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In Streptococcus thermophilus, Ammonia from Urea Hydrolysis Paradoxically Boosts Acidification and Reveals a New Regulatory Mechanism of Glycolysis

Stefania Arioli, Giulia Della Scala, Anđela Martinović, Leonardo Scaglioni, Stefania Mazzini, Federica Volontè, Martin Bastian Pedersen, Diego Mora

2022Microbiology Spectrum15 citationsDOIOpen Access PDF

Abstract

Finding that ammonia-generating enzymes, such as urease, and exogenous ammonia act on phosphofructokinase activity shed new light on the regulatory mechanisms that govern glycolysis. Phosphofructokinase is the key enzyme known to exert a regulatory role on glycolytic flux and, therefore, ammonia as an effector of phosphofructokinase acts, in cascade, modulating the glycolytic pathway. Apart from S. thermophilus, due to the high conservation of glycolytic enzymes in all branches of the tree of life and being aware of the role of ammonia as an effector of phosphofructokinase, we propose to reevaluate the physiological role of the ammonia production pathways in all organisms whose energy metabolism is supported by glycolysis.

Topics & Concepts

PhosphofructokinaseGlycolysisBiochemistryAmmoniaEffectorChemistryEnzymeFlux (metallurgy)BiologyOrganic chemistryNeonatal Health and BiochemistryGenomics and Phylogenetic StudiesStreptococcal Infections and Treatments
In Streptococcus thermophilus, Ammonia from Urea Hydrolysis Paradoxically Boosts Acidification and Reveals a New Regulatory Mechanism of Glycolysis | Litcius