Journal article

The lid domain is important, but not essential, for catalysis ofEscherichia colipyruvate kinase

Elena Sugrue, David Coombes, David Wood, Tong Zhu, Katherine A Donovan, Renwick CJ Dobson

European Biophysics Journal | SPRINGER | Published : 2020

Abstract

Pyruvate kinase catalyses the final step of the glycolytic pathway in central energy metabolism. The monomeric structure comprises three domains: a catalytic TIM-barrel, a regulatory domain involved in allosteric activation, and a lid domain that encloses the substrates. The lid domain is thought to close over the TIM-barrel domain forming contacts with the substrates to promote catalysis and may be involved in stabilising the activated state when the allosteric activator is bound. However, it remains unknown whether the lid domain is essential for pyruvate kinase catalytic or regulatory function. To address this, we removed the lid domain of Escherichia coli pyruvate kinase type 1 (PKTIM+Re..

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Grants

Awarded by New Zealand Royal Society Marsden Fund


Awarded by US Army Research Office


Funding Acknowledgements

This work is supported by the New Zealand Royal Society Marsden Fund (contract UOC1013) and the US Army Research Office under contract/grant number W911NF-11-1-0481.