Hydrogen peroxide-producing pyruvate oxidase from Lactobacillus delbrueckii is catalytically activated by phosphotidylethanolamine.
Autor: | Cornacchione LP; Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, MA, 02111, USA. Lou.Cornacchione@gmail.com., Hu LT; Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, MA, 02111, USA. |
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Jazyk: | angličtina |
Zdroj: | BMC microbiology [BMC Microbiol] 2020 May 24; Vol. 20 (1), pp. 128. Date of Electronic Publication: 2020 May 24. |
DOI: | 10.1186/s12866-020-01788-6 |
Abstrakt: | Background: Pyruvate 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. Results: We 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 Conclusions: To 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. |
Databáze: | MEDLINE |
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