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 rationalization of novel drug metabolizing mutants of cytochrome P450 BM3.

Proteins - 1 Apr 2008

Stjernschantz Eva, van Vugt-Lussenburg Barbara M A, Bonifacio Alois, de Beer Stephanie B A, van der Zwan Gert, Gooijer Cees, Commandeur Jan N M, Vermeulen Nico P E, Oostenbrink Chris

Abstract excerpt

Three newly discovered drug metabolizing mutants of cytochrome P450 BM3 (van Vugt-Lussenburg et al., Identification of critical residues in novel drug metabolizing mutants of Cytochrome P450 BM3 using random mutagenesis, J Med Chem 2007;50:455-461) have been studied at an atomistic level to provi...

Read the complete abstract on PubMed

Topics

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

Share to Computer Simulation
Share to Cytochrome P-450 CYP2D6
Share to Cytochrome P-450 Enzyme System

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Ligands

Share to Models, Molecular

Share to Mutation

Share to Pharmaceutical Preparations

Share to Protein Conformation

Source

Identifiers

PMID: 17957765
DOI: 10.1002/prot.21697

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-17957765-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural rationalization of novel drug metabolizing mutants of cytochrome P450 BM3.PMID 17957765Read ↗

Identification of critical residues in novel drug metabolizing mutants of cytochrome P450 BM3 using random mutagenesis.Semantic proximity Read ↗

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

The role of protein plasticity in computational rationalization studies on regioselectivity in testosterone hydroxylation by cytochrome P450 BM3 mutants.Semantic proximity Read ↗

Subtle structural changes in the Asp251Gly/Gln307His P450 BM3 mutant responsible for new activity toward diclofenac, tolbutamide and ibuprofen.Semantic proximity Read ↗

Application of drug metabolising mutants of cytochrome P450 BM3 (CYP102A1) as biocatalysts for the generation of reactive metabolites.Semantic proximity Read ↗

Structural and spectroscopic analysis of the F393H mutant of flavocytochrome P450 BM3.Semantic proximity Read ↗

Structural and spectroscopic characterization of P450 BM3 mutants with unprecedented P450 heme iron ligand sets. New heme ligation states influence conformational equilibria in P450 BM3.Semantic proximity Read ↗

Simulation-Guided Design of Cytochrome P450 for Chemo- and Regioselective Macrocyclic Oxidation.Semantic proximity Read ↗

Effect of Mutation and Substrate Binding on the Stability of Cytochrome P450BM3 Variants.Semantic proximity Read ↗

Free energy calculations give insight into the stereoselective hydroxylation of α-ionones by engineered cytochrome P450 BM3 mutants.Semantic proximity Read ↗

Evaluation of alkoxyresorufins as fluorescent substrates for cytochrome P450 BM3 and site-directed mutants.Semantic proximity Read ↗

A P450 BM-3 mutant hydroxylates alkanes, cycloalkanes, arenes and heteroarenes.Semantic proximity Read ↗

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