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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

Its defined molecular structure makes it useful for examining peptide behavior and intracellular signaling mechanisms under controlled research conditions

doi: 10.3390/md19060293 98

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Mitochondrial BCL-2 inhibits AMBRA1-induced autophagy

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