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2-methyl-cyclohexanone + NADPH
2-methylcyclohexanol + NADP+
-
-
-
-
?
3-methyl-cyclohexanone + NADPH
3-methylcyclohexanol + NADP+
-
-
-
-
?
3-methyl-cyclohexanone + NADPH
? + NADP+
-
-
-
-
?
3-quinuclidinone + NADPH + H+
1-azabicyclo[2.2.2]octan-3-ol + NADP+
wild-type and mutant Y201V enzymes
-
-
r
4-ethyl-cyclohexanone + NADPH
4-ethylcyclohexanol + NADP+
4-ethyl-cyclohexanone + NADPH
? + NADP+
-
-
-
-
?
4-methyl-cyclohexanone + NADPH
4-methylcyclohexanol + NADP+
4-methyl-cyclohexanone + NADPH
? + NADP+
4-methylcyclohexanone + NADPH + H+
4-methylcyclohexanol + NADP+
wild-type and mutant Y201V enzymes
-
-
r
4-piperidone + NADPH
piperidine-4-ol + NADP+
-
-
-
-
?
4-tetrahydro-thiopyranone + NADP+
?
-
-
-
-
?
4-tetrahydro-thiopyranone + NADPH
? + NADP+
-
-
-
-
?
6-hydroxytropinone + NADPH
? + NADP+
N-(2-fluoroethyl)nortropinone + NADPH
? + NADP+
-
-
-
-
?
N-ethylnortropinone + NADPH
? + NADP+
-
-
-
-
?
N-iso-propylnortropinone + NADPH
? + NADP+
-
-
-
-
?
N-methyl-4-piperidinone + NADPH
? + NADP+
N-methyl-4-piperidone + NADPH
N-methylpiperidin-4-ol + NADP+
N-methyltropinone + NADPH
N-methyl-3-beta-tropine + NADP+
-
-
-
-
ir
N-propyl-4-piperidinone + NADPH
? + NADP+
-
-
-
-
?
N-propyl-4-piperidone + NADPH
N-propylpiperidin-4-ol + NADP+
nortropinone + NADPH
? + NADP+
pseudotropine + NADP+
tropinone + NADPH + H+
-
-
-
r
psi-tropine + NADP+
tropinone + NADPH
-
-
-
r
tetrahydrothiopyran-4-one + NADPH
tetrahydrothiopyran-4-ol + NADP+
tropine + NADP+
tropinone + NADPH
-
-
-
-
r
tropinone + NADPH + H+
pseudotropine + NADP+
tropinone + NADPH + H+
tropine + NADP+
additional information
?
-
4-ethyl-cyclohexanone + NADPH
4-ethylcyclohexanol + NADP+
-
-
-
-
?
4-ethyl-cyclohexanone + NADPH
4-ethylcyclohexanol + NADP+
-
-
-
-
?
4-methyl-cyclohexanone + NADPH
4-methylcyclohexanol + NADP+
-
-
-
-
?
4-methyl-cyclohexanone + NADPH
4-methylcyclohexanol + NADP+
-
-
-
-
?
4-methyl-cyclohexanone + NADPH
? + NADP+
-
-
-
-
?
4-methyl-cyclohexanone + NADPH
? + NADP+
-
-
-
-
?
6-hydroxytropinone + NADPH
? + NADP+
-
-
-
-
?
6-hydroxytropinone + NADPH
? + NADP+
-
-
-
-
?
N-methyl-4-piperidinone + NADPH
? + NADP+
-
-
-
-
?
N-methyl-4-piperidinone + NADPH
? + NADP+
-
-
-
-
?
N-methyl-4-piperidinone + NADPH
? + NADP+
-
-
-
-
?
N-methyl-4-piperidone + NADPH
N-methylpiperidin-4-ol + NADP+
-
-
-
-
?
N-methyl-4-piperidone + NADPH
N-methylpiperidin-4-ol + NADP+
-
-
-
-
?
N-methyl-4-piperidone + NADPH
N-methylpiperidin-4-ol + NADP+
-
more efficient substrate, 230% of activity with tropinone
-
-
?
N-propyl-4-piperidone + NADPH
N-propylpiperidin-4-ol + NADP+
-
-
-
-
?
N-propyl-4-piperidone + NADPH
N-propylpiperidin-4-ol + NADP+
-
-
-
-
?
