Literature summary for 4.4.1.31 extracted from

Zhao, C.; Hoeppner, A.; Xu, Q.Z.; Gaertner, W.; Scheer, H.; Zhou, M.; Zhao, K.H.
Structures and enzymatic mechanisms of phycobiliprotein lyases CpcE/F and PecE/F (2017), Proc. Natl. Acad. Sci. USA, 114, 13170-13175 .

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Cloned(Commentary)

Cloned (Comment)	Organism
-	Nostoc sp. PCC 7120 = FACHB-418

Crystallization (Commentary)

Crystallization (Comment)	Organism
modeling of structure of the heterodimer, using the CpcE/F structure as template, cf. EC 34.4.1.32. A H87C88 motif critical for the isomerase activity of PecE/F is located at the loop between h20 and h21. The nucleophilic addition of Cys-88 to C10 of phycocyanobilin may induce the isomerization of phycocyanobilin into phycoviolobilin	Nostoc sp. PCC 7120 = FACHB-418

Organism

Organism	UniProt	Comment	Textmining
Nostoc sp. PCC 7120 = FACHB-418	P35791 and P35798	P35791 i.e. subunit PecE, P35798 i.e. subunit PecF	-

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Release 2023.1 (January 2023)