ArticleApplied and environmental microbiology2008
Poly(3-hydroxybutyrate) (PHB) depolymerase PhaZa1 is involved in mobilization of accumulated PHB in Ralstonia eutropha H16.
Article in Applied and environmental microbiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 56 citations in OpenAlex.
- Animal degradation of microbial storage polyhydroxyalkanoates.Nature ecology & evolution · 2026Article
- The Carbon Source Effect on the Production of Ralstonia eutropha H16 and Proteomic Response Underlying Targeting the Bioconversion with Solar Fuels.Applied biochemistry and biotechnology · 2022Article
- The transcription activator AtxA fromSynthetic biology (Oxford, England) · 2022Article
- 3-Hydroxybutyrate Derived from Poly-3-Hydroxybutyrate Mobilization Alleviates Protein Aggregation in Heat-Stressed Herbaspirillum seropedicae SmR1.Applied and environmental microbiology · 2020Article
- 3-Hydroxybutyrate Is Active Compound in Flax That Upregulates Genes Involved in DNA Methylation.International journal of molecular sciences · 2020Article
- Beyond Intracellular Accumulation of Polyhydroxyalkanoates: Chiral Hydroxyalkanoic Acids and Polymer Secretion.Frontiers in bioengineering and biotechnology · 2020Review
- The Puzzling Conservation and Diversification of Lipid Droplets from Bacteria to Eukaryotes.Results and problems in cell differentiation · 2020Article
- Quorum Sensing Controls Both Rhamnolipid and Polyhydroxyalkanoate Production inFrontiers in bioengineering and biotechnology · 2020Article
- Importance of Poly-3-Hydroxybutyrate Metabolism to the Ability of Herbaspirillum seropedicae To Promote Plant Growth.Applied and environmental microbiology · 2019Article
- Poly(3-Hydroxybutyrate) (PHB) Polymerase PhaC1 and PHB Depolymerase PhaZa1 of Ralstonia eutropha Are PhosphorylatedApplied and environmental microbiology · 2018Article
- Genome characteristics dictate poly-R-(3)-hydroxyalkanoate production in Cupriavidus necator H16.World journal of microbiology & biotechnology · 2018Review
- Absence of ppGpp Leads to Increased Mobilization of Intermediately Accumulated Poly(3-Hydroxybutyrate) in Ralstonia eutropha H16.Applied and environmental microbiology · 2017Article
- Regulation of Polyhydroxybutyrate Synthesis in the Soil Bacterium Bradyrhizobium diazoefficiens.Applied and environmental microbiology · 2016Article
- Engineering a predatory bacterium as a proficient killer agent for intracellular bio-products recovery: The case of the polyhydroxyalkanoates.Scientific reports · 2016Article
- σ54-Dependent Response to Nitrogen Limitation and Virulence in Burkholderia cenocepacia Strain H111.Applied and environmental microbiology · 2015Article
- A patatin-like protein associated with the polyhydroxyalkanoate (PHA) granules of Haloferax mediterranei acts as an efficient depolymerase in the degradation of native PHA.Applied and environmental microbiology · 2015Article
- Comparative proteome analysis reveals four novel polyhydroxybutyrate (PHB) granule-associated proteins in Ralstonia eutropha H16.Applied and environmental microbiology · 2015Article
- To be or not to be a poly(3-hydroxybutyrate) (PHB) depolymerase: PhaZd1 (PhaZ6) and PhaZd2 (PhaZ7) of Ralstonia eutropha, highly active PHB depolymerases with no detectable role in mobilization of accumulated PHB.Applied and environmental microbiology · 2014Article
- PHB granules are attached to the nucleoid via PhaM in Ralstonia eutropha.BMC microbiology · 2012Article
- Localization of poly(3-hydroxybutyrate) (PHB) granule-associated proteins during PHB granule formation and identification of two new phasins, PhaP6 and PhaP7, in Ralstonia eutropha H16.Journal of bacteriology · 2012Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The recently finished genome sequence of Ralstonia eutropha H16 harbors nine genes that are thought to encode functions for intracellular depolymerization (mobilization) of storage poly(3-hydroxybutyrate) (PHB). Based on amino acid similarities, the gene products belong to four classes (PhaZa1 to PhaZa5, PhaZb, PhaZc, and PhaZd1/PhaZd2). However, convincing direct evidence for the in vivo roles of the gene products is poor. In this study, we selected four candidate genes (phaZa1, phaZb, phaZc, and phaZd1) representing the four classes and investigated the physiological function of the gene products (i) with recombinant Escherichia coli strains and (ii) with R. eutropha null mutants. Evidence for weak but significant PHB depolymerase activity was obtained only for PhaZa1. The physiological roles of the other potential PHB depolymerases remain uncertain.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.