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

Xenobiotic/medium chain fatty acid: CoA ligase - a critical review on its role in fatty acid metabolism and the detoxification of benzoic acid and aspirin.

Expert opinion on drug metabolism & toxicology - 1 Oct 2016

van der Sluis Rencia, Erasmus Elardus

Abstract excerpt

INTRODUCTION: Activation of fatty acids by the acyl-CoA synthetases (ACSs) is the vital first step in fatty acid metabolism. The enzymatic and physiological characterization of the human xenobiotic/medium chain fatty acid: CoA ligases (ACSMs) has been severely neglected even though xenobiotics, such as benzoate and salicylate, are detoxified through this pathway. AREAS COVERED: This review will focus on the...

Read the complete abstract on PubMed

Topics

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

Share to Aspirin
Share to Coenzyme A Ligases

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

Share to Fatty Acids

Share to Polymorphism, Single Nucleotide

Share to Substrate Specificity

Share to Xenobiotics

Source

Identifiers

PMID: 27351777
DOI: 10.1080/17425255.2016.1206888

Genes

ACSM1

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

Xenobiotic/medium chain fatty acid: CoA ligase - a critical review on its role in fatty acid metabolism and the detoxification of benzoic acid and aspirin.PMID 27351777Read ↗

Analyses of the genetic diversity and protein expression variation of the acyl: CoA medium-chain ligases, ACSM2A and ACSM2B.Semantic proximity Read ↗

Glycine conjugation: importance in metabolism, the role of glycine N-acyltransferase, and factors that influence interindividual variation.Semantic proximity Read ↗

Functional Characterisation of Three Glycine N-Acyltransferase Variants and the Effect on Glycine Conjugation to Benzoyl-CoA.Semantic proximity Read ↗

Characterization, structure and inhibition of the human succinyl-CoA:glutarate-CoA transferase, a genetic modifier of glutaric aciduria type 1Semantic proximity Read ↗

Detoxification enzymes: cellular metabolism and susceptibility to various diseases.Semantic proximity Read ↗

Pharmacogenomics in aspirin intolerance.Semantic proximity Read ↗

Carboxylesterases in lipid metabolism: from mouse to human.Semantic proximity Read ↗

PharmGKB summary: mycophenolic acid pathway.Semantic proximity Read ↗

CYP4V2 fatty acid omega hydroxylase, a druggable target for the treatment of metabolic associated fatty liver disease (MAFLD).Semantic proximity Read ↗

Evolution, expression, and substrate specificities of aldehyde oxidase enzymes in eukaryotesSemantic proximity Read ↗

Vitamin B5 Metabolism is Essential for Vacuolar and Mitochondrial Integrity and Xenobiotic Detoxification in FungiSemantic proximity Read ↗

The human bile acid-CoA:amino acid N-acyltransferase functions in the conjugation of fatty acids to glycine.Semantic proximity Read ↗

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