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

The role of ALA-S and ALA-D in regulating porphyrin biosynthesis in a normal and a HEM R+ mutant strain of Saccharomyces cerevisiae.

Yeast (Chichester, England) - 1 Feb 1993

Correa García S, Bermúdez Moretti M, Cardalda C, Rossetti M V, Batlle A M

Abstract excerpt

Catabolite repression and derepression on delta-aminolevulinate synthase (ALA-S) and delta-aminolevulinate dehydratase (ALA-D) in a normal yeast strain, D27, and its derived D27/C6 (HEM R+) were investigated. ALA-S and ALA-D activities and intracellular ALA (I-ALA) at different physiological states of the cells were measured. In YPD medium, under conditions of repression and when glucose was exhausted, both...

Read the complete abstract on PubMed

Topics

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

Share to Cytochromes
Share to Enzyme Repression

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

Share to Hydroxymethylbilane Synthase

Share to Mutation

Share to Porphobilinogen Synthase

Share to Saccharomyces cerevisiae

Share to Spectrophotometry

Source

Identifiers

PMID: 8465603
DOI: 10.1002/yea.320090207

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

The role of ALA-S and ALA-D in regulating porphyrin biosynthesis in a normal and a HEM R+ mutant strain of Saccharomyces cerevisiae.PMID 8465603Read ↗

Regulatory role of ALA-S and ALA-D in a haem-deficient mutant of Saccharomyces cerevisiae.Semantic proximity Read ↗

Porphyrin biosynthesis in normal and haem mutants of Saccharomyces cerevisiae. Studies on the inheritance of the HEM R+ phenotype.Semantic proximity Read ↗

Delta-aminolevulinic acid transport in Saccharomyces cerevisiae.Semantic proximity Read ↗

Impact of hemB mutations on 5-aminolevulinic acid production in Escherichia coliSemantic proximity Read ↗

Heme synthesis in yeast does not require oxygen as an obligatory electron acceptor.Semantic proximity Read ↗

Different porphobilinogen-deaminase forms in wild and mutant strains of Saccharomyces cerevisiae. A possible correlation with its segregants behaviour.Semantic proximity Read ↗

Porphyrin biosynthesis intermediates are not regulating delta-aminolevulinic acid transport in Saccharomyces cerevisiae.Semantic proximity Read ↗

Regulation by heme of sterol uptake in Saccharomyces cerevisiae.Semantic proximity Read ↗

Glutathione as an endogenous sulphur source in the yeast Saccharomyces cerevisiae.Semantic proximity Read ↗

Sterol uptake in Saccharomyces cerevisiae heme auxotrophic mutants is affected by ergosterol and oleate but not by palmitoleate or by sterol esterification.Semantic proximity Read ↗

Use of batch and fed-batch fermentation for studies on the variation of glutathione content and its influence on the genotoxicity of methyl-nitro-nitrosoguanidine in yeast.Semantic proximity Read ↗

L-asparaginase II of saccharomyces cerevisiae. Activity profile during growth using an ure2 mutant P40-3C and a P40-3C + URE2p strain.Semantic proximity Read ↗

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