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

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

European journal of biochemistry - 1 Mar 1995

Schuster H, Rautenstrauss B, Mittag M, Stratmann D, Schweizer E

Abstract excerpt

The four known substrate binding sites of yeast fatty acid synthase (FAS), Ser819 (acetyltransferase, OHAC) and Ser5421 (malonyl/palmitoyl transferase, OHMa1) of subunit beta and Ser180 (pantetheine binding site, SHc) and Cys1305 (3-oxoacyl synthase, SHp) of subunit alpha were replaced, by targeted in vitro mutagenesis, by the non-acylatable amino acids glutamine, glycine or alanine. The four mutated FAS proteins...

Read the complete abstract on PubMed

Topics

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

Share to Acetates
Share to Amino Acid Sequence

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

Share to Base Sequence

Share to Binding Sites

Share to Fatty Acids

Share to Molecular Sequence Data

Share to Mutation

Share to Saccharomyces cerevisiae

Source

Identifiers

PMID: 7705357

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 · 12 closest

Substrate and product binding sites of yeast fatty acid synthase. Stoichiometry and binding kinetics of wild-type and in vitro mutated enzymes.PMID 7705357Read ↗

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

A nuclear magnetic resonance-based structural rationale for contrasting stoichiometry and ligand binding site(s) in fatty acid-binding proteins.Semantic proximity Read ↗

Specificity determinants for the pyruvate dehydrogenase component reaction mapped with mutated and prosthetic group modified lipoyl domains.Semantic proximity Read ↗

Structure of acyl carrier protein bound to FabI, the FASII enoyl reductase from Escherichia coli.Semantic proximity Read ↗

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

Kinetic and physiological effects of alterations in homologous isocitrate-binding sites of yeast NAD(+)-specific isocitrate dehydrogenase.Semantic proximity Read ↗

Key residues responsible for acyl carrier protein and beta-ketoacyl-acyl carrier protein reductase (FabG) interaction.Semantic proximity Read ↗

Isocitrate binding at two functionally distinct sites in yeast NAD+-specific isocitrate dehydrogenase.Semantic proximity Read ↗

Profiling of cytosolic and peroxisomal acetyl-CoA metabolism in Saccharomyces cerevisiae.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 ↗

Methylmalonate-semialdehyde dehydrogenase from Bacillus subtilis: substrate specificity and coenzyme A binding.Semantic proximity Read ↗

Substrate recognition by β-ketoacyl-ACP synthases.Semantic proximity Read ↗

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