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 stationary-phase acyl-coenzyme A synthetase of Streptomyces coelicolor A3(2) is necessary for the normal onset of antibiotic production.

Applied and environmental microbiology - 1 Sept 2002

Banchio C, Gramajo H

Abstract excerpt

The fadD1 and macs1 genes of Streptomyces coelicolor are part of a two-gene operon. Both genes encode putative acyl coenzyme A synthetases (ACSs). The amino acid sequence of FadD1 has high homology with those of several ACSs, while MACS1 has the closest homology with medium-chain ACSs, broadly known as SA proteins. Like FadD of Escherichia coli, FadD1 also has a broad substrate specificity, although saturated...

Read the complete abstract on PubMed

Topics

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

Share to Anti-Bacterial Agents
Share to Arabidopsis Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Coenzyme A Ligases

Share to Escherichia coli

Share to Fatty Acid Desaturases

Share to Sequence Analysis, Protein

Share to Streptomyces

Share to Transcription, Genetic

Source

Open in PubMed Open full text

Identifiers

PMID: 12200271
DOI: 10.1128/AEM.68.9.4240-4246.2002
PMCID: PMC124087

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A stationary-phase acyl-coenzyme A synthetase of Streptomyces coelicolor A3(2) is necessary for the normal onset of antibiotic production.PMID 12200271Read ↗

Transcriptional regulation of the macs1-fadD1 operon encoding two acyl-CoA synthases involved in the physiological differentiation of Streptomyces coelicolor.Semantic proximity Read ↗

ScbA from Streptomyces coelicolor A3(2) has homology to fatty acid synthases and is able to synthesize gamma-butyrolactones.Semantic proximity Read ↗

Role of an essential acyl coenzyme A carboxylase in the primary and secondary metabolism of Streptomyces coelicolor A3(2).Semantic proximity Read ↗

Genome-wide transcriptome analysis reveals that a pleiotropic antibiotic regulator, AfsS, modulates nutritional stress response in Streptomyces coelicolor A3(2).Semantic proximity Read ↗

Novel two-component systems implied in antibiotic production in Streptomyces coelicolor.Semantic proximity Read ↗

A putative two-component regulatory system involved in secondary metabolism in Streptomyces spp.Semantic proximity Read ↗

A single amino acid substitution in region 1.2 of the principal sigma factor of Streptomyces coelicolor A3(2) results in pleiotropic loss of antibiotic production.Semantic proximity Read ↗

afsR is a pleiotropic but conditionally required regulatory gene for antibiotic production in Streptomyces coelicolor A3(2).Semantic proximity Read ↗

The Gene bldA, a regulator of morphological differentiation and antibiotic production in streptomyces.Semantic proximity Read ↗

FasR, a novel class of transcriptional regulator, governs the activation of fatty acid biosynthesis genes in Streptomyces coelicolor.Semantic proximity Read ↗

Proteins encoded by the conservon of Streptomyces coelicolor A3(2) comprise a membrane-associated heterocomplex that resembles eukaryotic G protein-coupled regulatory system.Semantic proximity Read ↗

The Level of AdpA Directly Affects Expression of Developmental Genes in Streptomyces coelicolorSemantic proximity Read ↗

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