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

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

Archives of biochemistry and biophysics - 1 Oct 2001

Domanski T L, He Y Q, Scott E E, Wang Q, Halpert J R

Abstract excerpt

At least two substitutions were made at each of five amino acid residues in rat cytochrome P450 2B1 that align to residues of known importance in other P450s. The mutants were histidine tagged for purification from Escherichia coli, and the proteins were assessed for testosterone and 7-alkoxycoumarin oxidation. Alteration of each of the sites studied, Phe-115, Ser-294, Phe-297, Ala-298, and Leu-362, was found to...

Read the complete abstract on PubMed

Topics

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

Share to Aryl Hydrocarbon Hydroxylases
Share to Coumarins

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Cytochrome P-450 Enzyme System

Share to Hydroxylation

Share to Oxidants

Share to Steroid Hydroxylases

Share to Steroids

Share to Testosterone

Source

Identifiers

PMID: 11566023
DOI: 10.1006/abbi.2001.2504

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The role of cytochrome 2B1 substrate recognition site residues 115, 294, 297, 298, and 362 in the oxidation of steroids and 7-alkoxycoumarins.PMID 11566023Read ↗

Structural determinants of cytochrome P450 2B1 specificity: evidence for five substrate recognition sites.Semantic proximity Read ↗

Stoichiometry of 7-ethoxycoumarin metabolism by cytochrome P450 2B1 wild-type and five active-site mutants.Semantic proximity Read ↗

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

Terfenadine metabolism of human cytochrome P450 2J2 containing genetic variations (G312R, P351L and P115L).Semantic proximity Read ↗

Catalytic properties of polymorphic human cytochrome P450 1B1 variants.Semantic proximity Read ↗

Allelic variants of human cytochrome P450 1A1 (CYP1A1): effect of T461N and I462V substitutions on steroid hydroxylase specificity.Semantic proximity Read ↗

A rational approach to Re-engineer cytochrome P450 2B1 regioselectivity based on the crystal structure of cytochrome P450 2C5.Semantic proximity Read ↗

Specificity of 17beta-oestradiol and benzo[a]pyrene oxidation by polymorphic human cytochrome P4501B1 variants substituted at residues 48, 119 and 432.Semantic proximity Read ↗

Investigation of the mechanisms underlying the differential effects of the K262R mutation of P450 2B6 on catalytic activity.Semantic proximity Read ↗

Role of residue 478 as a determinant of the substrate specificity of cytochrome P450 2B1.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 ↗

Functional characterization of allelic variants of polymorphic human cytochrome P450 2A6 (CYP2A6*5, *7, *8, *18, *19, and *35).Semantic proximity Read ↗

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