N-propyl-4-piperidone + NADPH
N-propylpiperidin-4-ol + NADP+
-
more efficient substrate, 300% of activity with tropinone
-
-
?
nortropinone + NADPH
? + NADP+
-
-
-
-
?
nortropinone + NADPH
? + NADP+
-
-
-
-
?
tetrahydrothiopyran-4-one + NADPH
tetrahydrothiopyran-4-ol + NADP+
-
-
-
-
?
tetrahydrothiopyran-4-one + NADPH
tetrahydrothiopyran-4-ol + NADP+
-
-
-
-
?
tropinone + NADPH + H+
pseudotropine + NADP+
-
-
-
-
?
tropinone + NADPH + H+
pseudotropine + NADP+
-
-
-
-
?
tropinone + NADPH + H+
pseudotropine + NADP+
-
-
-
-
ir
tropinone + NADPH + H+
pseudotropine + NADP+
-
-
-
-
?
tropinone + NADPH + H+
pseudotropine + NADP+
-
-
-
-
?
tropinone + NADPH + H+
pseudotropine + NADP+
reaction of tropinone reductase II, EC 1.1.1.236, tropane alkaloid biosynthesis, overview
leading to formation of calystegines
-
?
tropinone + NADPH + H+
pseudotropine + NADP+
reaction of tropinone reductase II, EC 1.1.1.236
-
-
?
tropinone + NADPH + H+
pseudotropine + NADP+
-
-
-
-
?
tropinone + NADPH + H+
pseudotropine + NADP+
-
enzymes fails to catalyze the oxidation of tropine to tropinone in presence of NADP+
-
-
ir
tropinone + NADPH + H+
pseudotropine + NADP+
-
-
-
-
?
tropinone + NADPH + H+
pseudotropine + NADP+
-
-
-
-
ir
tropinone + NADPH + H+
pseudotropine + NADP+
-
-
-
?
tropinone + NADPH + H+
pseudotropine + NADP+
-
pseudotropine oxidation never observed
-
-
ir
tropinone + NADPH + H+
pseudotropine + NADP+
one of the substrates, tropinone, is rotated relative to the en product so as to make the spatial organization in the active site favorable for the reaction to proceed
-
-
?
tropinone + NADPH + H+
pseudotropine + NADP+
recombinant enzyme mutant Y201V, no activity by wild-type TR2 enzyme
-
-
r
tropinone + NADPH + H+
pseudotropine + NADP+
Hyoscyamus bohemicus
-
-
-
-
?
tropinone + NADPH + H+
pseudotropine + NADP+
Hyoscyamus canariensis
-
-
-
-
?
tropinone + NADPH + H+
pseudotropine + NADP+
-
-
-
-
?
tropinone + NADPH + H+
pseudotropine + NADP+
-
-
347972, 347973, 348021, 348022, 348023, 348024, 348025, 348026, 348028, 348030, 348033 -
-
?
tropinone + NADPH + H+
pseudotropine + NADP+
-
-
-
-
ir
tropinone + NADPH + H+
pseudotropine + NADP+
-
reverse reaction very inefficient, about 1.3% of the forward activity
-
-
r
tropinone + NADPH + H+
pseudotropine + NADP+
-
-
-
-
?
tropinone + NADPH + H+
pseudotropine + NADP+
Physalis edulis
-
-
-
-
?
tropinone + NADPH + H+
pseudotropine + NADP+
-
-
-
-
?
tropinone + NADPH + H+
pseudotropine + NADP+
-
-
-
-
?
tropinone + NADPH + H+
pseudotropine + NADP+
-
-
-
-
?
tropinone + NADPH + H+
pseudotropine + NADP+
-
-
-
?
tropinone + NADPH + H+
pseudotropine + NADP+
direction of biosynthesis
-
-
r
tropinone + NADPH + H+
pseudotropine + NADP+
stereospecific reduction of the 3-carbonyl group of tropinone to hydroxyl group (pseudotropine) with distinct stereospecific configuration, product identification by GC-MS analysis
-
-
r
tropinone + NADPH + H+
pseudotropine + NADP+
-
the enzyme is involved in tropane alkaloid biosynthesis, overview
leading to formation of calystegines
-
?
tropinone + NADPH + H+
pseudotropine + NADP+
-
active site structure and catalytic triad, the recombinant His-tagged enzyme shows 4fold higher activity compared to the wild-type enzyme, overview
-
-
?
tropinone + NADPH + H+
pseudotropine + NADP+
-
-
-
-
?
tropinone + NADPH + H+
pseudotropine + NADP+
-
-
-
-
ir
tropinone + NADPH + H+
pseudotropine + NADP+
-
-
-
-
r
tropinone + NADPH + H+
pseudotropine + NADP+
-
Solanum tuberosum tropinone reductase II reduces tropinone in vivo
-
-
r
tropinone + NADPH + H+
tropine + NADP+
-
-
only tropine formed by the reduction of tropinone, no evidence for the formation of psi-tropine
r
tropinone + NADPH + H+
tropine + NADP+
-
tropinone reductase I
-
-
?
tropinone + NADPH + H+
tropine + NADP+
-
tropinone reductase I
-
-
?
additional information
?
