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

Molecular basis for a functionally unique cytochrome P450IIB1 variant.

The Journal of biological chemistry - 25 Nov 1991

Kedzie K M, Balfour C A, Escobar G Y, Grimm S W, He Y A, Pepperl D J, Regan J W, Stevens J C, Halpert J R

Abstract excerpt

Liver microsomes from phenobarbital-treated rats of four inbred strains expressing distinct allelic variants of cytochrome P450IIB1 were analyzed. The Wistar Munich (WM) strain exhibited 5- to 10-fold lower androstenedione 16 beta-hydroxylase activity (a specific P450IIB1 marker) than the Lewis, Wistar Kyoto, and Wistar Furth strains. The androstenedione 16 beta-hydroxylase in the WM liver microsomes was...

Read the complete abstract on PubMed

Topics

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

Share to Alleles
Share to Cloning, Molecular
Share to DNA

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

Share to Genetic Variation

Share to Kinetics

Share to Plasmids

Source

Identifiers

PMID: 1718996

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

Molecular basis for a functionally unique cytochrome P450IIB1 variant.PMID 1718996Read ↗

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

A single active site mutation inverts stereoselectivity of 16-hydroxylation of testosterone catalyzed by engineered cytochrome P450 BM3.Semantic proximity Read ↗

An evaluation of cytochrome P450 isoform activities in the female dark agouti (DA) rat: relevance to its use as a model of the CYP2D6 poor metaboliser phenotype.Semantic proximity Read ↗

Pharmacogenetics and polymorphism of human P-450 which activates and detoxicates xenobiotics and carcinogens.Semantic proximity Read ↗

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

Comparisons of catalytic selectivity of cytochrome P450 subfamily enzymes from different species.Semantic proximity Read ↗

Enzymatic phenotyping and evolutionary relatedness of species specific cytochromes P450 17alpha.Semantic proximity Read ↗

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

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

Replacing the carboxy-terminal 28 residues of rabbit liver P-450 (laurate (omega-1)-hydroxylase) with those of P-450 (testosterone 16 alpha-hydroxylase) produces a new stereospecific hydroxylase activity.Semantic proximity Read ↗

Null phenotype for cytochrome P450 2B2 in the rat results from a deletion of its structural gene.Semantic proximity Read ↗

Sequence analyses of CYP2B genes and catalytic profiles for P450s in Qdj:Sprague-dawley rats that lack response to the phenobarbital-mediated induction of CYP2B2.Semantic proximity Read ↗

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