DB code: S00332

RLCP classification 9.1050.440000.8010 : Hydride transfer
9.5010.536200.8010 : Hydride transfer
CATH domain 3.40.50.720 : Rossmann fold Catalytic domain
E.C. 1.1.1.236
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
3.40.50.720 : Rossmann fold S00543 S00551 S00552 S00553 S00602 S00604 S00605 S00608 S00610 S00625 S00319 S00328 S00329 S00330 S00331 D00456 D00457 D00458 S00324 S00320 S00325 S00326 S00327 D00459 S00335 S00336 S00334 T00219 S00339 D00513 D00001 D00002 D00003 D00005 D00007 D00008 D00010 D00012 D00017 D00018 D00023 D00027 D00028 D00031 D00032 D00033 D00034 D00035 D00037 D00048 D00071 D00476 D00481 D00482 D00490 D00492 D00494 D00545 D00601 D00603 D00604 D00605 D00615 D00845 D00857 D00858 M00161 M00171 M00210 T00002 T00010 T00011 T00015 T00227 T00247 T00408 T00414 D00827 D00262 D00274 D00275 M00035 T00109

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Pfam
P50163 Tropinone reductase 2
EC 1.1.1.236
Tropinone reductase II
TR-II
PF00106 (adh_short)
[Graphical View]

KEGG enzyme name
tropinone reductase II
tropinone (psi-tropine-forming) reductase
pseudotropine forming tropinone reductase
tropinone reductase (ambiguous)
TR-II

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P50163 TRN2_DATST Pseudotropine + NADP(+) = tropinone + NADPH. Homodimer.

KEGG Pathways
Map code Pathways E.C.
MAP00960 Alkaloid biosynthesis II

Compound table
Substrates Products Intermediates
KEGG-id C00005 C00783 C00080 C00006 C02066
E.C.
Compound NADPH Tropinone H+ NADP+ Pseudotropine
Type amide group,amine group,nucleotide amine group,carbohydrate others amide group,amine group,nucleotide amine group,carbohydrate
ChEBI 16474
 16474
 		15378
 15378
 		18009
 18009
PubChem 5884
 5884
 		79038
 79038
 		1038
 1038
 		5886
 5886
 		8424
 8424
1ipeA Bound:NDP Unbound Unbound Unbound
1ipeB Bound:NDP Unbound Unbound Unbound
1ipfA Bound:NDP Bound:TNE Unbound Unbound
1ipfB Bound:NDP Bound:TNE Unbound Unbound
2ae1A Unbound Unbound Unbound Unbound
2ae2A Unbound Unbound Bound:NAP Bound:PTO
2ae2B Unbound Unbound Bound:NAP Bound:PTO

Reference for Active-site residues
resource references E.C.
Swiss-prot;P50163, P50162 & literature [4]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1ipeA SER 146;TYR 159;LYS 163
1ipeB SER 146;TYR 159;LYS 163
1ipfA SER 146;TYR 159;LYS 163
1ipfB SER 146;TYR 159;LYS 163
2ae1A SER 146;TYR 159;LYS 163
2ae2A SER 146;TYR 159;LYS 163
2ae2B SER 146;TYR 159;LYS 163

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[3]
p.4879
[4]
Fig.5, p.7636 1
[6]
Fig.4, p.5570-5571 1

References
[1]
Resource
Comments
Medline ID
PubMed ID 7765621
Journal Phytochemistry
Year 1994
Volume 37
Pages 391-400
Authors Portsteffen A, Drager B, Nahrstedt A
Title The reduction of tropinone in Datura stramonium root cultures by two specific reductases.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 10089520
Journal Acta Crystallogr D Biol Crystallogr
Year 1998
Volume 54
Pages 1405-7
Authors Yamashita A, Nakajima K, Kato H, Hashimoto T, Yamada Y, Oda J
Title Crystallization and preliminary crystallographic study of tropinone reductase II from Datura stramonium.
Related PDB
Related UniProtKB
[3]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
Medline ID 98226735
PubMed ID 9560196
Journal Proc Natl Acad Sci U S A
Year 1998
Volume 95
Pages 4876-81
Authors Nakajima K, Yamashita A, Akama H, Nakatsu T, Kato H, Hashimoto T, Oda J, Yamada Y
Title Crystal structures of two tropinone reductases: different reaction stereospecificities in the same protein fold.
Related PDB 1ae1 2ae1
Related UniProtKB P50162 P50163
[4]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
Medline ID 99316165
PubMed ID 10387002
Journal Biochemistry
Year 1999
Volume 38
Pages 7630-7
Authors Yamashita A, Kato H, Wakatsuki S, Tomizaki T, Nakatsu T, Nakajima K, Hashimoto T, Yamada Y, Oda J
Title Structure of tropinone reductase-II complexed with NADP+ and pseudotropine at 1.9 A resolution: implication for stereospecific substrate binding and catalysis.
Related PDB 2ae2
Related UniProtKB P50163
[5]
Resource
Comments
Medline ID
PubMed ID 10347221
Journal J Biol Chem
Year 1999
Volume 274
Pages 16563-8
Authors Nakajima K, Kato H, Oda J, Yamada Y, Hashimoto T
Title Site-directed mutagenesis of putative substrate-binding residues reveals a mechanism controlling the different stereospecificities of two tropinone reductases.
Related PDB
Related UniProtKB
[6]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 12741812
Journal Biochemistry
Year 2003
Volume 42
Pages 5566-73
Authors Yamashita A, Endo M, Higashi T, Nakatsu T, Yamada Y, Oda J, Kato H
Title Capturing enzyme structure prior to reaction initiation: tropinone reductase-II-substrate complexes.
Related PDB 1ipe 1ipf
Related UniProtKB

Comments
This enzyme is homologous to tropinone reductase I (EC 1.1.1.206; S00552 in EzCatDB). Both the enzymes catalyze NADPH-dependent reduction of tropinone, producing different diastereomers. The product of this enzyme is pseudotropine with a beta-hydroxyl group. Moreover, according to the literature [6], this enzyme can catalyze the reverse reaction, that is oxidation of pseudotropine to produce tropinone.
This enzyme belongs to the short-chain dehydrogenase/reductase (SDR) superfamily, along with Drosophia alcohol dehydrogenase (S00319 in EzCatDB). This enzyme has got a catalytic triad composed of conserved residues, Ser, Tyr, and Lys. The conformation of these residues, compared to that of the NAD molecule, seems to be similar to that of the homologous enzymes.
Thus, the catalytic mechanism of this enzyme must be similar to those of the homologues.

Created Updated
2011-06-30 2011-07-01