ArticleApplied and environmental microbiology2013
Functional identification of rubber oxygenase (RoxA) in soil and marine myxobacteria.
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 21 papers.
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Who cites it
21 citing papers in PubMed, 41 citations in OpenAlex.
- Myxobacteria: Versatile cell factories of novel commercial enzymes for bio-manufacturing.Biotechnology advances · 2025Review
- Cleavage of natural rubber by rubber oxygenases in Gram-negative bacteria.Applied microbiology and biotechnology · 2024Review
- Enzymatic reactions towards aldehydes: An overview.Flavour and fragrance journal · 2023Review
- Assembly strategies for rubber-degrading microbial consortia based on omics tools.Frontiers in bioengineering and biotechnology · 2023Review
- Microbial Degradation of Rubber: Actinobacteria.Polymers · 2021Review
- In silico functional and evolutionary analyses of rubber oxygenases (RoxA and RoxB).3 Biotech · 2020Article
- Towards the understanding of the enzymatic cleavage of polyisoprene by the dihaem-dioxygenase RoxA.AMB Express · 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
- Metabolic and Biosynthetic Diversity in Marine Myxobacteria.Marine drugs · 2018Review
- 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
- 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
- Latex Clearing Protein (Lcp) of Streptomyces sp. Strain K30 Is a b-Type Cytochrome and Differs from Rubber Oxygenase A (RoxA) in Its Biophysical Properties.Applied and environmental microbiology · 2015Article
- Latex clearing protein-an oxygenase cleaving poly(cis-1,4-isoprene) rubber at the cis double bonds.Applied and environmental microbiology · 2014Article
- Rubber oxygenase and latex clearing protein cleave rubber to different products and use different cleavage mechanisms.Applied and environmental microbiology · 2014Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The rubber oxygenase (RoxA) of Xanthomonas sp. strain 35Y (RoxA(Xsp)) is so far the only known extracellular c-type diheme cytochrome that is able to cleave poly(cis-1,4-isoprene). All other rubber-degrading bacteria described are Gram positive and employ a nonheme protein (latex-clearing protein [Lcp]) for the postulated primary attack of polyisoprene. Here, we identified RoxA orthologs in the genomes of Haliangium ochraceum, Myxococcus fulvus, Corallococcus coralloides, and Chondromyces apiculatus. The roxA orthologs of H. ochraceum (RoxA(Hoc)), C. coralloides BO35 (RoxA(Cco)), and M. fulvus (RoxA(Mfu)) were functionally expressed in a ΔroxA Xanthomonas sp. 35Y background. All RoxA orthologs oxidatively cleaved polyisoprene, as revealed by restoration of clearing-zone formation and detection of 12-oxo-4,8-dimethyltrideca-4,8-diene-1-al (ODTD) as a cleavage product. RoxA(Xsp), RoxA(Mfu), and RoxA(Cco) were purified and biochemically characterized. The optimal temperature of RoxA(Cco) and RoxA(Mfu) was between 22 and 30°C. All RoxA orthologs as isolated showed an oxidized UV-visible spectrum. Chemical reduction of RoxA(Cco) and RoxA(Mfu) indicated the presence of two slightly different heme centers with absorption maxima between 549 and 553 nm, similar to RoxA(Xsp). Sequence analysis and modeling of the three-dimensional structures of the RoxA orthologs revealed a high degree of similarity to the recently solved RoxA(Xsp) structure and included several conserved residues, notably, W302, F317, and a MauG motif at about H517. Lcp-like sequences were not detected in the genomes of the Xanthomonas sp. 35Y, H. ochraceum, M. fulvus, and C. coralloides. No RoxA orthologs were found in Gram-positive bacteria, and this first description of functional RoxA in Gram-negative bacteria other than Xanthomonas proves that RoxA is more common among rubber degraders than was previously assumed.
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