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

A mutation affecting carbon catabolite repression suppresses growth defects in pyruvate carboxylase mutants from Saccharomyces cerevisiae.

FEBS letters - 18 Dec 1995

Blázquez M A, Gamo F J, Gancedo C

Abstract excerpt

Yeasts with disruptions in the genes PYC1 and PYC2 encoding the isoenzymes of pyruvate carboxylase cannot grow in a glucose-ammonium medium (Stucka et al. (1991) Mol. Gen. Genet. 229, 307-315). We have isolated a dominant mutation, BPC1-1, that allows growth in this medium of yeasts with interrupted PYC1 and PYC2 genes. The BPC1-1 mutation abolishes catabolite repression of a series of genes and allows expression...

Read the complete abstract on PubMed

Topics

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

Share to Alleles
Share to Base Sequence
Share to DNA, Fungal

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

Share to Isoenzymes

Share to Molecular Sequence Data

Share to Mutation

Share to Phenotype

Share to Saccharomyces cerevisiae

Source

Identifiers

PMID: 8543050
DOI: 10.1016/0014-5793(95)01337-7

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

A mutation affecting carbon catabolite repression suppresses growth defects in pyruvate carboxylase mutants from Saccharomyces cerevisiae.PMID 8543050Read ↗

Yarrowia lipolytica mutants devoid of pyruvate carboxylase activity show an unusual growth phenotype.Semantic proximity Read ↗

Regulation of pyruvate carboxylase isozyme (PYC1, PYC2) gene expression in Saccharomyces cerevisiae during fermentative and nonfermentative growth.Semantic proximity Read ↗

Autoregulation of yeast pyruvate decarboxylase gene expression requires the enzyme but not its catalytic activity.Semantic proximity Read ↗

Physiological characterisation of a pyruvate-carboxylase-negative Saccharomyces cerevisiae mutant in batch and chemostat cultures.Semantic proximity Read ↗

Isolation of the Pichia pastoris PYC1 gene encoding pyruvate carboxylase and identification of a suppressor of the pyc phenotype.Semantic proximity Read ↗

Regulation of pyc1 encoding pyruvate carboxylase isozyme I by nitrogen sources in Saccharomyces cerevisiae.Semantic proximity Read ↗

Isolation of a yeast mutant deficient in pyruvate carboxylase activity.Semantic proximity Read ↗

Pyruvate kinase (Pyk1) levels influence both the rate and direction of carbon flux in yeast under fermentative conditions.Semantic proximity Read ↗

Yeast mutants of glucose metabolism with defects in the coordinate regulation of carbon assimilation.Semantic proximity Read ↗

Characterization of a glucose-repressed pyruvate kinase (Pyk2p) in Saccharomyces cerevisiae that is catalytically insensitive to fructose-1,6-bisphosphate.Semantic proximity Read ↗

The transcarboxylase domain of pyruvate carboxylase is essential for assembly of the peroxisomal flavoenzyme alcohol oxidase.Semantic proximity Read ↗

Directed evolution of pyruvate decarboxylase-negative Saccharomyces cerevisiae, yielding a C2-independent, glucose-tolerant, and pyruvate-hyperproducing yeast.Semantic proximity Read ↗

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