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

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

Biomolecules - 6 Jul 2023

Esteves Francisco, Almeida Cristina M M, Silva Sofia, Saldanha Inês, Urban Philippe, Rueff José, Pompon Denis, Truan Gilles, Kranendonk Michel

Abstract excerpt

A unique cytochrome P450 (CYP) oxidoreductase (CPR) sustains activities of human microsomal CYPs. Its function requires toggling between a closed conformation enabling electron transfers from NADPH to FAD and then FMN cofactors and open conformations forming complexes and transferring electrons to CYPs. We previously demonstrated that distinct features of the hinge region linking the FAD and FMN domain (FD)...

Read the complete abstract on PubMed

Topics

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

Share to Caffeine
Share to Cytochrome P-450 CYP1A2

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cytochrome P-450 Enzyme System

Share to Electron Transport

Share to Mutation

Share to NADPH-Ferrihemoprotein Reductase

Source

Open in PubMed Open full text

Identifiers

PMID: 37509119
DOI: 10.3390/biom13071083
PMCID: PMC10377444

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Single Mutations in Cytochrome P450 Oxidoreductase Can Alter the Specificity of Human Cytochrome P450 1A2-Mediated Caffeine Metabolism.PMID 37509119Read ↗

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

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

Interaction of CYP3A4 with caffeine: First insights into multiple 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 ↗

Impact of single nucleotide polymorphisms (R132Q and W120R) on the binding affinity and metabolic activity of CYP2C19 toward some therapeutically important substrates.Semantic proximity Read ↗

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 ↗

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

Impact of peripheral mutations on the access channels of human cytochrome P450 1A2Semantic proximity Read ↗

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

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

Crystal Structures of Drug-Metabolizing CYPs.Semantic proximity Read ↗

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

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