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

Multimeric options for the auto-activation of the Saccharomyces cerevisiae FAS type I megasynthase.

Structure (London, England : 1993) - 12 Aug 2009

Johansson Patrik, Mulinacci Barbara, Koestler Caecilia, Vollrath Ronnald, Oesterhelt Dieter, Grininger Martin

Abstract excerpt

The fungal type I fatty acid synthase (FAS) is a 2.6 MDa multienzyme complex, catalyzing all necessary steps for the synthesis of long acyl chains. To be catalytically competent, the FAS must be activated by a posttranslational modification of the central acyl carrier domain (ACP) by an intrinsic phosphopantetheine transferase (PPT). However, recent X-ray structures of the fungal FAS revealed a barrel-shaped...

Read the complete abstract on PubMed

Topics

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

Share to Acyl Carrier Protein
Share to Coenzyme A

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Fatty Acid Synthases

Share to Magnesium

Share to Models, Chemical

Share to Molecular Structure

Share to Protein Multimerization

Share to Transferases (Other Substituted Phosphate Groups)

Source

Identifiers

PMID: 19679086
DOI: 10.1016/j.str.2009.06.014

Genes

FAS

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Multimeric options for the auto-activation of the Saccharomyces cerevisiae FAS type I megasynthase.PMID 19679086Read ↗

Catalysis and mechanism of malonyl transferase activity in type II fatty acid biosynthesis acyl carrier proteins.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 ↗

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 ↗

The phosphatidylglycerol phosphate synthase PgsA utilizes a trifurcated amphipathic cavity for catalysis at the membrane-cytosol interfaceSemantic proximity Read ↗

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

Structure and molecular organization of mammalian fatty acid synthase.Semantic proximity Read ↗

Structural basis for channelling mechanism of a fatty acid beta-oxidation multienzyme complex.Semantic proximity Read ↗

Engineering fungal de novo fatty acid synthesis for short chain fatty acid production.Semantic proximity Read ↗

The Mycobacterium Tuberculosis FAS-II Dehydratases and Methyltransferases Define the Specificity of the Mycolic Acid Elongation ComplexesSemantic proximity Read ↗

Molecular basis for the activation of the Fatty Acid Kinase complex of <i>Staphylococcus aureus</i>Semantic proximity Read ↗

Evidence for a protein-protein interaction motif on an acyl carrier protein domain from a modular polyketide synthase.Semantic proximity Read ↗

A Eukaryotic Sensor for Membrane Lipid Saturation.Semantic proximity Read ↗

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