ArticleExtremophiles : life under extreme conditions2016
Characterization of a novel metallo-β-lactamases fold hydrolase from Pelagibacterium halotolerans, a marine halotolerant bacterium isolated from East China Sea.
Article in Extremophiles : life under extreme conditions, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Drought-induced microbial dynamics in cowpea rhizosphere: Exploring bacterial diversity and bioinoculant prospects.PloS one · 2025Article
- Comparative Metagenomic Study of Rhizospheric and Bulk Mercury-Contaminated Soils in the Mining District of Almadén.Frontiers in microbiology · 2022Article
- Carbapenem Resistance among Marine Bacteria-An Emerging Threat to the Global Health Sector.Microorganisms · 2021Review
- Diversity and Genetic Basis for Carbapenem Resistance in a Coastal Marine Environment.Applied and environmental microbiology · 2020Article
- Comparative mangrove metagenome reveals global prevalence of heavy metals and antibiotic resistome across different ecosystems.Scientific reports · 2018Article
- Biochemical and genetic characterization of a novel metallo-β-lactamase from marine bacterium Erythrobacter litoralis HTCC 2594.Scientific reports · 2018Article
- Microbial Diversity in Extreme Marine Habitats and Their Biomolecules.Microorganisms · 2017Review
- Pelagibacterium lixinzhangensis sp. nov., a Novel Member of the Genus Pelagibacterium.Current microbiology · 2016Article
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Authors and funding
5 authors.
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Abstract
In this study, a novel metallo-β-lactamases fold hydrolase PH-1 was identified from Pelagibacterium halotolerans B2(T). This novel member of the family Hyphomicrobiaceae was isolated from the East China Sea. In silico analysis demonstrated that PH-1 and its relative homologues cluster in a unique branch and constitute a new subgroup among MBLs. PH-1 was cloned and overexpressed in Escherichia coli BL21 in a soluble form. SDS-PAGE, MALDI-TOF/TOF-MS, and size-exclusion chromatography analysis demonstrated that the PH-1 was a monomer with molecular weight of about 29 kDa. Substrate specificity study showed PH-1 preferred penicillin type β-lactams and exhibited maximum activity toward penicillin-G. Additionally, our experiments also revealed that PH-1 was a halotolerant enzyme since it is active under 4 M NaCl. The enzyme activity of PH-1 was negatively affected by 1 mM Mn(2+) and EDTA. These observations lay a foundation for further study of MBLs from marine bacterium.
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