ArticleApplied and environmental microbiology2015
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.
Article in Applied and environmental microbiology, 2015. 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, 54 citations in OpenAlex.
- Nitrile rubber biodegradation byApplied and environmental microbiology · 2025Article
- Microbial plastic degradation: enzymes, pathways, challenges, and perspectives.Microbiology and molecular biology reviews : MMBR · 2025Review
- New insights on poly(Frontiers in bioengineering and biotechnology · 2025Article
- Endophytic bacterial diversity in the latex-bearing caulosphere of Hevea brasiliensis Müll. Arg.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2024Article
- Computational investigation of cis-1,4-polyisoprene binding to the latex-clearing protein LcpK30.PloS one · 2024Article
- Recent Theoretical Insights into the Oxidative Degradation of Biopolymers and Plastics by Metalloenzymes.International journal of molecular sciences · 2023Review
- Microbial enzymes will offer limited solutions to the global plastic pollution crisis.Microbial biotechnology · 2023Review
- Biodegradation of rubber in cultures of Rhodococcus rhodochrous and by its enzyme latex clearing protein.Biodegradation · 2022Article
- Characterization of Latex-Clearing Protein and Aldehyde Dehydrogenases Involved in the Utilization of poly(cis-1,4-isoprene) by Nocardia farcinica NBRC 15532Microorganisms · 2022Article
- Microbial Degradation of Rubber: Actinobacteria.Polymers · 2021Review
- In vitro studies on the degradation of common rubber waste material with the latex clearing protein (Lcp1Biodegradation · 2021Article
- Characterization of the genes responsible for rubber degradation in Actinoplanes sp. strain OR16.Applied microbiology and biotechnology · 2020Article
- Global Regulator of Rubber Degradation in Gordonia polyisoprenivorans VH2: Identification and Involvement in the Regulation Network.Applied and environmental microbiology · 2020Article
- Fragmentation of plastic objects in a laboratory seawater microcosm.Scientific reports · 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
- 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
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3 authors at 1 institution in 1 country.
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Abstract
Specific polyisoprene-cleaving activities of 1.5 U/mg and 4.6 U/mg were determined for purified Strep-tagged latex clearing protein (Lcp) of Streptomyces sp. strain K30 at 23 °C and 37 °C, respectively. Metal analysis revealed the presence of approximately one atom of iron per Lcp molecule. Copper, which had been identified in Lcp1VH2 of Gordonia polyisoprenivorans previously, was below the detection limit in LcpK30. Heme was identified as a cofactor in purified LcpK30 by (i) detection of characteristic α-, β-, and γ (Soret)-bands at 562 nm, 532 nm, and 430 nm in the visible spectrum after chemical reduction, (ii) detection of an acetone-extractable porphyrin molecule, (iii) determination of a heme b-type-specific absorption maximum (556 nm) after chemical conversion of the heme group to a bipyridyl-heme complex, and (iv) detection of a b-heme-specific m/z value of 616.2 via mass spectrometry. Spectroscopic analysis showed that purified Lcp as isolated contains an oxidized heme-Fe(3+) that is free of bound dioxygen. This is in contrast to the rubber oxygenase RoxA, a c-type heme-containing polyisoprene-cleaving enzyme present in Gram-negative rubber degraders, in which the covalently bound heme firmly binds a dioxygen molecule. LcpK30 also differed from RoxA in the lengths of the rubber degradation cleavage products and in having a higher melting point of 61.5 °C (RoxA, 54.3 °C). In summary, RoxA and Lcp both are equipped with a heme cofactor and catalyze an oxidative C-C cleavage reaction but differ in the heme subgroup type and in several biochemical and biophysical properties. These findings suggest differences in the catalytic reaction mechanisms.
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