ArticleApplied and environmental microbiology2015
A patatin-like protein associated with the polyhydroxyalkanoate (PHA) granules of Haloferax mediterranei acts as an efficient depolymerase in the degradation of native PHA.
Article in Applied and environmental microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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15 citing papers in PubMed, 29 citations in OpenAlex.
- Advanced Strategies for Poly(3-hydroxybutyrate-co-3-hydroxyvalerate) Production: PHA Synthase Homologous Overexpression in the ExtremophileMarine drugs · 2025Article
- Genetic identification of acetyl-CoA synthetases involved in acetate activation inApplied and environmental microbiology · 2025Article
- Transcriptomic profiling of haloarchaeal denitrification through RNA-Seq analysis.Applied and environmental microbiology · 2024Article
- Bioplastic Production from Agri-Food Waste through the Use ofMicroorganisms · 2024Review
- Unveiling the repressive mechanism of a PPS-like regulator (PspR) in polyhydroxyalkanoates biosynthesis network.Applied microbiology and biotechnology · 2024Article
- A novel halolysin without C-terminal extension from an extremely halophilic archaeon.Applied microbiology and biotechnology · 2022Article
- Evaluating haloarchaeal culture media for ultrahigh-molecular-weight polyhydroxyalkanoate biosynthesis by Haloferax mediterranei.Applied microbiology and biotechnology · 2021Article
- Tools for the discovery of biopolymer producing cysteine relays.Biophysical reviews · 2021Review
- Halophilic archaea and their potential to generate renewable fuels and chemicals.Biotechnology and bioengineering · 2021Review
- Characterization of a novel Cu-containing dissimilatory nitrite reductase from the haloarchaeon Halorussus sp. YCN54.Extremophiles : life under extreme conditions · 2020Article
- Current developments on polyhydroxyalkanoates synthesis by using halophiles as a promising cell factory.Microbial cell factories · 2020Review
- Unusual Phosphoenolpyruvate (PEP) Synthetase-Like Protein Crucial to Enhancement of Polyhydroxyalkanoate Accumulation in Haloferax mediterranei Revealed by Dissection of PEP-Pyruvate Interconversion Mechanism.Applied and environmental microbiology · 2019Article
- Polyhydroxyalkanoate Biosynthesis at the Edge of Water Activitiy-Haloarchaea as Biopolyester Factories.Bioengineering (Basel, Switzerland) · 2019Review
- Designing and EngineeringFrontiers in microbiology · 2019Article
- Enoyl-CoA hydratase mediates polyhydroxyalkanoate mobilization in Haloferax mediterranei.Scientific reports · 2016Article
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8 authors at 4 institutions in 1 country.
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Abstract
The key enzymes and pathways involved in polyhydroxyalkanoate (PHA) biosynthesis in haloarchaea have been identified in recent years, but the haloarchaeal enzymes for PHA degradation remain unknown. In this study, a patatin-like PHA depolymerase, PhaZh1, was determined to be located on the PHA granules in the haloarchaeon Haloferax mediterranei. PhaZh1 hydrolyzed the native PHA (nPHA) [including native polyhydroxybutyrate (nPHB) and native poly(3-hydroxybutyrate-co-3-hydroxyvalerate) (nPHBV) in this study] granules in vitro with 3-hydroxybutyrate (3HB) monomer as the primary product. The site-directed mutagenesis of PhaZh1 indicated that Gly16, Ser47 (in a classical lipase box, G-X-S47-X-G), and Asp195 of this depolymerase were essential for its activity in nPHA granule hydrolysis. Notably, phaZh1 and bdhA (encoding putative 3HB dehydrogenase) form a gene cluster (HFX_6463 to _6464) in H. mediterranei. The 3HB monomer generated from nPHA degradation by PhaZh1 could be further converted into acetoacetate by BdhA, indicating that PhaZh1-BdhA may constitute the first part of a PHA degradation pathway in vivo. Interestingly, although PhaZh1 showed efficient activity and was most likely the key enzyme in nPHA granule hydrolysis in vitro, the knockout of phaZh1 had no significant effect on the intracellular PHA mobilization, implying the existence of an alternative PHA mobilization pathway(s) that functions effectively within the cells of H. mediterranei. Therefore, identification of this patatin-like depolymerase of haloarchaea may provide a new strategy for producing the high-value-added chiral compound (R)-3HB and may also shed light on the PHA mobilization in haloarchaea.
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