Literature summary for 4.4.1.31 extracted from

Zhao, K.H.; Deng, M.G.; Zheng, M.; Zhou, M.; Parbel, A.; Storf, M.; Meyer, M.; Strohmann, B.; Scheer, H.
Novel activity of a phycobiliprotein lyase: both the attachment of phycocyanobilin and the isomerization to phycoviolobilin are catalyzed by the proteins PecE and PecF encoded by the phycoerythrocyanin operon (2000), FEBS Lett., 469, 9-13.

Search for more literature for 4.4.1.31

Cloned(Commentary)

Cloned (Comment)	Organism
overexpressed in Escherichia coli	Mastigocladus laminosus

Organism

Organism	UniProt	Comment	Textmining
Mastigocladus laminosus	P29729 and P29730	P29729: bilin biosynthesis protein PecE, P29730: bilin biosynthesis protein PecF	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
apo-[phycoerythrocyanin alpha-subunit] + (2R,3E)-phycocyanobilin	PecE and PecF jointly catalyze not only the addition of phycocyanobilin to PecA, but also its isomerization to the native phycoviolobilin chromophore	Mastigocladus laminosus	[phycoerythrocyanin alpha-subunit]-Cys84-phycoviolobilin	-	?

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)