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

Identification and analysis of conserved sequence motifs in cytochrome P450 family 2. Functional and structural role of a motif 187RFDYKD192 in CYP2B enzymes.

The Journal of biological chemistry - 1 Aug 2008

Oezguen Numan, Kumar Santosh, Hindupur Aditya, Braun Werner, Muralidhara B K, Halpert James R

Abstract excerpt

Using a multiple alignment of 175 cytochrome P450 (CYP) family 2 sequences, 20 conserved sequence motifs (CSMs) were identified with the program PCPMer. Functional importance of the CSM in CYP2B enzymes was assessed from available data on site-directed mutants and genetic variants. These analyses suggested an important role of the CSM 8, which corresponds to(187)RFDYKD(192) in CYP2B4. Further analysis showed that...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Motifs
Share to Aryl Hydrocarbon Hydroxylases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Catalysis

Share to Conserved Sequence

Share to Cytochrome P450 Family 2

Share to Hydrogen Bonding

Share to Inhibitory Concentration 50

Share to Temperature

Source

Open in PubMed Open full text

Identifiers

PMID: 18495666
DOI: 10.1074/jbc.M708582200
PMCID: PMC2490781

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

Identification and analysis of conserved sequence motifs in cytochrome P450 family 2. Functional and structural role of a motif 187RFDYKD192 in CYP2B enzymes.PMID 18495666Read ↗

Rational engineering of human cytochrome P450 2B6 for enhanced expression and stability: importance of a Leu264->Phe substitution.Semantic proximity Read ↗

Phylogenetic and functional analysis of the vertebrate cytochrome p450 2 family.Semantic proximity Read ↗

Identification of universal selectivity-determining positions in cytochrome P450 monooxygenases by systematic sequence-based literature mining.Semantic proximity Read ↗

Crystal structure of human cytochrome P450 2D6.Semantic proximity Read ↗

The role of cytochrome 2B1 substrate recognition site residues 115, 294, 297, 298, and 362 in the oxidation of steroids and 7-alkoxycoumarins.Semantic proximity Read ↗

Pharmacophore, QSAR, and binding mode studies of substrates of human cytochrome P450 2D6 (CYP2D6) using molecular docking and virtual mutations and an application to chinese herbal medicine screening.Semantic proximity Read ↗

Substrate routes to the buried active site may vary among cytochromes P450: mutagenesis of the F-G region in P450 2B1.Semantic proximity Read ↗

Identification of selectivity determinants in CYP monooxygenases by modelling and systematic analysis of sequence and structure.Semantic proximity Read ↗

The structure of human cytochrome P450 2C9 complexed with flurbiprofen at 2.0-A resolution.Semantic proximity Read ↗

Analysis of differential substrate selectivities of CYP2B6 and CYP2E1 by site-directed mutagenesis and molecular modeling.Semantic proximity Read ↗

Proteomics, modeling, and fluorescence assays delineate cytochrome b5 residues involved in binding and stimulation of cytochrome P450 17A1 17,20-lyase.Semantic proximity Read ↗

Functional characterization of cytochromes P450 2B from the desert woodrat Neotoma lepida.Semantic proximity Read ↗

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