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Literature summary extracted from

  • Tooley, A.J.; Cai, Y.A.; Glazer, A.N.
    Biosynthesis of a fluorescent cyanobacterial C-phycocyanin holo-a subunit in a heterologous host (2001), Proc. Natl. Acad. Sci. USA, 98, 10560-10565.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
4.4.1.32 synthesis reconstitution of the entire pathway for the synthesis of a fluorescent holophycobiliprotein subunit from Synechocystis sp. PCC6803 in Escherichia coli. Heme oxygenase 1 and 3Z-phycocyanobilin:ferredoxin oxidoreductase are expressed from one plasmid. Genes for the apoprotein C-phycocyanin a subunit, cpcA and the heterodimeric lyase subunit cpcE and cpcF that catalyze chromophore attachment are expressed from a second plasmid. Upon induction, recombinant Escherichia coli uses the cellular pool of heme to produce holo-CpcA with spectroscopic properties qualitatively and quantitatively similar to those of the same protein produced endogenously in cyanobacteria. About a third of the apo-CpcA is converted to holo-CpcA Synechocystis sp.

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.3.7.5 cloned into plasmid containing the sequence coding for HO1 protein Synechocystis sp.

Organism

EC Number Organism UniProt Comment Textmining
1.3.7.5 Synechocystis sp.
-
 cyanobacterium, strain PCC6803
-
4.4.1.32 Synechocystis sp. P72652 subunit CpcF
-
4.4.1.32 Synechocystis sp. P73638 subunit CpcE
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.7.5 (3Z)-phycocyanobilin + oxidized ferredoxin
-
 Synechocystis sp. biliverdin IXa + reduced ferredoxin
-
 ?