-
the bifunctional enzyme of Cochlearia officinalis is not stereospecific, in contrast to the Solanaceae species, and catalyzes both tropinone reductase reactions, a tyrosine residue in the active site of Cochlearia officinalis TR is responsible for binding and orientation of tropinone, overview
-
-
?
additional information
?
-
the enzyme shows broad substrate specificity, several synthetic ketones are accepted as substrates, with higher affinity and faster enzymatic turnover than observed for tropinone, overview
-
-
?
additional information
?
-
-
no activity with quinuclidione and 8-thiabicyclo[3.2.1]octan-2-one
-
-
?
additional information
?
-
-
tropinone feeding experiments
-
-
?
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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
additional information
three-dimensional structure modeling of DnTR2, catalytic triad Ser-Asn-Lys, role of Tyr201 in substrate binding, structure comparisons, overview
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
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
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
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
-
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
-
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
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
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
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Nakajima, K.; Kato, H.; Oda, J.; Yamada, Y.; Hashimoto, T.
Site-directed mutagenesis of putative substrate-binding residues reveals a mechanism controlling the different stereospecificities of two tropinone reductases
J. Biol. Chem.
274
16563-16568
1999
Arabidopsis sp., Datura stramonium, Hyoscyamus niger
brenda
Boswell, H.D.; Drger, B.; McLauchlan W.R.; Portsteffen, A.; Robins D.J.; Robins R.J.; Walton, N.J.
Specificities of the enzymes of N-alkyltropane biosynthesis in Brugmansia and Datura
Phytochemistry
52
871-878
1999
Brugmansia x candida, Datura stramonium, Hyoscyamus niger, Datura stramonium cv. D15/5
brenda
Draeger, B.; Hashimoto, T.; Yamada, Y.
Purification and characterization of pseudotropine forming tropinone reductase from Hyoscyamus niger root cultures
Agric. Biol. Chem.
52
2663-2667
1988
Datura stramonium, Hyoscyamus niger
-
brenda
Couladis, M.M.; Brent Friesen, J.; Landgrebe, M.E.; Leete, E.
Enzymes catalysing the reduction of tropinone to tropine and psi-tropine isolated from the roots of Datura innoxia
Phytochemistry
30
801-805
1991
Atropa belladonna, Datura inoxia, Datura stramonium, Hyoscyamus niger
-
brenda
Draeger, B.; Portsteffen, A.; Schaal, A.; McCabe, P.H.; Peerless, A.C.J.; Robins, R.J.
Levels of tropinone reductase activities influence the spectrum of tropane esters found in transformed root cultures of Daura stramonium L.
Planta
188
581-586
1992
Atropa belladonna, Datura inoxia, Datura stramonium, Hyoscyamus niger, Physalis peruviana
brenda
Hashimoto, T.; Nakajima, K.; Ongena, G.; Yamada, Y.
Two tropinone reductases with distinct stereospecificities from cultured roots of Hyoscyamus niger
Plant Physiol.
100
836-845
1992
Hyoscyamus niger
brenda
Portsteffen, A.; Draeger, B.; Nahrstedt, A.
Two tropinone reducing enzymes from Datura stramonium transformed root cultures
Phytochemistry
31
1135-1138
1992
Atropa belladonna, Calystegia sepium, Datura inoxia, Datura stramonium, Hyoscyamus bohemicus, Hyoscyamus canariensis, Hyoscyamus muticus, Hyoscyamus niger, Hyoscyamus pusillus, no activity in Brassica campestris, no activity in Browallia americana, no activity in Nicotiana tabacum, Alkekengi officinarum, Physalis edulis, Physalis philadelphica, Physochlaina orientalis
-
brenda
Nakajima, K.; Hashimoto, T.; Yamada, Y.
Two tropinone reductases with different stereospecificities are short-chain dehydrogenases evolved from a common ancestor
Proc. Natl. Acad. Sci. USA
90
9591-9595
1993
Atropa belladonna, Datura stramonium, Hyoscyamus niger, no activity in Nicotiana tabacum
brenda
Portsteffen, A.; Draeger, B.; Nahrstedt, A.
The reduction of tropinone in Datura stramonium root cultures by two specific reductases
Phytochemistry
37
391-400
1994
Atropa belladonna, Datura stramonium
brenda
Nakajima, K.; Yamashita, A.; Akama, H.; Nakatsu, T.; Kato, H.; Hashimoto, T.; Oda, J.; Yamada, Y.
Crystal structures of two tropinone reductases: Different reaction stereospecificities in the same protein fold
Proc. Natl. Acad. Sci. USA
95
4876-4881
1998
Datura stramonium, Hyoscyamus niger
brenda
Nakajima, K.; Hashimoto, T.
Two tropinone reductases, that catalyze opposite stereospecific reductions in tropane alkaloid biosynthesis, are localized in plant root with different cell-specific patterns
Plant Cell Physiol.
