Literature summary for 4.4.1.32 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.

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Application

Application	Comment	Organism
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.

Organism

Organism	UniProt	Comment	Textmining
Synechocystis sp.	P72652	subunit CpcF	-
Synechocystis sp.	P73638	subunit CpcE	-

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Release 2023.1 (January 2023)