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J. Biol. Chem., Vol. 269, Issue 12, 8686-8694, 03, 1994
CD Fairchild and AN Glazer
Phycobiliproteins carry linear tetrapyrrole chromophores (bilins)
thioether-linked to specific cysteine residues. The process of bilin
attachment to apoprotein in vivo has been characterized for only one bilin
attachment site on one phycobiliprotein, that on the alpha subunit of
phycocyanin (alpha PC). In the cyanobacterium Synechococcus sp. PCC 7002,
the addition of phycocyanobilin to apo-alpha PC is catalyzed by the protein
products of the cpcE and cpcF genes. We have purified and further
characterized the recombinant CpcE and CpcF proteins. CpcE and CpcF form an
enzymatically active 1:1 complex (CpcEF), stable to size exclusion
chromatography. CpcEF causes a reduction in alpha PC fluorescence and
strongly affects its absorption spectrum but has no effect on the beta
subunit. The CpcEF bilin addition activity exhibits simple Michaelis-Menten
kinetics with respect to the apo-alpha PC and to bilin. CpcEF also
catalyzes the addition of phycoerythrobilin to apo-alpha PC;
phycoerythrobilin is thought to be on the biosynthetic pathway of
phycocyanobilin. CpcEF shows a preference for phycocyanobilin relative to
phycoerythrobilin, both in binding affinity and in the rate of catalysis,
sufficient to account for selective attachment of phycocyanobilin to
apo-alpha PC.
Oligomeric structure, enzyme kinetics, and substrate specificity of the phycocyanin alpha subunit phycocyanobilin lyase
Department of Molecular and Cell Biology, University of California, Berkeley 94720.
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