Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

A combination of mutations in the CYP2D6*17 (CYP2D6Z) allele causes alterations in enzyme function.

Molecular pharmacology - 1 Dec 1997

Oscarson M, Hidestrand M, Johansson I, Ingelman-Sundberg M

Abstract excerpt

In many black African populations, the capacity for CYP2D6-dependent drug metabolism is generally reduced. A specific variant of the CYP2D6 gene (CYP2D6*17) that carries three functional mutations (T107I, R296C, and S486T) has been found to be present in Zimbabwean subjects with impaired CYP2D6-dependent hydroxylase activity. To evaluate whether the CYP2D6*17 allele was the major cause behind the decreased rate...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Alleles
Share to Black People
Share to DNA, Complementary

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Isoenzymes

Share to Mutagenesis, Site-Directed

Share to Mutation

Share to Saccharomyces cerevisiae

Share to Substrate Specificity

Source

Identifiers

PMID: 9415713
DOI: 10.1124/mol.52.6.1034

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A combination of mutations in the CYP2D6*17 (CYP2D6Z) allele causes alterations in enzyme function.PMID 9415713Read ↗

CYP2D6 Allelic Variants *34, *17-2, *17-3, and *53 and a Thr309Ala Mutant Display Altered Kinetics and NADPH Coupling in Metabolism of Bufuralol and Dextromethorphan and Altered Susceptibility to Inactivation by SCH 66712.Semantic proximity Read ↗

The molecular and enzyme kinetic basis for the diminished activity of the cytochrome P450 2D6.17 (CYP2D6.17) variant. Potential implications for CYP2D6 phenotyping studies and the clinical use of CYP2D6 substrate drugs in some African populations.Semantic proximity Read ↗

Characterization of the CYP2D6*29 allele commonly present in a black Tanzanian population causing reduced catalytic activity.Semantic proximity Read ↗

Characterization of cytochrome P450 2D6.1 (CYP2D6.1), CYP2D6.2, and CYP2D6.17 activities toward model CYP2D6 substrates dextromethorphan, bufuralol, and debrisoquine.Semantic proximity Read ↗

Pharmacogenetics of cytochrome P450 2B6 (CYP2B6): advances on polymorphisms, mechanisms, and clinical relevanceSemantic proximity Read ↗

In vitro functional assessment of 22 newly identified CYP2D6 allelic variants in the Chinese population.Semantic proximity Read ↗

Polymorphisms of CYP2D17 in cynomolgus and rhesus macaques: an evidence of the genetic basis for the variability of CYP2D-dependent drug metabolism.Semantic proximity Read ↗

A novel mutant variant of the CYP2D6 gene (CYP2D6*17) common in a black African population: association with diminished debrisoquine hydroxylase activity.Semantic proximity Read ↗

Functional properties of CYP2D6 1 (wild-type) and CYP2D6 7 (His324Pro) expressed by recombinant baculovirus in insect cells.Semantic proximity Read ↗

Functional influence of human CYP2D6 allelic variations: P34S, E418K, S486T, and R296C.Semantic proximity Read ↗

Point mutation of cytochrome P450 2A6 (a polymorphic variant CYP2A6.25) confers new substrate specificity towards flavonoids.Semantic proximity Read ↗

The African-specific CYP2D617 allele encodes an enzyme with changed substrate specificity.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.