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Facilitated Substrate Channeling in a Self‐Assembled Trifunctional Enzyme Complex
Author(s) -
You Chun,
Myung Suwan,
Zhang Y.H. Percival
Publication year - 2012
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201202441
Subject(s) - aldolase a , triosephosphate isomerase , enzyme , cyan , fructose bisphosphate aldolase , chemistry , substrate (aquarium) , biochemistry , isomerase , biology , physics , ecology , optics
Three enzymes , triosephosphate isomerase (orange in picture), aldolase (cyan), and fructose 1,6‐bisphosphatase (purple), which contained dockerins (red), self‐assembled into a static trifunctional enzyme complex through interaction with a mini‐scaffoldin protein consisting of three different cohesins (green). The synthetic enzyme complex exhibited an enhanced reaction rate compared to the noncomplexed three‐enzyme mixture at the same enzyme concentration.