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Chemical Compound Review

AC1O5ZM2     3-[2-[(E)-[(5E)-3-(2- carboxyethyl)-5...

Synonyms: 18097-67-1
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Disease relevance of Phycoerythrobilin


High impact information on Phycoerythrobilin


Biological context of Phycoerythrobilin

  • Values for the rate of energy transfer k(HT) (0.47 ns(-1)) and the angle 2theta between the transition dipole moment directions (2theta = 45 +/- 5 degrees) were determined from an analysis of the concentration dependence of the anisotropy at five different PEB/Cph1 stoichiometries [10].
  • These open reading frames may encode a lyase specific for the attachment of phycoerythrobilin to alpha RPCII [11].
  • The deduced amino acid sequences were compared to class II phycoerythrin from Synechococcus sp. strain WH8020 and found to share 92% identity, yet the proteins differ in the bilin isomer (phycoerythrobilin versus phycourobilin) bound to two of the six chromophore attachment sites [12].

Anatomical context of Phycoerythrobilin


Associations of Phycoerythrobilin with other chemical compounds


Gene context of Phycoerythrobilin

  • The spectroscopic and chemical properties of these peptides were compared with those of P. cruentum B-phycoerythrin peptide alpha-1 PEB, Cys(PEB)-Tyr-Arg, in which the bilin is A-ring linked (Schoenleber, R. W., Leung, S.-L., Lundell, D. J., Glazer, A. N., and Rapoport, H. (1983) J. Am. Chem. Soc. 105, 4072-4076) [9].
  • In contrast, the phycoerythrobilin on peptide beta-3 is attached through two thioether linkages to cysteinyl residues 10 residues apart [18].
  • Structures and apoprotein linkages of phycoerythrobilin and phycocyanobilin [19].

Analytical, diagnostic and therapeutic context of Phycoerythrobilin

  • Secondary ion mass spectrometry showed the bilins in these peptides and in alpha-1 PEB to have the same mass [9].
  • Sequential titration of apo Cph1 with PEB alone to full occupancy did not affect the intensity decay but led to a substantial increase in depolarization [10].
  • Results indicate that fluorescent proteins formed by attachment of phycoerythrobilin to expressed apo-subunits of phycobiliproteins can be used as fluorescent probes for analysis of cells by microscopy and flow cytometry [13].


  1. Insights into Phycoerythrobilin Biosynthesis Point toward Metabolic Channeling. Dammeyer, T., Frankenberg-Dinkel, N. J. Biol. Chem. (2006) [Pubmed]
  2. Mechanism of Cph1 phytochrome assembly from stopped-flow kinetics and circular dichroism. Borucki, B., Otto, H., Rottwinkel, G., Hughes, J., Heyn, M.P., Lamparter, T. Biochemistry (2003) [Pubmed]
  3. Metabolic engineering to produce phytochromes with phytochromobilin, phycocyanobilin, or phycoerythrobilin chromophore in Escherichia coli. Mukougawa, K., Kanamoto, H., Kobayashi, T., Yokota, A., Kohchi, T. FEBS Lett. (2006) [Pubmed]
  4. Chromatic adaptation in marine Synechococcus strains. Palenik, B. Appl. Environ. Microbiol. (2001) [Pubmed]
  5. Lesions in phycoerythrin chromophore biosynthesis in Fremyella diplosiphon reveal coordinated light regulation of apoprotein and pigment biosynthetic enzyme gene expression. Alvey, R.M., Karty, J.A., Roos, E., Reilly, J.P., Kehoe, D.M. Plant Cell (2003) [Pubmed]
  6. Oligomeric structure, enzyme kinetics, and substrate specificity of the phycocyanin alpha subunit phycocyanobilin lyase. Fairchild, C.D., Glazer, A.N. J. Biol. Chem. (1994) [Pubmed]
  7. Phytochrome assembly. Defining chromophore structural requirements for covalent attachment and photoreversibility. Li, L., Lagarias, J.C. J. Biol. Chem. (1992) [Pubmed]
  8. In vitro attachment of bilins to apophycocyanin. I. Specific covalent adduct formation at cysteinyl residues involved in phycocyanobilin binding in C-phycocyanin. Arciero, D.M., Bryant, D.A., Glazer, A.N. J. Biol. Chem. (1988) [Pubmed]
  9. Phycobiliprotein-bilin linkage diversity. II. Structural studies on A- and D-ring-linked phycoerythrobilins. Klotz, A.V., Glazer, A.N., Bishop, J.E., Nagy, J.O., Rapoport, H. J. Biol. Chem. (1986) [Pubmed]
  10. Dimerization and inter-chromophore distance of Cph1 phytochrome from Synechocystis, as monitored by fluorescence homo and hetero energy transfer. Otto, H., Lamparter, T., Borucki, B., Hughes, J., Heyn, M.P. Biochemistry (2003) [Pubmed]
  11. Genes of the R-phycocyanin II locus of marine Synechococcus spp., and comparison of protein-chromophore interactions in phycocyanins differing in bilin composition. de Lorimier, R., Wilbanks, S.M., Glazer, A.N. Plant Mol. Biol. (1993) [Pubmed]
  12. Sequence comparison of two highly homologous phycoerythrins differing in bilin composition. de Lorimier, R., Chen, C.C., Glazer, A.N. Plant Mol. Biol. (1992) [Pubmed]
  13. Formation of fluorescent proteins by the attachment of phycoerythrobilin to R-phycoerythrin alpha and beta apo-subunits. Isailovic, D., Sultana, I., Phillips, G.J., Yeung, E.S. Anal. Biochem. (2006) [Pubmed]
  14. Defensive ink pigment processing and secretion in Aplysia californica: concentration and storage of phycoerythrobilin in the ink gland. Prince, J., Nolen, T.G., Coelho, L. J. Exp. Biol. (1998) [Pubmed]
  15. Characterization of R-phycocyanin. Chromophore content of R-phycocyanin and C-phycoerythrin. Glazer, A.N., Hixson, C.S. J. Biol. Chem. (1975) [Pubmed]
  16. Isolation and characterization of R-phycoerythrin subunits and enzymatic digests. Isailovic, D., Li, H.W., Yeung, E.S. Journal of chromatography. A. (2004) [Pubmed]
  17. Mediation of ultrafast light-harvesting by a central dimer in phycoerythrin 545 studied by transient absorption and global analysis. Doust, A.B., van Stokkum, I.H., Larsen, D.S., Wilk, K.E., Curmi, P.M., van Grondelle, R., Scholes, G.D. The journal of physical chemistry. B, Condensed matter, materials, surfaces, interfaces & biophysical. (2005) [Pubmed]
  18. Bilin attachment sites in the alpha and beta subunits of B-phycoerythrin. Amino acid sequence studies. Lundell, D.J., Glazer, A.N., DeLange, R.J., Brown, D.M. J. Biol. Chem. (1984) [Pubmed]
  19. Structures and apoprotein linkages of phycoerythrobilin and phycocyanobilin. Killilea, S.D., O'Carra, P., Murphy, R.F. Biochem. J. (1980) [Pubmed]
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