ArticlePlant, cell & environment2025
The Highly Conserved Cys95 Residue of Fructose-1,6-Bisphosphatase 1 Mediates the pH-Driven Structure and Activity of the Enzyme and Photosynthesis.
Article in Plant, cell & environment, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
In Arabidopsis, exposure to microbial volatile compounds promotes thiol reduction of the Cys95 residue of the photosynthetic enzyme fructose-1,6-bisphosphatase (cFBP1). Although highly conserved in plants, the Cys95 function still remains unknown. We characterised recombinant wild-type (WT) cFBP1 and a variant (C95S) in which the Cys95 residue was replaced by serine. Furthermore, we characterised cFBP1-lacking cfbp1 transgenic plants expressing WT or C95S cFBP1. Cys95 replacement by serine reduced cFBP1 activity and its Mg
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