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Literature summary for 1.14.11.31 extracted from

  • Kachhap, S.; Wojdyla, Z.; Komorek, P.; Kluza, A.; Kurpiewska, K.; Jachimska, B.; Borowski, T.
    It takes two to tango - The case of thebaine 6-O-demethylase (2020), Int. J. Biol. Macromol., 163, 718-729 .
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Papaver somniferum D4N500
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General Information

General Information Comment Organism
metabolism the enzyme-substrate complex of T6ODM has a 1:2 stoichiometry. The key residues responsible for substrate binding are Val128, Glu133, Met150 and Agr219 for the substrate in the distal position, and Asp144, Leu235 and Leu353 for the proximal substrate molecule. Tthe oxo ligand is bound trans to His295 and the enzyme catalyzes hydroxylation of the C6-bound methoxy group according to the established rebound mechanism. The final stage of the demethylation reaction includes deformylation and enol-keton tautomerization steps and is most likely catalyzed by water molecules and takes place in the solvent Papaver somniferum