1.1.1.206: tropinone reductase I
This is an abbreviated version!
For detailed information about tropinone reductase I, go to the full flat file.
Word Map on EC 1.1.1.206
-
1.1.1.206
-
tropane
-
reductases
-
hyoscyamine
-
scopolamine
-
datura
-
pseudotropine
-
stramonium
-
solanaceae
-
calystegines
-
putrescine
-
n-methyltransferase
-
solanaceous
-
3-quinuclidinone
-
synthesis
-
nortropane
- 1.1.1.206
-
tropane
- reductases
- hyoscyamine
- scopolamine
- datura
- pseudotropine
- stramonium
- solanaceae
-
calystegines
- putrescine
- n-methyltransferase
-
solanaceous
- 3-quinuclidinone
- synthesis
-
nortropane
Reaction
Synonyms
BaTRI, dehydrogenase, tropine, DnTR1, DsTRI, EC 1.1.1.293, More, TR-I, TR1, TRI, Tri2, tropine biosynthetic tropinone reductase, Tropine dehydrogenase, tropine-forming reductase, tropine-forming tropinone reductase, tropinone reductase, tropinone reductase I, tropinone reductase II, tropinone reductase-I, tropinone reductase-I 2, WcTR-I, WsTR-I, WsTR-I protein
ECTree
Advanced search results
General Information
General Information on EC 1.1.1.206 - tropinone reductase I
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
evolution
malfunction
metabolism
physiological function
additional information
tropinone reductase TR-I belongs to the short chain dehydrogenase/reductase family, SDR, of enzymes and has a YSASK as the signature YXXXK motif of SDRs, catalytic tetrade comprises N, S, Y, and K residues, overview
evolution
enzyme TRI belongs to the family of short chain dehydrogenases/reductases (SDRs) that catalyse NAD(P)(H)-dependent redox reactions
evolution
enzyme TRI belongs to the family of short chain dehydrogenases/reductases (SDRs) that catalyse NAD(P)(H)-dependent redox reactions
evolution
the enzyme belongs to the short chain dehydrogenase/reductase (SDR) superfamily that is composed of a group of NAD(P)H-dependent oxidoreductases that typically consist of 250-350 amino acids. Tropinone reductases (TRs) are a group of the SDR superfamily, that use the NADPH as coenzyme to reduce tropinone DnTR1 also contains the sequence pattern G-X3-G-X-G in the cofactor binding motif and active site motif (S-N-K)
evolution
tropinone reductases (TRs) are small proteins belonging to the SDR (short chain dehydrogenase/reductase) family of enzymes. The enzyme's sequence contains the signature YXXXK motif of SDRs. Residues His112, Ala160, Val168, Ile223 and Phe226 are conserved in the TRs, and conserved at corresponding positions in WcTR-I, and involved in stereospecificity of the respective TR-Is. Tropane alkaloids might have evolved independently in plants, at least in Solanaceae and Erythroxylaceae
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
-
effects of overexpression of putrescine N-methyltransferase (EC 2.1.1.53, Pmt) and hyoscyamine 6beta-hydroxylase (EC 1.14.11.11, H6h) in Hyoscyamus senecionis plants on TRI and TRII enzyme expression rates, plant growth rates, and alkaloids content, overview
malfunction
-
effects of overexpression of putrescine N-methyltransferase (EC 2.1.1.53, Pmt) and hyoscyamine 6beta-hydroxylase (EC 1.14.11.11, H6h) in Hyoscyamus senecionis plants on TRI and TRII enzyme expression rates, plant growth rates, and alkaloids content, overview
malfunction
Hyoscyamus muticus Cairo
-
effects of overexpression of putrescine N-methyltransferase (EC 2.1.1.53, Pmt) and hyoscyamine 6beta-hydroxylase (EC 1.14.11.11, H6h) in Hyoscyamus senecionis plants on TRI and TRII enzyme expression rates, plant growth rates, and alkaloids content, overview
-
the enzyme catalyzes a step intermediary enroute to biosynthesis of tropane esters of medicinal importance, i.e. hyoscyamine/scopolamine
metabolism
-
tropinone reductase II is part of biosynthesis of calystegines, overview. Hyoscyamine is the main tropane alkaloid of the leaf and root of Hyoscyamus muticus. Higher amounts of littorine as an intermediate compound in the pathway, and 3'-hydroxylittorine are accumulated in roots than in other organs
metabolism
-
tropinone reductase II is part of biosynthesis of calystegines, overview. Scopolamine is the main tropane alkaloid compound in Hyoscyamus senecionis leaves. Higher amounts of littorine as an intermediate compound in the pathway, and 3'-hydroxylittorine are accumulated in roots than in other organs
metabolism
