ArticleMicrobiological research
Differential contribution of the proline and glutamine pathways to glutamate biosynthesis and nitrogen assimilation in yeast lacking glutamate dehydrogenase.
Article in Microbiological research. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed, 26 citations in OpenAlex.
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- Metabolic and Synthetic Biology Strategies for Enhancing Single-Cell Protein Production in Saccharomyces cerevisiae.Biotechnology journal · 2026Review
- Deciphering the ammonia transformation mechanism of a novel marine multi-stress-tolerant yeast,Applied and environmental microbiology · 2025Article
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- Identification and genomic analysis of a thermophilic bacterial strain that reduces ammonia loss from composting.Microbiology spectrum · 2024Article
- Proteomics ofJournal of fungi (Basel, Switzerland) · 2023Article
- Effects of Different Nitrogen Levels on Lignocellulolytic Enzyme Production and Gene Expression under Straw-State Cultivation inInternational journal of molecular sciences · 2023Article
- Transcriptomic and enzymatic analysis reveals the roles of glutamate dehydrogenase in Corynebacterium glutamicum.AMB Express · 2022Article
- The pleiotropic effects of the glutamate dehydrogenase (GDH) pathway in Saccharomyces cerevisiae.Microbial cell factories · 2018Review
- A metabolomic study of the effect ofNPJ biofilms and microbiomesArticle
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2 authors at 1 institution in 1 country.
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Abstract
In Saccharomyces cerevisiae, the glutamate dehydrogenase (GDH) enzymes play a pivotal role in glutamate biosynthesis and nitrogen assimilation. It has been proposed that, in GDH-deficient yeast, either the proline utilization (PUT) or the glutamine synthetase-glutamate synthase (GS/GOGAT) pathway serves as the alternative pathway for glutamate production and nitrogen assimilation to the exclusion of the other. Using a gdh-null mutant (gdh1Δ2Δ3Δ), this ambiguity was addressed using a combination of growth studies and pathway-specific enzyme assays on a variety of nitrogen sources (ammonia, glutamine, proline and urea). The GDH-null mutant was viable on all nitrogen sources tested, confirming that alternate pathways for nitrogen assimilation exist in the gdh-null strain. Enzyme assays point to GS/GOGAT as the primary alternative pathway on the preferred nitrogen sources ammonia and glutamine, whereas growth on proline required both the PUT and GS/GOGAT pathways. In contrast, growth on glucose-urea media elicited a decrease in GOGAT activity along with an increase in activity of the PUT pathway specific enzyme Δ(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH). Together, these results suggest the alternative pathway for nitrogen assimilation in strains lacking the preferred GDH-dependent route is nitrogen source dependent and that neither GS/GOGAT nor PUT serves as the sole compensatory pathway.
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