ArticleBMC microbiology2020
Hydrogen peroxide-producing pyruvate oxidase from Lactobacillus delbrueckii is catalytically activated by phosphotidylethanolamine.
Article in BMC microbiology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 16 citations in OpenAlex.
- Human colostrum as a probiotic reservoir: a genomic insights into potential probiotic traits.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2026Article
- Understanding the probiotic potential of a healthy human vaginal flora, Lactobacillus gasseri K9: genomic and in vitro aspects.Journal, genetic engineering & biotechnology · 2026Article
- Preparation and biomedical applications of single-metal atom catalysts.Nature protocols · 2026Review
- The Potential Teeth Bleaching and Halitosis Prevention Effects ofJournal of functional biomaterials · 2024Article
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- The development of an ingestible biosensor for the characterization of gut metabolites related to major depressive disorder: hypothesis and theory.Frontiers in systems biology · 2023Article
- Post-translational modification of Streptococcus sanguinis SpxB influences protein solubility and HMolecular oral microbiology · 2021Article
- High-quality whole-genome sequence analysis of Lactobacillus paragasseri UBLG-36 reveals oxalate-degrading potential of the strain.PloS one · 2021Article
- Raising the 'Good' Oxidants for Immune Protection.Frontiers in immunology · 2021Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
backgroundPyruvate oxidase (Pox) is an important enzyme in bacterial metabolism for increasing ATP production and providing a fitness advantage via hydrogen peroxide production. However, few Pox enzymes have been characterized from bacterial species. The tetrameric non-hydrogen-peroxide producing Pox from E. coli is activated by phospholipids, which is important for its function in vivo.
resultsWe characterized the hydrogenperoxide-producing Pox from L. delbrueckii strain STYM1 and showed it is specifically activated by phosphotidylethanolamine (16:0-18:1), but not by phosphotidylcholine or phosphotidylglycerol. This activation is a mixture of K- and V-type activation as both k
conclusionsTo our knowledge this is the first known hydrogenperoxide-producing Pox enzyme that is activated by phospholipids. Our results suggest that there are substantial differences between Pox enzymes from different bacterial species, which could be important for their role in biological systems as well as in the development of Pox-based biosensors.
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