Literature summary for 4.4.1.30 extracted from

Shen, G.; Saunee, N.; Williams, S.; Gallo, E.; Schluchter, W.; Bryant, D.
Identification and characterization of a new class of bilin lyase: The cpcT gene encodes a bilin lyase responsible for attachment of phycocyanobilin to Cys-153 on the beta-subunit of phycocyanin in Synechococcus sp. PCC 7002 (2006), J. Biol. Chem., 281, 17768-17778.

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Organism

Organism	UniProt	Comment	Textmining
Synechococcus sp.	B1XI94	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
apo-[phycocyanin beta-subunit] + phycocyanobilin	-	Synechococcus sp.	[phycocyanin beta-subunit]-Cys153-phycocyanobilin	CpcT is a phycocyanobilin lyase that specifically attaches phycocyanobilin to Cys153 of the phycocyanin beta-subunit	?

Synonyms

Synonyms	Comment	Organism
cpcT	-	Synechococcus sp.

General Information

General Information	Comment	Organism
physiological function	cpcT null mutant contains 40% less phycocyanin than wild type and produces smaller phycobilisomes with red-shifted absorbance and fluorescence emission maxima. Phycocyanin from the cpcT mutant has an absorbance maximum at 634 nm compared with 626 nm for the wild-type. The phycocyanin beta-subunit from the cpcT mutant has slightly smaller apparent molecular weight on SDS-PAGE. No phycocyanobilin chromophore is bound to the peptide containing Cys153 derived from the phycocyanin beta-subunit of the cpcT mutant	Synechococcus sp.

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Release 2023.1 (January 2023)