ArticleProceedings of the National Academy of Sciences of the United States of America2013
Structure of the processive rubber oxygenase RoxA from Xanthomonas sp.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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26 citing papers in PubMed, 48 citations in OpenAlex.
- Review
- Heme handling in the system II heme lyase CcsBA from Bacteroides thetaiotaomicron.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2026Article
- Cleavage of natural rubber by rubber oxygenases in Gram-negative bacteria.Applied microbiology and biotechnology · 2024Review
- Recent Theoretical Insights into the Oxidative Degradation of Biopolymers and Plastics by Metalloenzymes.International journal of molecular sciences · 2023Review
- Assembly strategies for rubber-degrading microbial consortia based on omics tools.Frontiers in bioengineering and biotechnology · 2023Review
- In silico functional and evolutionary analyses of rubber oxygenases (RoxA and RoxB).3 Biotech · 2020Article
- Enzymatic degradation of plant biomass and synthetic polymers.Nature reviews. Chemistry · 2020Review
- Towards the understanding of the enzymatic cleavage of polyisoprene by the dihaem-dioxygenase RoxA.AMB Express · 2019Article
- First report of cis-1,4-polyisoprene degradation by Gordonia paraffinivorans.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2019Article
- Complete genome sequence of natural rubber-degrading, gram-negative bacterium,Biotechnology reports (Amsterdam, Netherlands) · 2019Article
- Rubber oxygenases.Applied microbiology and biotechnology · 2019Review
- Rhizobacter gummiphilus NS21 has two rubber oxygenases (RoxA and RoxB) acting synergistically in rubber utilisation.Applied microbiology and biotechnology · 2018Article
- Article
- Production of functionalized oligo-isoprenoids by enzymatic cleavage of rubber.Microbial biotechnology · 2017Article
- Structural and Functional Analysis of Latex Clearing Protein (Lcp) Provides Insight into the Enzymatic Cleavage of Rubber.Scientific reports · 2017Article
- RoxB Is a Novel Type of Rubber Oxygenase That Combines Properties of Rubber Oxygenase RoxA and Latex Clearing Protein (Lcp).Applied and environmental microbiology · 2017Article
- Assays for the Detection of Rubber Oxygenase Activities.Bio-protocol · 2017Article
- Heterolytic OO bond cleavage: Functional role of Glu113 during bis-Fe(IV) formation in MauG.Journal of inorganic biochemistry · 2017Article
- Cleavage of Rubber by the Latex Clearing Protein (Lcp) of Streptomyces sp. Strain K30: Molecular Insights.Applied and environmental microbiology · 2016Article
- Biochemical and spectroscopic characterization of purified Latex Clearing Protein (Lcp) from newly isolated rubber degrading Rhodococcus rhodochrous strain RPK1 reveals novel properties of Lcp.BMC microbiology · 2016Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Rubber oxygenase A (RoxA) is one of only two known enzymes able to catalyze the oxidative cleavage of latex for biodegradation. RoxA acts as a processive dioxygenase to yield the predominant product 12-oxo-4,8-dimethyl-trideca-4,8-diene-1-al (ODTD), a tri-isoprene unit. Here we present a structural analysis of RoxA from Xanthomonas sp. strain 35Y at a resolution of 1.8 Å. The enzyme is a 75-kDa diheme c-type cytochrome with an unusually low degree of secondary structure. Analysis of the heme group arrangement and peptide chain topology of RoxA confirmed a distant kinship with diheme peroxidases of the CcpA family, but the proteins are functionally distinct, and the extracellular RoxA has evolved to have twice the molecular mass by successively accumulating extensions of peripheral loops. RoxA incorporates both oxygen atoms of its cosubstrate dioxygen into the rubber cleavage product ODTD, and we show that RoxA is isolated with O2 stably bound to the active site heme iron. Activation and cleavage of O2 require binding of polyisoprene, and thus the substrate needs to use hydrophobic access channels to reach the deeply buried active site of RoxA. The location and nature of these channels support a processive mechanism of latex cleavage.
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