Title : Comparison of catalytical activity and stereoselectivity between the recombinant human cytochrome P450 2D6.1 and 2D6.10.

Pub. Date : 2012 May

PMID : 22764579






4 Functional Relationships(s)
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1 In this study, the co-expression enzyme of human recombinant CYPOR, CYPb5 and CYP2D6.1 or CYP2D6.10 with the Bac-to-Bac system in baculovirus-infected insect cells was used to study the catalytical activity to imipramine metabolism and stereoselective metabolism of propranolol. Propranolol cytochrome P450 family 2 subfamily D member 6 Homo sapiens
2 In this study, the co-expression enzyme of human recombinant CYPOR, CYPb5 and CYP2D6.1 or CYP2D6.10 with the Bac-to-Bac system in baculovirus-infected insect cells was used to study the catalytical activity to imipramine metabolism and stereoselective metabolism of propranolol. Propranolol cytochrome P450 family 2 subfamily D member 6 Homo sapiens
3 Both of CYP2D6.1 and CYP2D6.10 produced more hydroxyl propranolol from the R-(+)-isomer than from the S-(-)-isomer while there was no obvious difference for N-desisopropylation propranolol production between R-(+)- and S-(-)- isomer. Propranolol cytochrome P450 family 2 subfamily D member 6 Homo sapiens
4 Both of CYP2D6.1 and CYP2D6.10 produced more hydroxyl propranolol from the R-(+)-isomer than from the S-(-)-isomer while there was no obvious difference for N-desisopropylation propranolol production between R-(+)- and S-(-)- isomer. Propranolol cytochrome P450 family 2 subfamily D member 6 Homo sapiens