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Full-Text Articles in Life Sciences
Cpet Is The Phycoerythrobilin Lyase For Cys-165 On Beta-Phycoerythrin From Fremyella Diplosiphon And The Chaperone-Like Protein Cpez Greatly Improves Its Activity., Wendy M. Schluchter, A. A. Nguyen, K. L. Joseph, A. N. Bussell, S. Pokhrel, A. J. Karty, M. C. Kronfel, D. M. Kehoe
Cpet Is The Phycoerythrobilin Lyase For Cys-165 On Beta-Phycoerythrin From Fremyella Diplosiphon And The Chaperone-Like Protein Cpez Greatly Improves Its Activity., Wendy M. Schluchter, A. A. Nguyen, K. L. Joseph, A. N. Bussell, S. Pokhrel, A. J. Karty, M. C. Kronfel, D. M. Kehoe
Biological Sciences Faculty Publications
Bilin lyases are enzymes which ligate linear tetrapyrrole chromophores to specific cysteine residues on light harvesting proteins present in cyanobacteria and red algae. The lyases responsible for chromophorylating the light harvesting protein phycoerythrin (PE) have not been fully characterized. In this study, we explore the role of CpeT, a putative bilin lyase, in the biosynthesis of PE in the cyanobacterium Fremyella diplosiphon. Recombinant protein studies show that CpeT alone can bind phycoerythrobilin (PEB), but CpeZ, a chaperone-like protein, is needed in order to correctly and efficiently attach PEB to the beta-subunit of PE. MS analyses of the recombinant beta-subunit of …