Tropinone reductase II

In enzymology, a tropinone reductase II (EC 1.1.1.236) is an enzyme that catalyzes the chemical reaction

pseudotropine + NADP+ tropinone + NADPH + H+
tropinone reductase
Identifiers
EC number1.1.1.236
CAS number136111-61-0
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

Thus, the two substrates of this enzyme are pseudotropine 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 pseudotropine:NADP+ 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.

Structural studies

As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes 1AE1, 1IPE, 1IPF, 1XHL, 2AE1, and 2AE2.

References

    • Drager B, Hashimoto T, Yamada Y (1988). "Purification and characterization of pseudotropine forming tropinone reductase from Hyoscyamus niger root cultures". Agric. Biol. Chem. 52 (10): 2663–2667. doi:10.1271/bbb1961.52.2663.
    • Couladis MM, Friesen JB, Landgrebe ME, Leete E (1991). "Enzymes catalysing the reduction of tropinone to tropine and ψ-tropine isolated from the roots of Datura innoxia". Phytochemistry. 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. Bibcode:1993PNAS...90.9591N. 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.


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