Literature summary for 4.4.1.29 extracted from

Shen, G.; Schluchter, W.; Bryant, D.
Biogenesis of phycobiliproteins: I. cpcS-I and cpcU mutants of the cyanobacterium Synechococcus sp. PCC 7002 define a heterodimeric phyococyanobilin lyase specific for beta-phycocyanin and allophycocyanin subunits (2008), J. Biol. Chem., 283, 7503-7512.

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Organism

Organism	UniProt	Comment	Textmining
Synechococcus sp.	A8HTM2	subunit CpcS1	-

General Information

General Information	Comment	Organism
physiological function	sSingle and double mutant strains for lyase subunits cpcSI and cpcU exhibit slower growth rates, reduced apo-phycobiliprotein levels, and impaired assembly of phycobilisomes. A cpcSI cpcU cpcT triple mutant is nearly devoid of apo-phycobiliprotein. The cpcSI and cpcU mutants produce an altered form of the phycocyanin beta-subunit, which has a mass about 588 Da smaller than the wild-type protein. The modified phycobilisomes from the cpcsI, cpcU, and cpcSIcpcU mutant strains carry a phycocyanobilin chromophore at Cys153 of CpcB but not at Cys82. Both CpcSI and CpcU are required for covalent attachment of phycocyanobilin to Cys82 of the phycocyanin subunit	Synechococcus sp.

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Release 2023.1 (January 2023)