EzCatDB: S00552
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DB codeS00552
RLCP classification9.1050.440000.8010 : Hydride transfer
9.5010.536200.8010 : Hydride transfer
CATH domainDomain 13.40.50.720 : Rossmann foldCatalytic domain
E.C.1.1.1.206

CATH domainRelated DB codes (homologues)
3.40.50.720 : Rossmann foldS00543,S00551,S00553,S00602,S00604,S00605,S00608,S00610,S00625,S00319,S00328,S00329,S00330,S00331,S00332,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

P50162
Protein nameTropinone reductase 1tropinone reductase I
tropine dehydrogenase
tropinone reductase (ambiguous)
TR-I
SynonymsEC 1.1.1.206
Tropinone reductase I
TR-I
Tropine dehydrogenase
PfamPF00106 (adh_short)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00960Alkaloid biosynthesis II

UniProtKB:Accession NumberP50162
Entry nameTRN1_DATST
ActivityTropine + NADP(+) = tropinone + NADPH.
SubunitHomodimer.
Subcellular location
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC00005C00783C00080C00006C00729
CompoundNADPHTropinoneH+NADP+Tropine
Typeamide group,amine group,nucleotideamine group,carbohydrateothersamide group,amine group,nucleotideamine group,carbohydrate
ChEBI16474

15378
18009

PubChem5884
79038
1038
5886
8424
             
1ae1AUnboundUnbound Bound:NAPUnbound
1ae1BUnboundUnbound Bound:NAPUnbound

Active-site residues
resource
Swiss-prot;P50163, P50162 & literature [4]
pdbCatalytic residues
         
1ae1ASER 158;TYR 171;LYS 175
1ae1BSER 158;TYR 171;LYS 175

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 II (EC 1.1.1.236; S00332 in EzCatDB). Both the enzymes catalyze NADPH-dependent reduction of tropinone, producing different diastereomers. The product of this enzyme is tropine with an alpha-hydroxyl group.
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
2004-07-142011-07-01
Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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