40
1099-1107
1999
Atropa belladonna, Datura stramonium, Hyoscyamus niger, no activity in Nicotiana tabacum
brenda
Yamashita, A.; Kato, H.; Wakatsuki, S.; Tomizaki, T.; Nakatsu, T.; Nakajima, K.; Hashimoto, T.; Yamada, Y.; Oda, J.
Structure of tropinone reductase-II complexed with NADP+ and pseudotropine at 1.9 A resolution: implication for stereospecific substrate binding and catalysis
Biochemistry
38
7630-7637
1999
Datura stramonium (P50163)
brenda
Keiner, R.; Kaiser, H.; Nakajima, K.; Hashimoto, T.; Draeger, B.
Molecular cloning, expression and characterization of tropinone reductase II, an enzyme of the SDR family in Solanum tuberosum (L.)
Plant Mol. Biol.
48
299-308
2002
Atropa belladonna, Datura stramonium, Hyoscyamus niger, Solanum tuberosum
brenda
Yamashita, A.; Endo, M.; Higashi, T.; Nakatsu, T.; Yamada, Y.; Oda, J.; Kato, H.
Capturing enzyme structure prior to reaction initiation: tropinone reductase-II-substrate complexes
Biochemistry
42
5566-5573
2003
Datura stramonium (P50163)
brenda
Richter, U.; Rothe, G.; Fabian, A.K.; Rahfeld, B.; Drager, B.
Overexpression of tropinone reductases alters alkaloid composition in Atropa belladonna root cultures
J. Exp. Bot.
56
645-652
2005
Datura stramonium (P50163)
brenda
Draeger, B.
Tropinone reductases, enzymes at the branch point of tropane alkaloid metabolism
Phytochemistry
67
327-337
2006
Atropa belladonna, Datura stramonium, Hyoscyamus niger, Solanum tuberosum
brenda
Kaiser, H.; Richter, U.; Keiner, R.; Brabant, A.; Hause, B.; Draeger, B.
Immunolocalisation of two tropinone reductases in potato (Solanum tuberosum L.) root, stolon, and tuber sprouts
Planta
225
127-137
2006
Solanum tuberosum
brenda
Brock, A.; Brandt, W.; Draeger, B.
The functional divergence of short-chain dehydrogenases involved in tropinone reduction
Plant J.
54
388-401
2008
Cochlearia officinalis (A7DY56)
brenda
Freydank, A.C.; Brandt, W.; Draeger, B.
Protein structure modeling indicates hexahistidine-tag interference with enzyme activity
Proteins
72
173-183
2008
Solanum dulcamara
brenda
Kai, G.; Li, L.; Jiang, Y.; Yan, X.; Zhang, Y.; Lu, X.; Liao, P.; Chen, J.
Molecular cloning, characterization of two tropinone reductases in Anisodus acutangulus and enhancement of tropane alkaloids production in AaTRI-transformed hairy roots
Biotechnol. Appl. Biochem.
54
:177-186
2009
Anisodus acutangulus (B2L2W9)
brenda
Dehghan, E.; Shahriari Ahmadi, F.; Ghotbi Ravandi, E.; Reed, D.W.; Covello, P.S.; Bahrami, A.R.
An atypical pattern of accumulation of scopolamine and other tropane alkaloids and expression of alkaloid pathway genes in Hyoscyamus senecionis
Plant Physiol. Biochem.
70C
188-194
2013
Hyoscyamus muticus, Hyoscyamus senecionis
brenda
Cheng, X.; Chen, W.; Zhou, Z.; Liu, J.; Wang, H.
Functional characterization of a novel tropinone reductase-like gene in Dendrobium nobile Lindl
J. Plant Physiol.
170
958-964
2013
Dendrobium nobile (H9BQR9)
brenda
Kuester, N.; Rosahl, S.; Draeger, B.
Potato plants with genetically engineered tropane alkaloid precursors
Planta
245
355-365
2017
Solanum tuberosum
brenda
Wu, N.; Jian, D.; Xiang, M.; Chen, M.; Lan, X.; Liao, Z.; Liu, X.
Biochemical characterization reveals the functional divergence of two tropinone reductases from Przewalskia tangutica
Biotechnol. Appl. Biochem.
66
597-606
2019
Przewalskia tangutica (A0A6B7HD48)
brenda
Dehghan, E.; Reed, D.W.; Covello, P.S.; Hasanpour, Z.; Palazon, J.; Oksman-Caldentey, K.M.; Ahmadi, F.S.
Genetically engineered hairy root cultures of Hyoscyamus senecionis and H. muticus ploidy as a promising parameter in the metabolic engineering of tropane alkaloids
Plant Cell Rep.
36
1615-1626
2017
Hyoscyamus muticus, Hyoscyamus senecionis, Hyoscyamus muticus Cairo
brenda