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

Histidine 386 and its role in cyclooxygenase and peroxidase catalysis by prostaglandin-endoperoxide H synthases.

The Journal of biological chemistry - 14 Nov 2003

Seibold Steve A, Ball Terry, Hsi Linda C, Mills Denise A, Abeysinghe Rajeewa D, Micielli Renee, Rieke Caroline Jill, Cukier Robert I, Smith William L

Abstract excerpt

Prostaglandin-endoperoxide H synthases (PGHSs) have a cyclooxygenase that forms prostaglandin (PG) G2 from arachidonic acid (AA) plus oxygen and a peroxidase that reduces the PGG2 to PGH2. The peroxidase activates the cyclooxygenase. This involves an initial oxidation of the peroxidase heme group by hydroperoxide, followed by oxidation of Tyr385 to a tyrosyl radical within the cyclooxygenase site. His386 of...

Read the complete abstract on PubMed

Topics

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

Share to Cyclooxygenase 1
Share to Heme

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

Share to Histidine

Share to Linoleic Acid

Share to Microsomes

Share to Peroxidase

Share to Prostaglandin-Endoperoxide Synthases

Share to Prostaglandins

Source

Identifiers

PMID: 12952981
DOI: 10.1074/jbc.M306319200

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

Histidine 386 and its role in cyclooxygenase and peroxidase catalysis by prostaglandin-endoperoxide H synthases.PMID 12952981Read ↗

Substitution of tyrosine for the proximal histidine ligand to the heme of prostaglandin endoperoxide synthase 2: implications for the mechanism of cyclooxygenase activation and catalysis.Semantic proximity Read ↗

Role of Tyr348 in Tyr385 radical dynamics and cyclooxygenase inhibitor interactions in prostaglandin H synthase-2.Semantic proximity Read ↗

Peroxide-induced radical formation at TYR385 and TYR504 in human PGHS-1.Semantic proximity Read ↗

Crystal structure of arachidonic acid bound to a mutant of prostaglandin endoperoxide H synthase-1 that forms predominantly 11-hydroperoxyeicosatetraenoic acid.Semantic proximity Read ↗

Mutational and X-ray crystallographic analysis of the interaction of dihomo-gamma -linolenic acid with prostaglandin endoperoxide H synthases.Semantic proximity Read ↗

Decreased cyclooxygenase inhibition by aspirin in polymorphic variants of human prostaglandin H synthase-1.Semantic proximity Read ↗

The aspirin and heme-binding sites of ovine and murine prostaglandin endoperoxide synthases.Semantic proximity Read ↗

Structural characterization of arachidonyl radicals formed by prostaglandin H synthase-2 and prostaglandin H synthase-1 reconstituted with mangano protoporphyrin IX.Semantic proximity Read ↗

Different catalytically competent arrangements of arachidonic acid within the cyclooxygenase active site of prostaglandin endoperoxide H synthase-1 lead to the formation of different oxygenated products.Semantic proximity Read ↗

Distinct influences of carboxyl terminal segment structure on function in the two isoforms of prostaglandin H synthase.Semantic proximity Read ↗

Structure of eicosapentaenoic and linoleic acids in the cyclooxygenase site of prostaglandin endoperoxide H synthase-1.Semantic proximity Read ↗

Structural and functional characterization of human microsomal prostaglandin E synthase-1 by computational modeling and site-directed mutagenesis.Semantic proximity Read ↗

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