ArticleFolia microbiologica1998
Glucose repression of maltase and methanol-oxidizing enzymes in the methylotrophic yeast Hansenula polymorpha: isolation and study of regulatory mutants.
Article in Folia microbiologica, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed, 20 citations in OpenAlex.
- Characterization of a Maltase from an Early-Diverged Non-Conventional YeastInternational journal of molecular sciences · 2019Article
- Article
- Maltase protein of Ogataea (Hansenula) polymorpha is a counterpart to the resurrected ancestor protein ancMALS of yeast maltases and isomaltases.Yeast (Chichester, England) · 2016Article
- Pichia pastoris 14-3-3 regulates transcriptional activity of the methanol inducible transcription factor Mxr1 by direct interaction.Molecular microbiology · 2012Article
- Regulation of methanol utilisation pathway genes in yeasts.Microbial cell factories · 2006Article
- Sugar repression in the methylotrophic yeast Hansenula polymorpha studied by using hexokinase-negative, glucokinase-negative and double kinase-negative mutants.Folia microbiologica · 2000Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
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Abstract
Regulation of the synthesis of maltase and methanol-oxidizing enzymes by the carbon source has been analyzed in the methylotrophic yeast Hansenula polymorpha. Maltase was shown to be responsible for the growth of H. polymorpha not only on maltose, but also on sucrose. The affinity of maltase towards maltase substrates decreased in the order: 4-nitrophenyl glucoside (PNPG) < sucrose < maltose. Mutants with glucose repression-insensitive synthesis of alcohol oxidase and maltase were obtained from H. polymorpha by mutagenesis and subsequent selection on methanol medium in the presence of 2-deoxy-D-glucose. One of the isolated mutants, L63, was studied in more detail. Mutant L63 was recessive and monogenic and it was not deficient in hexokinase. Its analysis revealed that H. polymorpha most probably has a repressor protein that in the presence of glucose can down-regulate expression of both maltase and enzymes of methanol oxidation.
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