enzymes TR-I and TR-II catalyze the conversion of tropinone into tropane alcohols (tropine and pseudotropine, respectively). The steps are intermediary enroute to biosynthesis of tropane esters of medicinal importance, hyoscyamine/scopolamine, and calystegins, respectively. The enzyme has a wide substrate specificity but does not cover the substrates of other plant SDR enzymes related to menthol metabolism. The leaf tissue expression of the enzyme with these catalytic features suggests physiologically much prodigal rate of operation of the tropane alkaloid pathway in the leaf tissue itself
metabolism
the enzyme catalyzes the NADPH-dependent tropinone to tropine conversion step in tropane metabolism, metabolic pathway of tropane alkaloid biosynthesis, overview
metabolism
tropinone reductases form a branch point in the pathway leading to tropine (TRI) and to pseudotropine (TRII) during the tropane alkaloid biosynthesis, overview. Enzyme TRI is involved in the formation of tropine, the preproduct of hyoscyamine, whereas enzyme TRII, EC 1.1.1.236, is responsible for the generation of pseudotropine
metabolism
two tropinone reductases (TRs) constitute an important branch point in the tropanalkaloid biosynthetic pathway. Tropinone reductase I or tropine-forming reductase, EC 1.1.1.206, reduces tropinone to tropine during tropanalkaloid biosynthesis, whereas tropinone reductase II, EC 1.1.1.236, reduces tropinone to pseudotropine, diverging metabolic flux to nortropane calystegine A3. TRI activity controls metabolic flux towards hyoscyamine and downstream tropanalkaloids' biosynthesis
metabolism
two tropinone reductases (TRs) constitute an important branch point in the tropanalkaloid biosynthetic pathway. Tropinone reductase I or tropine-forming reductase, EC 1.1.1.206, reduces tropinone to tropine during tropanalkaloid biosynthesis, whereas tropinone reductase II, EC 1.1.1.236, reduces tropinone to pseudotropine, diverging metabolic flux to nortropane calystegine A3. TRI activity controls metabolic flux towards hyoscyamine and downstream tropanalkaloids' biosynthesis
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
DnTR1 regulation may be involved in a jasmonate-dependent pathway
physiological function
physiological role of tropinone reductase enzyme in tropane alkaloid biosynthesis in aerial tissues of the plant. The metabolic step of tropine formation may be regulated by, besides through the transcript and protein levels, the tissue concentration of tropinone
physiological function
tropine forming tropinone reductase (TRI) catalyzes a tropinone reduction competing with TRII, EC 1.1.1.236. Tropine formation is essential in the course of the biosynthesis of the medicinal tropine alkaloids atropine and scopolamine that are not found in potato
physiological function
in TRI-overexpressing root cultures, the hyoscyamine contents are 1.7- to 2.9fold higher than those in control
superimposition of three-dimensional models of tropinone reductases,overview
additional information
-
superimposition of three-dimensional models of tropinone reductases,overview
additional information
a three dimensional model is prepared by taking Datura stramonium TR-II, PDB ID 1ipf, as template, structure comparison, overview
additional information
-
a three dimensional model is prepared by taking Datura stramonium TR-II, PDB ID 1ipf, as template, structure comparison, overview
additional information
enzyme three-dimensional structure modelling
additional information
enzyme three-dimensional structure molecular modeling, overview
additional information
-
enzyme three-dimensional structure molecular modeling, overview
additional information
three-dimensional enzyme structure comparisons, overview
additional information
three-dimensional structure modelling of DnTR1, overview. DnTR1 also contains the sequence pattern G-X3-G-X-G in the cofactor binding motif and active site motif (S-N-K). The positive and negative charges on the binding pockets surface of DsTRI are due to His112. The three catalytic residues are Ser158, Tyr171, and Lys175 in DsTRI
additional information
-
three-dimensional structure modelling of DnTR1, overview. DnTR1 also contains the sequence pattern G-X3-G-X-G in the cofactor binding motif and active site motif (S-N-K). The positive and negative charges on the binding pockets surface of DsTRI are due to His112. The three catalytic residues are Ser158, Tyr171, and Lys175 in DsTRI