EC Number   |
General Information |
Reference |
|---|
   1.1.1.236 | 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 |
760748 |
| 1.1.1.236 | evolution |
DnTR2 amino acid sequence contains a conserved Rossmann folding structure, which includes a conserved NAD(P)H binding motif (Gly-X3-Gly-X-Gly) and catalytic residues Ser-Asn-Lys, suggesting that DnTR2 is a member of the SDR superfamily |
740901 |
| 1.1.1.236 | malfunction |
DnTR2 residue Tyr201 is located at the opposite side of Arg110 in the inner substrate binding surface. These structural characters suggest that the disabled tropinone reduction activity of DnTR2 may be caused by the replacement of an uncharged amino acid at position 201 |
740901 |
| 1.1.1.236 | 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 |
-, 763572 |
| 1.1.1.236 | metabolism |
tropinone reductase I is involved in the scopolamine biosynthetic pathway, 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 |
726209 |
| 1.1.1.236 | metabolism |
tropinone reductase I is involved in the scopolamine biosynthetic pathway, 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 |
726209 |
| 1.1.1.236 | 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 |
760748 |
| 1.1.1.236 | more |
three-dimensional structure modeling of DnTR2, catalytic triad Ser-Asn-Lys, role of Tyr201 in substrate binding, structure comparisons, overview |
740901 |
| 1.1.1.236 | physiological function |
pseudotropine forming tropinone reductase (TRII) catalyzes a tropinone reduction competing with TRI, EC 1.1.1.206. StTRII is the main enzyme catalyzing the synthesis of pseudotropine from tropinone. StTRII plays a role in calystegine formation in potato sprouts |
741221 |
