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The complete absence of dimerization in C396S suggests that Cys396 may be involved in an inter-molecular disulfide bond that results in the formation of an oligomeric structure that combines GSAAT with other enzymes, factors or molecular chaperones involved in ALA formation, such as GluTR, GBP ( The purified UT recombinant GSAAT variants were not entirely reduced, and additional reducing power enhanced their enzyme activities