ArticleApplied and environmental microbiology2009
b-type dihydroorotate dehydrogenase is purified as a H2O2-forming NADH oxidase from Bifidobacterium bifidum.
Article in Applied and environmental microbiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 32 citations in OpenAlex.
- Roles of flavoprotein oxidase and the exogenous heme- and quinone-dependent respiratory chain in lactic acid bacteria.Bioscience of microbiota, food and health · 2024Review
- Oxidative Stress Response of Probiotic StrainFoods (Basel, Switzerland) · 2023Article
- Antimicrobial activity of Limosilactobacillus fermentum strains isolated from the human oral cavity against Streptococcus mutans.Scientific reports · 2023Article
- The Role of Hydrogen-Peroxide (HAntioxidants (Basel, Switzerland) · 2023Review
- Novel Insights into the Molecular Mechanisms Underlying Robustness and Stability in Probiotic Bifidobacteria.Applied and environmental microbiology · 2023Article
- Characterisation of putative class 1A DHODH-like proteins from Mucorales and dematiaceous mould species.PloS one · 2023Article
- Stress Response in Bifidobacteria.Microbiology and molecular biology reviews : MMBR · 2022Review
- Genome-Wide Assessment of Stress-Associated Genes in Bifidobacteria.Applied and environmental microbiology · 2022Article
- Optimized UV-Spectrophotometric Assay to Screen Bacterial Uricase Activity Using Whole Cell Suspension.Frontiers in microbiology · 2022Article
- Biomarkers and Utility of the Antioxidant Potential of Probiotic Lactobacilli and Bifidobacteria as Representatives of the Human Gut Microbiota.Biomedicines · 2021Review
- Probiotic Effector Compounds: Current Knowledge and Future Perspectives.Frontiers in microbiology · 2021Review
- Molecular insights into probiotic mechanisms of action employed against intestinal pathogenic bacteria.Gut microbes · 2020Review
- OScientific reports · 2018Article
- Hydrogen peroxide production by lactobacilli promotes epithelial restitution during colitis.Redox biology · 2018Article
- H(2)O(2) production in species of the Lactobacillus acidophilus group: a central role for a novel NADH-dependent flavin reductase.Applied and environmental microbiology · 2014Article
- Acquired tolerance to oxidative stress in Bifidobacterium longum 105-A via expression of a catalase gene.Applied and environmental microbiology · 2012Article
- Molecular clues to understand the aerotolerance phenotype of Bifidobacterium animalis subsp. lactis.Applied and environmental microbiology · 2012Article
- New method for selection of hydrogen peroxide adapted bifidobacteria cells using continuous culture and immobilized cell technology.Microbial cell factories · 2010Article
- Biosynthesis and degradation of H2O2 by vaginal lactobacilli.Applied and environmental microbiology · 2010Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Our previous report showed the existence of microaerophilic Bifidobacterium species that can grow well under aerobic conditions rather than anoxic conditions in a liquid shaking culture. The difference in the aerobic growth properties between the O(2)-sensitive and microaerophilic species is due to the existence of a system to produce H(2)O(2) in the growth medium. In this study, we purified and characterized the NADH oxidase that is considered to be a key enzyme in the production of H(2)O(2). Bifidobacterium bifidum, an O(2)-sensitive bacterium and the type species of the genus Bifidobacterium, possessed one dominant active fraction of NADH oxidase and a minor active fraction of NAD(P)H oxidase activity detected in the first step of column chromatography for purification of the enzyme. The dominant active fraction was further purified and determined from its N-terminal sequence to be a homologue of b-type dihydroorotate dehydrogenase (DHOD), composed of PyrK (31 kDa) and PyrDb (34 kDa) subunits. The genes that encode PyrK and PryDb are tandemly located within an operon structure. The purified enzyme was found to be a heterotetramer showing the typical spectrum of a flavoprotein, and flavin mononucleotide and flavin adenine dinucleotide were identified as cofactors. The purified enzyme was characterized as the enzyme that catalyzes the DHOD reaction and also catalyzes a H(2)O(2)-forming NADH oxidase reaction in the presence of O(2). The kinetic parameters suggested that the enzyme could be involved in H(2)O(2) production in highly aerated environments.
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