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

Active site proton delivery and the lyase activity of human CYP17A1.

Biochemical and biophysical research communications - 3 Jan 2014

Khatri Yogan, Gregory Michael C, Grinkova Yelena V, Denisov Ilia G, Sligar Stephen G

Abstract excerpt

Cytochrome P450 CYP17A1 catalyzes a series of reactions that lie at the intersection of corticoid and androgen biosynthesis and thus occupies an essential role in steroid hormone metabolism. This multifunctional enzyme catalyzes the 17α-hydroxylation of Δ4- and Δ5-steroids progesterone and pregnenolone to form the corresponding 17α-hydroxy products through its hydroxylase activity, and a subsequent...

Read the complete abstract on PubMed

Topics

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

Share to Catalysis
Share to Catalytic Domain
Share to Mutation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Progesterone

Share to Protons

Share to Steroid 17-alpha-Hydroxylase

Share to Threonine

Source

Open in PubMed Open full text

Identifiers

PMID: 24299954
DOI: 10.1016/j.bbrc.2013.11.094
PMCID: PMC3912944

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

Active site proton delivery and the lyase activity of human CYP17A1.PMID 24299954Read ↗

Mechanism of the Clinically Relevant E305G Mutation in Human P450 CYP17A1.Semantic proximity Read ↗

Structures of human steroidogenic cytochrome P450 17A1 with substrates.Semantic proximity Read ↗

A Novel A105Y Mutant of CYP17A1 Exhibits Almost Perfect Regioselectivity in the Production of 17α-Hydroxyprogesterone.Semantic proximity Read ↗

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

The cationic charges on Arg347, Arg358 and Arg449 of human cytochrome P450c17 (CYP17) are essential for the enzyme's cytochrome b5-dependent acyl-carbon cleavage activities.Semantic proximity Read ↗

Functional role of the conserved i-helix residue I346 in CYP5A1-Nanodiscs.Semantic proximity Read ↗

Hydroxylation Regiochemistry Is Robust to Active Site Mutations in Cytochrome P450cam (CYP101A1).Semantic proximity Read ↗

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

Complete POR ablation in human adrenal cells reveals steroidogenic rerouting and variant-dependent loss of cytochrome P450 supportSemantic proximity Read ↗

Towards a unifying mechanism for CYP17 mutations that cause isolated 17,20-lyase deficiency.Semantic proximity Read ↗

Mechanistic Scrutiny Identifies a Kinetic Role for Cytochrome b5 Regulation of Human Cytochrome P450c17 (CYP17A1, P450 17A1).Semantic proximity Read ↗

Synergistic effects of mutations in cytochrome P450cam designed to mimic CYP101D1.Semantic proximity Read ↗

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