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CATH domain | Related DB codes (homologues) |
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3.40.50.720 : Rossmann fold | S00543,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 | UniProtKB | KEGG |
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| P50162 |
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Protein name | Tropinone reductase 1 | tropinone reductase Itropine dehydrogenasetropinone reductase (ambiguous)TR-I |
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Synonyms | EC 1.1.1.206Tropinone reductase ITR-ITropine dehydrogenase |
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Pfam | PF00106 (adh_short) [Graphical view]
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KEGG pathways | MAP code | Pathways |
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MAP00960 | Alkaloid biosynthesis II |
UniProtKB:Accession Number | P50162 |
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Entry name | TRN1_DATST |
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Activity | Tropine + NADP(+) = tropinone + NADPH. |
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Subunit | Homodimer. |
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Subcellular location |
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Cofactor |
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Active-site residues | resource |
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Swiss-prot;P50163, P50162 & literature [4] | pdb | Catalytic residues |
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1ae1A |  |  |  |  |  |  |  | SER 158;TYR 171;LYS 175
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1ae1B |  |  |  |  |  |  |  | SER 158;TYR 171;LYS 175
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References for Catalytic Mechanism | References | Sections | No. of steps in catalysis |
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[3] | p.4879 |
| [4] | Fig.5, p.7636 | 1 | [6] | Fig.4, p.5570-5571 | 1 |
references | [1] |
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PubMed ID | 7765621 |
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Journal | Phytochemistry |
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Year | 1994 |
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Volume | 37 |
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Pages | 391-400 |
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Authors | Portsteffen A, Drager B, Nahrstedt A |
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Title | The reduction of tropinone in Datura stramonium root cultures by two specific reductases. |
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[2] |
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PubMed ID | 10089520 |
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Journal | Acta Crystallogr D Biol Crystallogr |
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Year | 1998 |
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Volume | 54 |
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Pages | 1405-7 |
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Authors | Yamashita A, Nakajima K, Kato H, Hashimoto T, Yamada Y, Oda J |
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Title | Crystallization and preliminary crystallographic study of tropinone reductase II from Datura stramonium. |
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[3] |
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Comments | X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). |
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Medline ID | 98226735 |
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PubMed ID | 9560196 |
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Journal | Proc Natl Acad Sci U S A |
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Year | 1998 |
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Volume | 95 |
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Pages | 4876-81 |
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Authors | Nakajima K, Yamashita A, Akama H, Nakatsu T, Kato H, Hashimoto T, Oda J, Yamada Y |
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Title | Crystal structures of two tropinone reductases: different reaction stereospecificities in the same protein fold. |
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Related PDB | 1ae1,2ae1 |
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Related UniProtKB | P50162,P50163 |
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[4] |
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Comments | X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS). |
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Medline ID | 99316165 |
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PubMed ID | 10387002 |
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Journal | Biochemistry |
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Year | 1999 |
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Volume | 38 |
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Pages | 7630-7 |
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Authors | Yamashita A, Kato H, Wakatsuki S, Tomizaki T, Nakatsu T, Nakajima K, Hashimoto T, Yamada Y, Oda J |
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Title | Structure of tropinone reductase-II complexed with NADP+ and pseudotropine at 1.9 A resolution: implication for stereospecific substrate binding and catalysis. |
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Related PDB | 2ae2 |
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Related UniProtKB | P50163 |
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[5] |
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PubMed ID | 10347221 |
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Journal | J Biol Chem |
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Year | 1999 |
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Volume | 274 |
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Pages | 16563-8 |
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Authors | Nakajima K, Kato H, Oda J, Yamada Y, Hashimoto T |
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Title | Site-directed mutagenesis of putative substrate-binding residues reveals a mechanism controlling the different stereospecificities of two tropinone reductases. |
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[6] |
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Comments | X-ray crystallography |
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PubMed ID | 12741812 |
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Journal | Biochemistry |
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Year | 2003 |
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Volume | 42 |
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Pages | 5566-73 |
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Authors | Yamashita A, Endo M, Higashi T, Nakatsu T, Yamada Y, Oda J, Kato H |
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Title | Capturing enzyme structure prior to reaction initiation: tropinone reductase-II-substrate complexes. |
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Related PDB | 1ipe,1ipf |
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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.
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created | updated |
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2004-07-14 | 2011-07-01 |
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