The assembly of RuBisCO and CA on DNA scaffold provides a platform for further study on the spatial control of RuBisCO and associating enzymes.Ĭarbonic anhydrase II Carboxysome DNA scaffold Modular adaptor RuBisCO.Ĭopyright © 2019 Elsevier Ltd. In line with the recent study, our results suggest that the proximity in the interenzyme distance of RuBisCO and CA is not the crucial determinant for the enhanced RuBisCO activity in carboxysome. Although the natural carboxysome assembly is believed to enhance the RuBisCO activity, the co-assembly of RuBisCO and CA reduced the RuBisCO activity, suggesting that the preferential CO 2 dehydration by CA reduced the RuBisCO reaction rate. To mimic the environment of the natural microcompartment in cyanobacterial carboxysome that encapsulate the second enzyme carbonic anhydrase (CA) with RuBisCO, RuBisCO was next co-assembled with CA on the DNA scaffold. The enzyme assembly was characterized by atomic force microscopy and RuBisCO assembled on the DNA scaffold showed avid enzymatic activity with retaining its parent carboxylase function. In this study, a RuBisCO dimer from Rhodospirillum rubrum was assembled on a DNA scaffold using a dimeric DNA binding protein as an adaptor.
Download for offline reading, highlight, bookmark or take notes while you read SCAFFOLDING - THE HANDBOOK FOR ESTIMATING and PRODUCT KNOWLEDGE. Read this book using Google Play Books app on your PC, android, iOS devices. Despite of the important function in the global carbon cycle, RuBisCO suffers from a slow reaction rate and a competing reaction with O 2 which draw attentions to improve the enzyme efficiency. SCAFFOLDING - THE HANDBOOK FOR ESTIMATING and PRODUCT KNOWLEDGE - Ebook written by Michael 'Terry' Marks. Ribulose-1,5-biphosphate carboxylase/oxygenase (RuBisCO), an enzyme in the Calvin-Benson-Bassham cycle of photosynthesis, catalyzes the first step of CO 2 fixation in plants, algae, and photosynthetic bacteria.