both catalyze the stereospecific reduction of the 3-carbonyl group of tropinone to hydroxyl groups (tropine) with different stereospecific configurations. Tropinone reductase I (TRI, EC 1.1.1.206) reduces the ketone to the alcohol in the tropine ring to give products such as hyoscyamine and scopolamine, whereas pseudotropine reductase II (TRII) reduces tropinone to pseudotropine to give products of opposite configuration, such as the ones participating in the biosynthesis of nortropane alkaloids including calystegines. TRI and TRII compete for the same substrate tropinone. TRI plays an important role in tropane alkaloids biosynthesis | Przewalskia tangutica |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 117.9 | - |
tropinone | pH 6.4, 30°C, enzyme TRI | Przewalskia tangutica | |
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Release 2023.1 (January 2023)
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