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

Prostaglandin endoperoxide synthase. The aspirin acetylation region.

The Journal of biological chemistry - 15 Jun 1992

Shimokawa T, Smith W L

Abstract excerpt

Aspirin selectively acetylates Ser-530 of prostaglandin endoperoxide (PGH) synthase-1. This causes inactivation of the cyclooxygenase activity of the enzyme, but does not appreciably affect its peroxidase activity. Although the aspirin-acetylated enzyme is inactive, we found that PGH synthase-1 in which Ser-530 had been replaced with an alanine was catalytically active; accordingly, we proposed that aspirin...

Read the complete abstract on PubMed

Topics

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

Share to Acetylation
Share to Amino Acid Sequence
Share to Base Sequence

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

Share to Blotting, Western

Share to Cell Line

Share to Electrophoresis, Polyacrylamide Gel

Share to Molecular Sequence Data

Share to Mutation

Source

Identifiers

PMID: 1601897

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

Prostaglandin endoperoxide synthase. The aspirin acetylation region.PMID 1601897Read ↗

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

Functional analysis of the molecular determinants of cyclooxygenase-2 acetylation by 2-acetoxyphenylhept-2-ynyl sulfide.Semantic proximity Read ↗

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

A novel mechanism of cyclooxygenase-2 inhibition involving interactions with Ser-530 and Tyr-385.Semantic proximity Read ↗

Amino acid determinants in cyclooxygenase-2 oxygenation of the endocannabinoid 2-arachidonylglycerol.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 ↗

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

Arginine 120 of prostaglandin G/H synthase-1 is required for the inhibition by nonsteroidal anti-inflammatory drugs containing a carboxylic acid moiety.Semantic proximity Read ↗

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

Probing the Electrostatic and Steric Requirements for Substrate Binding in Human Platelet-Type 12-Lipoxygenase.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 ↗

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