The structure of Synechococcus elongatus enolase reveals key aspects of phosphoenolpyruvate binding
- PMID: 35400670
- PMCID: PMC8996150
- DOI: 10.1107/S2053230X22003612
The structure of Synechococcus elongatus enolase reveals key aspects of phosphoenolpyruvate binding
Abstract
A structure-function characterization of Synechococcus elongatus enolase (SeEN) is presented, representing the first structural report on a cyanobacterial enolase. X-ray crystal structures of SeEN in its apoenzyme form and in complex with phosphoenolpyruvate are reported at 2.05 and 2.30 Å resolution, respectively. SeEN displays the typical fold of enolases, with a conformationally flexible loop that closes the active site upon substrate binding, assisted by two metal ions that stabilize the negatively charged groups. The enzyme exhibits a catalytic efficiency of 1.2 × 105 M-1 s-1 for the dehydration of 2-phospho-D-glycerate, which is comparable to the kinetic parameters of related enzymes. These results expand the understanding of the biophysical features of these enzymes, broadening the toolbox for metabolic engineering applications.
Keywords: Synechococcus elongatus; cyanobacteria; enolases; phosphoenolpyruvate.
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