Phycobiliprotein biosynthesis in cyanobacteria: structure and function of enzymes involved in post-translational modification.

Wendy M. Schluchter, Gaozhong Shen, Richard M. Alvey, Avijit Biswas, Nicolle A. Saunée, Shervonda R. Williams, Crystal A. Mille, Donald A. Bryant

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63 Scopus citations


Cyanobacterial phycobiliproteins are brilliantly colored due to the presence of covalently attached chromophores called bilins, linear tetrapyrroles derived from heme. For most phycobiliproteins, these post-translational modifications are catalyzed by enzymes called bilin lyases; these enzymes ensure that the appropriate bilins are attached to the correct cysteine residues with the proper stereochemistry on each phycobiliprotein subunit. Phycobiliproteins also contain a unique, post-translational modification, the methylation of a conserved asparagine (Asn) present at beta-72, which occurs on the beta-subunits of all phycobiliproteins. We have identified and characterized several new families of bilin lyases, which are responsible for attaching PCB to phycobiliproteins as well as the Asn methyl transferase for beta-subunits in Synechococcus sp. PCC 7002 and Synechocystis sp. PCC 6803. All of the enzymes responsible for synthesis of holo-phycobiliproteins are now known for this cyanobacterium, and a brief discussion of each enzyme family and its role in the biosynthesis of phycobiliproteins is presented here. In addition, the first structure of a bilin lyase has recently been solved (PDB ID: 3BDR). This structure shows that the bilin lyases are most similar to the lipocalin protein structural family, which also includes the bilin-binding protein found in some butterflies.

Original languageEnglish (US)
Pages (from-to)211-228
Number of pages18
JournalAdvances in experimental medicine and biology
StatePublished - 2010

All Science Journal Classification (ASJC) codes

  • General Biochemistry, Genetics and Molecular Biology


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