Selective chemical modification of human liver aldehyde dehydrogenases E1 and E2 by iodoacetamide.

Involvement of Serine 74 in the Enzyme-Coenzyme Interaction of Rat Liver Mitochondrial Aldehyde Dehydrogenase

“…Even before the primary structures of aldehyde dehydrogenases were known, it was observed that thiol-directed cysteine reagents would cause the inactivation of the enzyme (Hempel & Pietruszko, 1981). It was postulated that the enzyme oxidized aldehydes in a manner analogous to that of glyceraldehyde-3-phoshphate dehydrogenase (Feldman & Weiner, 1972).…”

The ligand unwrapping/rewrapping pathway that exchanges metals in S-acetylated, hexacoordinate N2S2O2complexes

“…[9][10][11][12][13] The reactivity of cysteinyl sulfur in proteins with acetylating agents, such as iodoacetamide, AA, and iodoacetate, Ac, has found application for cysteine protection and as an analytical tool for protein sequencing/mass spectrometry experiments. [14][15][16][17][18][19] The latter is used to monitor the increased mass of the cysteine residues and of the protein as a whole, and in the former, to prevent the formation of disulde bonds in the tertiary structure of proteins. 20 While thioethers are typically poorer metal-binding ligands, the carboxylate or carboxamido terminus is a potential donor, leading to the possibility of coordination number expansion.…”

Structure of mitochondrial aldehyde dehydrogenase: the genetic component of ethanol aversion

“…The chemical and kinetic mechanisms of the ALDH1 and ALDH2 have been extensively investigated [3]. The participation of two amino acid residues, Cys302 and Glu268, in the catalytic mechanism was suggested by chemical modification studies [8][9][10]. More recent mutagenesis studies strongly support the idea that Cys302 functions as the active-site nucleophile and that Glu268 functions as the general base necessary for both the hemiacetal formation and deacylation [11,12].…”