Local view for "https://dbmi-icode-01.dbmi.pitt.edu/dikb/resource/Evidence/419"
| Predicate | Value (sorted: none) |
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| rdf:type |
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| rdf:type |
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| rdfs:label |
"evidence_1423"
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| ?:Evidence_type |
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| ?:Evidence_enzyme_system |
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| dc:date |
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| ?:content |
"Enzyme system: recombinant CYP enzymes in baculovirus infected insect cells
NADPH added: yes
Quote:
cDNA-expressed CYP isoforms were used to identify the isoforms that are able to mediate the N-dealkylation of perphenazine, which is considered a major metabolic pathway for the drug. Using human liver microsomal preparations (HLM), inhibition studies were carried out to establish the relative contributions of the CYP isoforms involved in the N-dealkylation reaction. RESULTS: CYP isoforms 1A2, 3A4, 2C8, 2C9, 2C18, 2C19 and 2D6 were able to mediate the N-dealkylation of perphenazine. Reaction velocities and their relative abundance in HLM suggested that CYP1A2, 3A4, 2C19 and 2D6 were the most important contributors to N-dealkylation. Apparent Km values of CYP1A2 and CYP2D6 were in the range 1-2 microM, and Km values of CYP2C19 and CYP3A4 were 14 microM and 7.9 microM, respectively."
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| rdfs:seeAlso |
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All properties reside in the graph file:///home/swish/src/ClioPatria/guidelines/dikb.ttl
The resource appears as object in one triple:
{ perphenazine_is_not_substrate_of_cyp3a4, <http://purl.org/swan/1.2/swan-commons#citesAsRefutingEvidence>, evidence_1423 }
Context graph
