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| {{enzyme
| | The writer's name is Christy Brookins. She works as a journey agent but soon she'll be on her personal. It's not a typical factor but what I like doing is to climb but I don't have the time recently. Kentucky is exactly where I've usually been residing.<br><br>Have a look at my page; real psychics ([http://appin.co.kr/board_Zqtv22/688025 http://appin.co.kr/board_Zqtv22/688025]) |
| | Name = tropinone reductase
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| | EC_number = 1.1.1.236
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| | CAS_number = 136111-61-0
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| | IUBMB_EC_number = 1/1/1/236
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| | GO_code = 0050358
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| In [[enzymology]], a '''tropinone reductase II''' ({{EC number|1.1.1.236}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]
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| :pseudotropine + NADP<sup>+</sup> <math>\rightleftharpoons</math> tropinone + NADPH + H<sup>+</sup>
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| Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[pseudotropine]] and [[nicotinamide adenine dinucleotide phosphate|NADP<sup>+</sup>]], whereas its 3 [[product (chemistry)|products]] are [[tropinone]], [[nicotinamide adenine dinucleotide phosphate|NADPH]], and [[hydrogen ion|H<sup>+</sup>]].
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| This enzyme belongs to the family of [[oxidoreductase]]s, specifically those acting on the CH-OH group of donor with NAD<sup>+</sup> or NADP<sup>+</sup> as acceptor. The systematic name of this enzyme class is '''pseudotropine:NADP<sup>+</sup> 3-oxidoreductase'''. Other names in common use include '''tropinone (psi-tropine-forming) reductase''', '''pseudotropine forming tropinone reductase''', '''tropinone reductase (ambiguous)''', and '''TR-II'''. This enzyme participates in [[alkaloid biosynthesis ii]].
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| ==Structural studies==
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| As of late 2007, 6 [[tertiary structure|structures]] have been solved for this class of enzymes, with [[Protein Data Bank|PDB]] accession codes {{PDB link|1AE1}}, {{PDB link|1IPE}}, {{PDB link|1IPF}}, {{PDB link|1XHL}}, {{PDB link|2AE1}}, and {{PDB link|2AE2}}.
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| ==References==
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| {{reflist|1}}
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| * {{cite journal | author = Drager B, Hashimoto T and Yamada Y | date = 1988 | title = Purification and characterization of pseudotropine forming tropinone reductase from ''Hyoscyamus niger'' root cultures | journal = Agric. Biol. Chem. | volume = 52 | pages = 2663–2667 | doi = 10.1271/bbb1961.52.2663 | issue = 10 }}
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| * {{cite journal | author = Couladis MM, Friesen JB, Landgrebe ME and Leete E | date = 1991 | title = Enzymes catalysing the reduction of tropinone to tropine and ψ-tropine isolated from the roots of ''Datura innoxia'' | journal = Pytochemistry | volume = 30 | pages = 801–805 | doi = 10.1016/0031-9422(91)85255-X | issue = 3 }}
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| * {{cite journal | author = Nakajima K, Hashimoto T, Yamada Y | date = 1993 | title = Two tropinone reductases with different stereospecificities are short-chain dehydrogenases evolved from a common ancestor | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 90 | pages = 9591–5 | pmid = 8415746 | doi = 10.1073/pnas.90.20.9591 | issue = 20 | pmc = 47615 }}
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| * {{cite journal | author = Drager B | date = 2006 | title = Tropinone reductases, enzymes at the branch point of tropane alkaloid metabolism | journal = [[Phytochemistry (journal)|Phytochemistry]]. | volume = 67 | pages = 327–37 | pmid = 16426652 | doi = 10.1016/j.phytochem.2005.12.001 | issue = 4 }}
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| [[Category:EC 1.1.1]]
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| [[Category:NADPH-dependent enzymes]]
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| [[Category:Enzymes of known structure]]
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| {{1.1.1-enzyme-stub}}
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The writer's name is Christy Brookins. She works as a journey agent but soon she'll be on her personal. It's not a typical factor but what I like doing is to climb but I don't have the time recently. Kentucky is exactly where I've usually been residing.
Have a look at my page; real psychics (http://appin.co.kr/board_Zqtv22/688025)