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

Structural context of NADPH-cytochrome P450 reductase mutations that alter cytochrome P450 1A2 substrate regioselectivity.

Drug metabolism and disposition: the biological fate of chemicals - 1 Jun 2026

Burris-Hiday Sarah D, Esteves Francisco, Kranendonk Michel, Scott Emily E

Abstract excerpt

NADPH-cytochrome P450 (P450) reductase serves as the obligate redox partner for the majority of human P450 enzymes, those responsible for both drug metabolism and homeostasis. NADPH-derived electrons are accepted by the reductase FAD-containing domain and then transferred to its flavin mononucleotide-containing domain (FMND). This domain directly binds P450 enzymes, providing electrons essential for P450...

Read the complete abstract on PubMed

Topics

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

Share to Crystallography, X-Ray
Share to Cytochrome P-450 CYP1A2

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Flavin Mononucleotide

Share to Models, Molecular

Share to NADPH-Ferrihemoprotein Reductase

Share to Protein Conformation

Share to Substrate Specificity

Source

Open in PubMed Open full text

Identifiers

PMID: 42105715
DOI: 10.1016/j.dmd.2026.100300
PMCID: PMC13494183

Genes

CYP1A2

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 8 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural context of NADPH-cytochrome P450 reductase mutations that alter cytochrome P450 1A2 substrate regioselectivity.PMID 42105715Read ↗

Single Mutations in Cytochrome P450 Oxidoreductase Can Alter the Specificity of Human Cytochrome P450 1A2-Mediated Caffeine Metabolism.Semantic proximity Read ↗

Interaction Modes of Microsomal Cytochrome P450s with Its Reductase and the Role of Substrate Binding.Semantic proximity Read ↗

Variability in Loss of Multiple Enzyme Activities Due to the Human Genetic Variation P284T Located in the Flexible Hinge Region of NADPH Cytochrome P450 OxidoreductaseSemantic proximity Read ↗

Analysis of coumarin 7-hydroxylation activity of cytochrome P450 2A6 using random mutagenesis.Semantic proximity Read ↗

Key mutations alter the cytochrome P450 BM3 conformational landscape and remove inherent substrate bias.Semantic proximity Read ↗

Structure and function of an NADPH-cytochrome P450 oxidoreductase in an open conformation capable of reducing cytochrome P450.Semantic proximity Read ↗

Molecular Mechanisms Underlying Single Nucleotide Polymorphism-Induced Reactivity Decrease in CYP2D6.Semantic proximity Read ↗

Loss of multiple enzyme activities due to the human genetic variation P284T in NADPH cytochrome P450 oxidoreductaseSemantic proximity Read ↗

Clinical, structural and functional implications of mutations and polymorphisms in human NADPH P450 oxidoreductase.Semantic proximity Read ↗

Directed-evolution analysis of human cytochrome P450 2A6 for enhanced enzymatic catalysis.Semantic proximity Read ↗

Active-site topologies of human CYP2D6 and its aspartate-301 --> glutamate, asparagine, and glycine mutants.Semantic proximity Read ↗

A theoretical study on the mechanism of a superficial mutation inhibiting the enzymatic activity of CYP1A2.Semantic proximity Read ↗

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