Functional analysis of conserved histidines in ADP-glucose pyrophosphorylase from Escherichia coli.

Abstract

Two absolutely conserved histidines and a third highly conserved histidine are noted in 11 bacterial and plant ADP-glucose pyrophosphorylases. These histidines were individually mutagenized in the E. coli enzyme to glutamine in order to determine their function. Glutamine mutations at residues 143 and 156 produced functional enzymes in cell extracts with… (More)

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@article{Hill1998FunctionalAO, title={Functional analysis of conserved histidines in ADP-glucose pyrophosphorylase from Escherichia coli.}, author={Meredith A Hill and Jochen Preiss}, journal={Biochemical and biophysical research communications}, year={1998}, volume={244 2}, pages={573-7} }