ArticleProceedings of the National Academy of Sciences of the United States of America2007
Phycobilin:cystein-84 biliprotein lyase, a near-universal lyase for cysteine-84-binding sites in cyanobacterial phycobiliproteins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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44 citing papers in PubMed, 123 citations in OpenAlex.
- Evolutionary insights into bilin biosynthesis: Functional characterization of pre-PcyA enzymes.Protein science : a publication of the Protein Society · 2026Article
- Improved Stability and Brightness Following Iterative Redesign of a De Novo Biliprotein.Biochemistry · 2026Article
- Description of a New Marine Cyanobacterium from the Cabo Verde Archipelago: Pigments Profile and Biotechnological Potential ofMarine drugs · 2026Article
- Assembly of allophycocyanin from individual subunits: involvement of apo-form in the formation of trimers.Photosynthesis research · 2025Article
- Crystallographic and biochemical analyses of a far-red allophycocyanin to address the mechanism of the super-red-shift.Photosynthesis research · 2024Article
- Optimization of Phycocyanobilin Synthesis inGenes · 2024Article
- Exploring the Origins and Evolution of Oxygenic and Anoxygenic Photosynthesis in Deeply Branched Cyanobacteriota.Molecular biology and evolution · 2024Article
- A Single-Site Mutation Tunes Fluorescence and Chromophorylation of an Orange Fluorescent Cyanobacteriochrome.Chembiochem : a European journal of chemical biology · 2023Article
- Zinc-Induced Fluorescence Turn-On in Native and Mutant Phycoerythrobilin-Binding Orange Fluorescent Proteins.Biochemistry · 2023Article
- Zinc-Induced Fluorescence Turn-on in Native and Mutant Phycoerythrobilin-Binding Orange Fluorescent Proteins.bioRxiv : the preprint server for biology · 2023Article
- A Single Site Mutation Tunes Fluorescence and Chromophorylation of an Orange Fluorescent Cyanobacteriochrome.bioRxiv : the preprint server for biology · 2023Article
- Absolute quantification of cellular levels of photosynthesis-related proteins in Synechocystis sp. PCC 6803.Photosynthesis research · 2023Article
- Core and rod structures of a thermophilic cyanobacterial light-harvesting phycobilisome.Nature communications · 2022Article
- The phycoerythrobilin isomerization activity of MpeV inFrontiers in microbiology · 2022Article
- Cloning ofGenes · 2019Article
- Interplay between differentially expressed enzymes contributes to light color acclimation in marineProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Metabolic engineering of Escherichia coli for efficient biosynthesis of fluorescent phycobiliprotein.Microbial cell factories · 2019Article
- CpeF is the bilin lyase that ligates the doubly linked phycoerythrobilin on β-phycoerythrin in the cyanobacteriumThe Journal of biological chemistry · 2019Article
- Biosynthesis of Fluorescent β Subunits of C-Phycocyanin fromMolecules (Basel, Switzerland) · 2018Article
- De novo synthetic biliprotein design, assembly and excitation energy transfer.Journal of the Royal Society, Interface · 2018Article
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Authors and funding
10 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Phycobilisomes, the light-harvesting complexes of cyanobacteria and red algae, contain two to four types of chromophores that are attached covalently to seven or more members of a family of homologous proteins, each carrying one to four binding sites. Chromophore binding to apoproteins is catalyzed by lyases, of which only few have been characterized in detail. The situation is complicated by nonenzymatic background binding to some apoproteins. Using a modular multiplasmidic expression-reconstitution assay in Escherichia coli with low background binding, phycobilin:cystein-84 biliprotein lyase (CpeS1) from Anabaena PCC7120, has been characterized as a nearly universal lyase for the cysteine-84-binding site that is conserved in all biliproteins. It catalyzes covalent attachment of phycocyanobilin to all allophycocyanin subunits and to cysteine-84 in the beta-subunits of C-phycocyanin and phycoerythrocyanin. Together with the known lyases, it can thereby account for chromophore binding to all binding sites of the phycobiliproteins of Anabaena PCC7120. Moreover, it catalyzes the attachment of phycoerythrobilin to cysteine-84 of both subunits of C-phycoerythrin. The only exceptions not served by CpeS1 among the cysteine-84 sites are the alpha-subunits from phycocyanin and phycoerythrocyanin, which, by sequence analyses, have been defined as members of a subclass that is served by the more specialized E/F type lyases.
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