Tropinone reductase I
tropine dehydrogenase | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||
EC number | 1.1.1.206 | ||||||||
CAS number | 118390-87-7 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / EGO | ||||||||
|
In enzymology, a tropinone reductase I (EC 1.1.1.206) is an enzyme that catalyzes the chemical reaction
- tropine + NADP+ tropinone + NADPH + H+
Thus, the two substrates of this enzyme are tropine and NADP+, whereas its 3 products are tropinone, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is tropine:NADP+ 3alpha-oxidoreductase. Other names in common use include tropine dehydrogenase, tropinone reductase (ambiguous), and TR-I. This enzyme participates in alkaloid biosynthesis ii.
References
- Koelen KJ and Gross, GG (1982). "Partial purification and properties of tropine dehydrogenase from root cultures of Datura stramonium". Planta Med. 44 (4): 227–230. doi:10.1055/s-2007-971454. PMID 17402126.
- Couladis MM, Friesen JB, Landgrebe ME and Leete E (1991). "Enzymes catalysing the reduction of tropinone to tropine and ψ-tropine isolated from the roots of Datura innoxia'". Pytochemistry 30 (3): 801–805. doi:10.1016/0031-9422(91)85255-X.
- Nakajima K, Hashimoto T, Yamada Y (1993). "Two tropinone reductases with different stereospecificities are short-chain dehydrogenases evolved from a common ancestor". Proc. Natl. Acad. Sci. U.S.A. 90 (20): 9591–5. doi:10.1073/pnas.90.20.9591. PMC 47615. PMID 8415746.
- Drager B (2006). "Tropinone reductases, enzymes at the branch point of tropane alkaloid metabolism". Phytochemistry. 67 (4): 327–37. doi:10.1016/j.phytochem.2005.12.001. PMID 16426652.
|
This article is issued from Wikipedia - version of the Wednesday, March 30, 2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.