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Literature summary extracted from

  • Singh, W.; Hui, C.; Li, C.; Huang, M.
    Thebaine is selectively demethylated by thebaine 6-O-demethylase and codeine-3-O-demethylase at distinct binding sites A computational study (2021), Inorg. Chem., 60, 10199-10214 .
    View publication on PubMed

Organism

EC Number Organism UniProt Comment Textmining
1.14.11.31 Papaver somniferum D4N500
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1.14.11.32 Papaver somniferum D4N502
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General Information

EC Number General Information Comment Organism
1.14.11.31 metabolism thebaine binds at the two distinct sites of T6ODM and codeine-3-O-demethylase CODM, EC 1.14.11.31, which determines the precise regioselectivity at C6 and C3 positions of thebaine respectively. Thebaine binds in site II (characteristic due to the presence of Asp313) of T6ODM for C6 selectivity. It binds in site I (characteristic due to the presence of Asp143) of CODM for C3 selectivity. Thebaine forms stable ionic interaction with these aspartate residues via its positively charged tertiary amino group and is further stabilized by the hydrophobic interactions via its B ring. The binding of oxygen to the nonheme iron is followed by the Fe(IV)=O bond flip, yielding an octahedral intermediate. During the decarboxylation reaction process, the C-terminal lid in the enzyme changes from the closed conformation in the 5C coordinate Fe(IV)=O complex to an active open conformation in the 6C coordinate complex Papaver somniferum
1.14.11.32 metabolism thebaine binds at the two distinct sites of thebaine 6-O-demethylase T6ODM, Ec 1.14.11.31, and codeine-3-O-demethylase CODM, which determines the precise regioselectivity at C6 and C3 positions of thebaine respectively. Thebaine binds in site II (characteristic due to the presence of Asp313) of T6ODM for C6 selectivity. It binds in site I (characteristic due to the presence of Asp143) of CODM for C3 selectivity. Thebaine forms stable ionic interaction with these aspartate residues via its positively charged tertiary amino group and is further stabilized by the hydrophobic interactions via its B ring. The binding of oxygen to the nonheme iron is followed by the Fe(IV)=O bond flip, yielding an octahedral intermediate. During the decarboxylation reaction process, the C-terminal lid in the enzyme changes from the closed conformation in the 5C coordinate Fe(IV)=O complex to an active open conformation in the 6C coordinate complex Papaver somniferum