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

Assembly of the covalent linkage between lipoic acid and its cognate enzymes.

Chemistry & biology - 1 Dec 2003

Zhao Xin, Miller J Richard, Jiang Yanfang, Marletta Michael A, Cronan John E

Abstract excerpt

Lipoic acid is synthesized from octanoic acid by insertion of sulfur atoms at carbons 6 and 8 and is covalently attached to a pyruvate dehydrogenase (PDH) subunit. We show that sulfur atoms can be inserted into octanoyl moieties attached to a PDH subunit or a derived domain. Escherichia coli lipB mutants grew well when supplemented with octanoate in place of lipoate. Octanoate growth required both lipoate protein...

Read the complete abstract on PubMed

Topics

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

Share to Acyltransferases
Share to Chromatography, High Pressure Liquid

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

Share to Ligases

Share to Lipoproteins

Share to Mass Spectrometry

Share to Protein Subunits

Share to Pyruvate Dehydrogenase (Lipoamide)

Share to Sulfur

Source

Identifiers

PMID: 14700636
DOI: 10.1016/j.chembiol.2003.11.016

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

Assembly of the covalent linkage between lipoic acid and its cognate enzymes.PMID 14700636Read ↗

Assembly of Lipoic Acid on Its Cognate Enzymes: an Extraordinary and Essential Biosynthetic PathwaySemantic proximity Read ↗

Lipoic acid metabolism in Escherichia coli: the lplA and lipB genes define redundant pathways for ligation of lipoyl groups to apoprotein.Semantic proximity Read ↗

Repurposing lipoic acid changes electron flow in two important metabolic pathways of Escherichia coli.Semantic proximity Read ↗

Bacterial lipoate protein ligases rescue lipoylation and respiration deficiency in mammalsSemantic proximity Read ↗

Characterization of a lipoate-protein ligase A gene of rice (Oryza sativa L.).Semantic proximity Read ↗

Scavenging of cytosolic octanoic acid by mutant LplA lipoate ligases allows growth of Escherichia coli strains lacking the LipB octanoyltransferase of lipoic acid synthesis.Semantic proximity Read ↗

Octanoylation of the lipoyl domains of the pyruvate dehydrogenase complex in a lipoyl-deficient strain of Escherichia coli.Semantic proximity Read ↗

Biosynthesis of lipoic acid: characterization of the lipoic acid auxotrophs Escherichia coli W1485-lip2 and JRG33-lip9.Semantic proximity Read ↗

Engineering of an active animal fatty acid synthase dimer with only one competent subunit.Semantic proximity Read ↗

Crystal structure of lipoate-protein ligase A from Escherichia coli. Determination of the lipoic acid-binding site.Semantic proximity Read ↗

A universal pocket in fatty acyl-AMP ligases ensures redirection of fatty acid pool away from coenzyme A-based activation.Semantic proximity Read ↗

The role of loop and beta-turn residues as structural and functional determinants for the lipoyl domain from the Escherichia coli 2-oxoglutarate dehydrogenase complex.Semantic proximity Read ↗

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