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Literature summary for 4.4.1.32 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 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

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

Crystallization (Commentary)

Crystallization (Comment) Organism
structure of the heterodimer of CpcE/F at 1.89 A resolution. Both subunits are twisted, crescent-shaped alpha-solenoid structures. CpcE has 15 and CpcF 10 helices. The inner (concave) layer of CpcE (helices h2, 4, 6, 8, 10, 12, and 14) and the outer (convex) layer of CpcF (h16, 18, 20, 22, and 24) form a cavity into which the phycocyanobilin chromophore can be modeled Nostoc sp. PCC 7120 = FACHB-418

Organism

Organism UniProt Comment Textmining
Nostoc sp. PCC 7120 = FACHB-418 P07125 and P29985 P07125 i.e. subunit CpcE, P29985 i.e. subunit CpcF
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