ArticleApplied and environmental microbiology2013
Haloarchaeal-type β-ketothiolases involved in Poly(3-hydroxybutyrate-co-3-hydroxyvalerate) synthesis in Haloferax mediterranei.
Article in Applied and environmental microbiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 30 citations in OpenAlex.
- Insights into transcriptional expression and putative functions of multiple polyhydroxyalkanoate synthase paralogs in Haloferax mediterranei.FEMS microbiology letters · 2026Article
- Bioplastic Production from Agri-Food Waste through the Use ofMicroorganisms · 2024Review
- Copolymers and Blends Based on 3-Hydroxybutyrate and 3-Hydroxyvalerate Units.International journal of molecular sciences · 2023Review
- An updated overview on the regulatory circuits of polyhydroxyalkanoates synthesis.Microbial biotechnology · 2022Review
- Study on the production of high 3HV content PHBVFrontiers in microbiology · 2022Article
- Production of Polyhydroxyalkanoates in Unsterilized Hyper-Saline Medium by Halophiles Using Waste Silkworm Excrement as Carbon Source.Molecules (Basel, Switzerland) · 2021Article
- Optimising PHBV biopolymer production in haloarchaea via CRISPRi-mediated redirection of carbon flux.Communications biology · 2021Article
- Current developments on polyhydroxyalkanoates synthesis by using halophiles as a promising cell factory.Microbial cell factories · 2020Review
- Polyhydroxyalkanoate Biosynthesis at the Edge of Water Activitiy-Haloarchaea as Biopolyester Factories.Bioengineering (Basel, Switzerland) · 2019Review
- Archaeal acetoacetyl-CoA thiolase/HMG-CoA synthase complex channels the intermediate via a fused CoA-binding site.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Characterization of an Aldolase Involved in Cholesterol Side Chain Degradation in Mycobacterium tuberculosis.Journal of bacteriology · 2018Article
- Enoyl-CoA hydratase mediates polyhydroxyalkanoate mobilization in Haloferax mediterranei.Scientific reports · 2016Article
- 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
- Integration of poly-3-(hydroxybutyrate-co-hydroxyvalerate) production by Haloferax mediterranei through utilization of stillage from rice-based ethanol manufacture in India and its techno-economic analysis.World journal of microbiology & biotechnology · 2015Article
- A novel DNA-binding protein, PhaR, plays a central role in the regulation of polyhydroxyalkanoate accumulation and granule formation in the haloarchaeon Haloferax mediterranei.Applied and environmental microbiology · 2015Article
- Propionyl coenzyme A (propionyl-CoA) carboxylase in Haloferax mediterranei: Indispensability for propionyl-CoA assimilation and impacts on global metabolism.Applied and environmental microbiology · 2015Article
- Production of poly-3-(hydroxybutyrate-co-hydroxyvalerate) by Haloferax mediterranei using rice-based ethanol stillage with simultaneous recovery and re-use of medium salts.Extremophiles : life under extreme conditions · 2014Article
- Archaeal production of polyhydroxyalkanoate (PHA) co- and terpolyesters from biodiesel industry-derived by-products.Archaea (Vancouver, B.C.) · 2013Article
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7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The key enzymes for poly(3-hydroxybutyrate-co-3-hydroxyvalerate) (PHBV) biosynthesis in haloarchaea have been identified except the β-ketothiolase(s), which condense two acetyl coenzyme A (acetyl-CoA) molecules to acetoacetyl-CoA, or one acetyl-CoA and one propionyl-CoA to 3-ketovaleryl-CoA. Whole-genome analysis has revealed eight potential β-ketothiolase genes in the haloarchaeon Haloferax mediterranei, among which the PHBV-specific BktB and PhaA were identified by gene knockout and complementation analysis. Unlike all known bacterial counterparts encoded by a single gene, the haloarchaeal PhaA that was involved in acetoacetyl-CoA generation, was composed of two different types of subunits (PhaAα and PhaAβ) and encoded by the cotranscribed HFX_1023 (phaAα) and HFX_1022 (phaAβ) genes. Similarly, the BktB that was involved in generation of acetoacetyl-CoA and 3-ketovaleryl-CoA, was also composed of two different types of subunits (BktBα and BktBβ) and encoded by cotranscribed HFX_6004 (bktBα) and HFX_6003 (bktBβ). BktBα and PhaAα were the catalytic subunits and determined substrate specificities of BktB and PhaA, respectively. Their catalytic triad "Ser-His-His" was distinct from the bacterial "Cys-His-Cys." BktBβ and PhaAβ both contained an oligosaccharide-binding fold domain, which was essential for the β-ketothiolase activity. Interestingly, BktBβ and PhaAβ were functionally interchangeable, although PhaAβ preferred functioning with PhaAα. In addition, BktB showed biotechnological potential for the production of PHBV with the desired 3-hydroxyvalerate fraction in haloarchaea. This is the first report of the haloarchaeal type of PHBV-specific β-ketothiolases, which are distinct from their bacterial counterparts in both subunit composition and catalytic residues.
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