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Literature summary for 1.1.1.206 extracted from

  • Nakajima, K.; Kato, H.; Oda, J.; Yamada, Y.; Hashimoto, T.
    Site-directed mutagenesis of putative substrate-binding residues reveals a mechanism controlling the different stereospecificities of two tropinone reductases (1999), J. Biol. Chem., 274, 16563-16568.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
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Datura stramonium

Protein Variants

Protein Variants Comment Organism
A160S higher Km for tropinone that wild type enzyme Datura stramonium
H112F higher Km for tropinone that wild type enzyme Datura stramonium
H112Y higher Km for tropinone that wild type enzyme Datura stramonium
additional information various mutants: H112Y/A160S, A160S/V168E, V168E/H112Y, H112Y/A160S/V168E, I223L/F226L, H112Y/A160S/V168E/I223L/F226L, all mutants have different Km values for tropinone and NADPH Datura stramonium
V168E lower Km for tropinone that wild type enzyme Datura stramonium

Organism

Organism UniProt Comment Textmining
Datura stramonium
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