ArticleThe Journal of biological chemistry2016
Structure of the Catalytic Domain of the Class I Polyhydroxybutyrate Synthase from Cupriavidus necator.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
30 citing papers in PubMed, 95 citations in OpenAlex.
- In silico elucidation of polyhydroxyalkanoate biosynthesis pathways in Brevibacterium daeguense and Brevibacterium yomogidense.World journal of microbiology & biotechnology · 2026Article
- PHA synthase variant design using a conditional variational autoencoder.PLoS computational biology · 2026Article
- Metabolic Engineering Strategies for Enhanced Polyhydroxyalkanoate (PHA) Production inPolymers · 2025Review
- Structures of Polyhydroxyalkanoate Synthase PhaC from Aeromonas caviae, Producing Biodegradable Plastics.Angewandte Chemie (International ed. in English) · 2025Article
- Superlative short chain length and medium chain length polyhydroxyalkanoates microbial producers isolated from Malaysian environment.Archives of microbiology · 2025Review
- N-terminal truncation of PhaCMicrobial cell factories · 2024Article
- Article
- Exploring Class I polyhydroxyalkanoate synthases with broad substrate specificity for polymerization of structurally diverse monomer units.Frontiers in bioengineering and biotechnology · 2023Article
- A review on microbial synthesis of lactate-containing polyesters.World journal of microbiology & biotechnology · 2022Review
- Microplastics a Novel Substratum for Polyhydroxyalkanoate (PHA)-Producing Bacteria in Aquatic Environments.Current microbiology · 2022Article
- Construction of a Rhodobacter sphaeroides Strain That Efficiently Produces Hydrogen Gas from Acetate without Poly(β-Hydroxybutyrate) Accumulation: Insight into the Role of PhaR in Acetate Metabolism.Applied and environmental microbiology · 2022Article
- High natural PHA production from acetate in Cobetia sp. MC34 and Cobetia marina DSM 4741Microbial cell factories · 2021Article
- Genome-Wide Metabolic Reconstruction of the Synthesis of Polyhydroxyalkanoates from Sugars and Fatty Acids byMicroorganisms · 2021Review
- Prospects of Using Biocatalysis for the Synthesis and Modification of Polymers.Molecules (Basel, Switzerland) · 2021Review
- Tools for the discovery of biopolymer producing cysteine relays.Biophysical reviews · 2021Review
- Engineering ofFrontiers in bioengineering and biotechnology · 2021Article
- Article
- PHA Production and PHA Synthases of the Halophilic BacteriumBioengineering (Basel, Switzerland) · 2020Article
- Complete Genome Sequence of a Novel Polyhydroxyalkanoate (PHA) Producer, Jeongeupia sp. USM3 (JCM 19920) and Characterization of Its PHA Synthases.Current microbiology · 2020Article
- Functional Annotation of ABHD14B, an Orphan Serine Hydrolase Enzyme.Biochemistry · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Polyhydroxybutyrate synthase (PhaC) catalyzes the polymerization of 3-(R)-hydroxybutyryl-coenzyme A as a means of carbon storage in many bacteria. The resulting polymers can be used to make biodegradable materials with properties similar to those of thermoplastics and are an environmentally friendly alternative to traditional petroleum-based plastics. A full biochemical and mechanistic understanding of this process has been hindered in part by a lack of structural information on PhaC. Here we present the first structure of the catalytic domain (residues 201-589) of the class I PhaC from Cupriavidus necator (formerly Ralstonia eutropha) to 1.80 Å resolution. We observe a symmetrical dimeric architecture in which the active site of each monomer is separated from the other by ∼33 Å across an extensive dimer interface, suggesting a mechanism in which polyhydroxybutyrate biosynthesis occurs at a single active site. The structure additionally highlights key side chain interactions within the active site that play likely roles in facilitating catalysis, leading to the proposal of a modified mechanistic scheme involving two distinct roles for the active site histidine. We also identify putative substrate entrance and product egress routes within the enzyme, which are discussed in the context of previously reported biochemical observations. Our structure lays a foundation for further biochemical and structural characterization of PhaC, which could assist in engineering efforts for the production of eco-friendly materials.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.