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

Regulation of histidine and proline degradation enzymes by amino acid availability in Bacillus subtilis.

Journal of bacteriology - 1 Sept 1990

Atkinson M R, Wray L V, Fisher S H

Abstract excerpt

The first enzymes of the histidine (hut) and proline degradative pathways, histidase and proline oxidase, could not be induced in Bacillus subtilis cells growing in glucose minimal medium containing a mixture of 16 amino acids. Addition of the 16-amino-acid mixture to induced wild-type cells growing in citrate minimal medium repressed histidase synthesis 25- to 250-fold and proline oxidase synthesis 16-fold. A...

Topics

Ammonia-Lyases
Bacillus subtilis
Enzyme Induction
Genotype
Histidine
Histidine Ammonia-Lyase
Homeostasis
Mutation
Operon
Oxidoreductases Acting on CH-NH Group Donors
Plasmids

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Proline

Proline Oxidase

Promoter Regions, Genetic

Restriction Mapping

Source

Open in PubMed Open full text

Identifiers

PMID: 2118500
DOI: 10.1128/jb.172.9.4758-4765.1990
PMCID: PMC213128

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2118500-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Regulation of histidine and proline degradation enzymes by amino acid availability in Bacillus subtilis.PMID 2118500Read ↗

Role of CodY in regulation of the Bacillus subtilis hut operon.Semantic proximity Read ↗

Modulation of Bacillus subtilis catabolite repression by transition state regulatory protein AbrB.Semantic proximity Read ↗

How To Deal with Toxic Amino Acids: the Bipartite AzlCD Complex Exports Histidine in Bacillus subtilis.Semantic proximity Read ↗

Identification of genes and gene products whose expression is activated during nitrogen-limited growth in Bacillus subtilis.Semantic proximity Read ↗

Dual involvement of CbrAB and NtrBC in the regulation of histidine utilization in Pseudomonas fluorescens SBW25.Semantic proximity Read ↗

Histidine aminotransferase activity in Streptomyces tendae and its correlation with nikkomycin production.Semantic proximity Read ↗

Alterations in the flow of one-carbon units affect KinB-dependent sporulation in Bacillus subtilis.Semantic proximity Read ↗

Tn1000-mediated insertion mutagenesis of the histidine utilization (hut) gene cluster from Klebsiella aerogenes: genetic analysis of hut and unusual target specificity of Tn1000.Semantic proximity Read ↗

A membrane transporter required for 3-hydroxybutyrate uptake during the early sporulation stage in Bacillus subtilis.Semantic proximity Read ↗

Mutations that render the promoter of the histidine operon of Salmonella typhimurium insensitive to nutrient-rich medium repression and amino acid downshift.Semantic proximity Read ↗

Insufficient expression of the ilv-leu operon encoding enzymes of branched-chain amino acid biosynthesis limits growth of a Bacillus subtilis ccpA mutant.Semantic proximity Read ↗

Histidinol phosphate phosphatase, catalyzing the penultimate step of the histidine biosynthesis pathway, is encoded by ytvP (hisJ) in Bacillus subtilis.Semantic proximity Read ↗

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