Structural basis for evolution of product diversity in soybean glutathione biosynthesis.

The Plant Cell
Ashley GalantJoseph M Jez

Abstract

The redox active peptide glutathione is ubiquitous in nature, but some plants also synthesize glutathione analogs in response to environmental stresses. To understand the evolution of chemical diversity in the closely related enzymes homoglutathione synthetase (hGS) and glutathione synthetase (GS), we determined the structures of soybean (Glycine max) hGS in three states: apoenzyme, bound to gamma-glutamylcysteine (gammaEC), and with hGSH, ADP, and a sulfate ion bound in the active site. Domain movements and rearrangement of active site loops change the structure from an open active site form (apoenzyme and gammaEC complex) to a closed active site form (hGSH*ADP*SO(4)(2-) complex). The structure of hGS shows that two amino acid differences in an active site loop provide extra space to accommodate the longer beta-Ala moiety of hGSH in comparison to the glycinyl group of glutathione. Mutation of either Leu-487 or Pro-488 to an Ala improves catalytic efficiency using Gly, but a double mutation (L487A/P488A) is required to convert the substrate preference of hGS from beta-Ala to Gly. These structures, combined with site-directed mutagenesis, reveal the molecular changes that define the substrate preference of hGS, explain the produ...Continue Reading

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Citations

Apr 7, 2010·Amino Acids·Hankuil YiJoseph M Jez
Nov 4, 2011·International Journal of Phytoremediation·Joseph M Jez
Dec 24, 2013·Plant Physiology and Biochemistry : PPB·Mary L PreussJoseph M Jez
May 23, 2012·Natural Product Reports·Geoffrey E Ravilious, Joseph M Jez
Mar 2, 2016·Chemico-biological Interactions·Joseph M JezJonathan Herrmann
Jun 25, 2013·Plant Physiology and Biochemistry : PPB·Sarvajeet Singh GillNarendra Tuteja
Mar 3, 2019·Journal of Experimental Botany·Joseph M Jez
Mar 12, 2010·The Journal of Biological Chemistry·Ekaterina I Biterova, Joseph J Barycki
Aug 14, 2021·Nature Chemical Biology·Itai SharonT Martin Schmeing

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