EzCatDB: S00332
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DB codeS00332
RLCP classification9.1050.440000.8010 : Hydride transfer
9.5010.536200.8010 : Hydride transfer
CATH domainDomain 13.40.50.720 : Rossmann foldCatalytic domain
E.C.1.1.1.236

CATH domainRelated DB codes (homologues)
3.40.50.720 : Rossmann foldS00543,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

Enzyme Name
UniProtKBKEGG

P50163
Protein nameTropinone reductase 2tropinone reductase II
tropinone (psi-tropine-forming) reductase
pseudotropine forming tropinone reductase
tropinone reductase (ambiguous)
TR-II
SynonymsEC 1.1.1.236
Tropinone reductase II
TR-II
PfamPF00106 (adh_short)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00960Alkaloid biosynthesis II

UniProtKB:Accession NumberP50163
Entry nameTRN2_DATST
ActivityPseudotropine + NADP(+) = tropinone + NADPH.
SubunitHomodimer.
Subcellular location
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC00005C00783C00080C00006C02066
CompoundNADPHTropinoneH+NADP+Pseudotropine
Typeamide group,amine group,nucleotideamine group,carbohydrateothersamide group,amine group,nucleotideamine group,carbohydrate
ChEBI16474

15378
18009

PubChem5884
79038
1038
5886
8424
             
1ipeABound:NDPUnbound UnboundUnbound
1ipeBBound:NDPUnbound UnboundUnbound
1ipfABound:NDPBound:TNE UnboundUnbound
1ipfBBound:NDPBound:TNE UnboundUnbound
2ae1AUnboundUnbound UnboundUnbound
2ae2AUnboundUnbound Bound:NAPBound:PTO
2ae2BUnboundUnbound Bound:NAPBound:PTO

Active-site residues
resource
Swiss-prot;P50163, P50162 & literature [4]
pdbCatalytic residues
         
1ipeASER 146;TYR 159;LYS 163
1ipeBSER 146;TYR 159;LYS 163
1ipfASER 146;TYR 159;LYS 163
1ipfBSER 146;TYR 159;LYS 163
2ae1ASER 146;TYR 159;LYS 163
2ae2ASER 146;TYR 159;LYS 163
2ae2BSER 146;TYR 159;LYS 163

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[3]p.4879
[4]Fig.5, p.76361
[6]Fig.4, p.5570-55711

references
[1]
PubMed ID7765621
JournalPhytochemistry
Year1994
Volume37
Pages391-400
AuthorsPortsteffen A, Drager B, Nahrstedt A
TitleThe reduction of tropinone in Datura stramonium root cultures by two specific reductases.
[2]
PubMed ID10089520
JournalActa Crystallogr D Biol Crystallogr
Year1998
Volume54
Pages1405-7
AuthorsYamashita A, Nakajima K, Kato H, Hashimoto T, Yamada Y, Oda J
TitleCrystallization and preliminary crystallographic study of tropinone reductase II from Datura stramonium.
[3]
CommentsX-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
Medline ID98226735
PubMed ID9560196
JournalProc Natl Acad Sci U S A
Year1998
Volume95
Pages4876-81
AuthorsNakajima K, Yamashita A, Akama H, Nakatsu T, Kato H, Hashimoto T, Oda J, Yamada Y
TitleCrystal structures of two tropinone reductases: different reaction stereospecificities in the same protein fold.
Related PDB1ae1,2ae1
Related UniProtKBP50162,P50163
[4]
CommentsX-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
Medline ID99316165
PubMed ID10387002
JournalBiochemistry
Year1999
Volume38
Pages7630-7
AuthorsYamashita A, Kato H, Wakatsuki S, Tomizaki T, Nakatsu T, Nakajima K, Hashimoto T, Yamada Y, Oda J
TitleStructure of tropinone reductase-II complexed with NADP+ and pseudotropine at 1.9 A resolution: implication for stereospecific substrate binding and catalysis.
Related PDB2ae2
Related UniProtKBP50163
[5]
PubMed ID10347221
JournalJ Biol Chem
Year1999
Volume274
Pages16563-8
AuthorsNakajima K, Kato H, Oda J, Yamada Y, Hashimoto T
TitleSite-directed mutagenesis of putative substrate-binding residues reveals a mechanism controlling the different stereospecificities of two tropinone reductases.
[6]
CommentsX-ray crystallography
PubMed ID12741812
JournalBiochemistry
Year2003
Volume42
Pages5566-73
AuthorsYamashita A, Endo M, Higashi T, Nakatsu T, Yamada Y, Oda J, Kato H
TitleCapturing enzyme structure prior to reaction initiation: tropinone reductase-II-substrate complexes.
Related PDB1ipe,1ipf

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.

createdupdated
2011-06-302011-07-01


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Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
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Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
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