作者: Axel DUCRET , Walter SIDLER , Gerhard FRANK , Herbert ZUBER
DOI: 10.1111/J.1432-1033.1994.TB18769.X
关键词: Phycoerythrocyanin 、 Biochemistry 、 Phycobiliprotein 、 Phycocyanobilin 、 Peptide sequence 、 Phycoerythrobilin 、 Biology 、 Porphyridium cruentum 、 Phycoerythrin 、 Phycocyanin
摘要: We present here the complete primary structure of R-phycocyanin-I alpha and beta subunits from red alga Porphyridium cruentum. The chain is composed 162 amino acid residues (18049 Da, calculated sequence, including chromophore) carries a phycocyanobilin pigment covalently linked to Cys84. contains 172 acids (19344Da, chromophores) at Cys82 phycoerythrobilin Cys153. A gamma-N-methyl asparagine residue was also characterised position 72 similar other phycobiliprotein subunits. cruentum shares high sequence identity with C-phycocyanins (69-83%), R-phycocyanins (66-70%) in less extent phycoerythrocyanins (57-65%) various sources. presented phylogenetic trees are based on comparison all sequences known so far confirm clear affiliation phycocyanin family. In spite their particular phycobilin pattern, they do not represent intermediate forms between phycoerythrin Phycoerythrocyanin, phycocyanin-related adapted green light harvesting, shown belong However, diverge phycocyanins different function it suggested that should be assigned separate group within