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

P450c17 mutations R347H and R358Q selectively disrupt 17,20-lyase activity by disrupting interactions with P450 oxidoreductase and cytochrome b5.

Molecular endocrinology (Baltimore, Md.) - 1 Jan 1999

Geller D H, Auchus R J, Miller W L

Abstract excerpt

Cytochrome P450c17 catalyzes steroid 17alpha-hydroxylase and 17,20-lyase activities and hence is a key enzyme in the production of human glucocorticoids and sex steroids. These two activities are catalyzed in a single substrate-binding site but are regulated independently in human physiology. We have recently shown that cytochrome b5 facilitates 17,20-lyase activity by allosterically promoting the interaction of...

Read the complete abstract on PubMed

Topics

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

Share to COS Cells
Share to Cytochrome P-450 Enzyme System

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

Share to Kinetics

Share to Mutation

Share to Oxidoreductases

Share to Recombinant Proteins

Share to Structure-Activity Relationship

Share to Yeasts

Source

Identifiers

PMID: 9892022
DOI: 10.1210/mend.13.1.0219

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

P450c17 mutations R347H and R358Q selectively disrupt 17,20-lyase activity by disrupting interactions with P450 oxidoreductase and cytochrome b5.PMID 9892022Read ↗

The molecular basis of isolated 17,20 lyase deficiency.Semantic proximity Read ↗

Pitfalls in characterizing P450c17 mutations associated with isolated 17,20-lyase deficiency.Semantic proximity Read ↗

Probing structural and functional domains of human P450c17.Semantic proximity Read ↗

Molecular modeling of human P450c17 (17alpha-hydroxylase/17,20-lyase): insights into reaction mechanisms and effects of mutations.Semantic proximity Read ↗

Novel P450c17 mutation H373D causing combined 17alpha-hydroxylase/17,20-lyase deficiency.Semantic proximity Read ↗

Homozygous Mutation G539R in the Gene for P450 Oxidoreductase in a Family Previously Diagnosed as Having 17,20-Lyase DeficiencySemantic proximity Read ↗

Mutation of histidine 373 to leucine in cytochrome P450c17 causes 17 alpha-hydroxylase deficiency.Semantic proximity Read ↗

The regulation of 17,20 lyase activity.Semantic proximity Read ↗

The genetic and functional basis of isolated 17,20-lyase deficiency.Semantic proximity Read ↗

A Missense Mutation in the Human Cytochrome b5 Gene causes 46,XY Disorder of Sex Development due to True Isolated 17,20 Lyase DeficiencySemantic proximity Read ↗

Novel mutation of the CYP17 gene in two unrelated patients with combined 17alpha-hydroxylase/17,20-lyase deficiency: demonstration of absent enzyme activity by expressing the mutant CYP17 gene and by three-dimensional modeling.Semantic proximity Read ↗

Isolated 17,20-lyase deficiency due to the cytochrome b5 mutation W27X.Semantic proximity Read ↗

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