Alteration of the alpha helix region of cyanobacterial ribulose 1,5-bisphosphate carboxylase/oxygenase to reflect sequences found in high substrate specificity enzymes

Archives of Biochemistry and Biophysics
R T RamageF Robert Tabita

Abstract

The sequence at the alpha helix region of the eight-stranded beta/alpha barrel domain of the large subunit of Synechococcus sp. strain PCC 6301 ribulosebisphosphate carboxylase/oxygenase (rubisco) was altered by site-directed mutagenesis. Changes were made to match the corresponding residues in the rubisco large subunit of chromophytic and rhodophytic algae, which have considerably higher substrate specificity factors (ratio of the rate constants for the carboxylase and oxygenase reactions). A set of cumulative mutations of one to eight amino acid residues was prepared and examined and it was found that mutant enzymes which contained from one to five substitutions all exhibited substantial decreases in carboxylase activity. Mutant enzymes which contained from six to eight amino acid substitutions were inactive and failed to maintain their native quarternary structure. For enzymes which maintained their native structure, consecutive changes in the alpha helix 6 region yielded a progressive increase in the K(m) for ribulosebisphosphate, confirming the importance of this region in substrate binding. Despite these results, and previous studies which indicated the importance and potential of residues in the alpha helix 6 region to i...Continue Reading

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Citations

Sep 12, 2002·Annual Review of Plant Biology·Robert J Spreitzer, Michael E Salvucci
Oct 30, 2019·International Journal of Molecular Sciences·Yu Zhou, Spencer Whitney
Oct 16, 2008·Journal of the American Chemical Society·Babu Kannappan, Jill E Gready
Feb 26, 2008·Plant Physiology and Biochemistry : PPB·Inger Andersson, Anders Backlund

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