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

A novel function of yeast fatty acid synthase. Subunit alpha is capable of self-pantetheinylation.

European journal of biochemistry - 1 May 2000

Fichtlscherer F, Wellein C, Mittag M, Schweizer E

Abstract excerpt

The prosthetic group of yeast fatty acid synthase (FAS), 4'-phosphopantetheine, is covalently linked to Ser180 of subunit alpha. It originates from coenzyme A and is transferred to the enzyme by a specific phosphopantetheine:protein transferase (PPTase). The present study demonstrates that the FAS-activating PPTase of yeast represents a distinct catalytic domain of the FAS complex and resides within the...

Read the complete abstract on PubMed

Topics

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

Share to Amidohydrolases
Share to Catalytic Domain
Share to Coenzyme A

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

Share to Fatty Acid Synthases

Share to Genetic Complementation Test

Share to GPI-Linked Proteins

Share to Mutagenesis

Share to Saccharomyces cerevisiae

Source

Identifiers

PMID: 10785388
DOI: 10.1046/j.1432-1327.2000.01282.x

Genes

FAS

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 · 8 closest

A novel function of yeast fatty acid synthase. Subunit alpha is capable of self-pantetheinylation.PMID 10785388Read ↗

Multimeric options for the auto-activation of the Saccharomyces cerevisiae FAS type I megasynthase.Semantic proximity Read ↗

Substrate and product binding sites of yeast fatty acid synthase. Stoichiometry and binding kinetics of wild-type and in vitro mutated enzymes.Semantic proximity Read ↗

Fatty acid synthase dimers containing catalytically active beta-ketoacyl synthase or malonyl/acetyltransferase domains in only one subunit can support fatty acid synthesis at the acyl carrier protein domains of both subunits.Semantic proximity Read ↗

Mapping of functional interactions between domains of the animal fatty acid synthase by mutant complementation in vitro.Semantic proximity Read ↗

Fatty acid elongation in yeast--biochemical characteristics of the enzyme system and isolation of elongation-defective mutants.Semantic proximity Read ↗

Differential proteolytic sensitivity of yeast fatty acid synthetase subunits alpha and beta contributing to a balanced ratio of both fatty acid synthetase components.Semantic proximity Read ↗

A Single Mutation in the "DSL" Motif of the Acyl Carrier Protein Can Prevent Its In Vivo Phosphopantetheinylation by E. coli Holo-Acyl Carrier Protein Synthase (AcpS).Semantic proximity Read ↗

Mitochondrial Phosphopantetheinylation is Required for Oxidative FunctionSemantic proximity Read ↗

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