Glutamate optimizes enzymatic activity under high hydrostatic pressure in Desulfovibrio species: effects on the ubiquitous thioredoxin system

In piezophilic microorganisms, enzymes are optimized to perform under high hydrostatic pressure. The two major reported mechanisms responsible for such adaptation in bacterial species changes amino acids the protein structure, favoring their activity and stability high-pressure conditions, possible accumulation of micromolecular co-solutes cytoplasm. Recently, glutamate cytoplasm Desulfovibrio has been growth conditions. this study, analysis effect on enzymatic thioredoxin reductase/thioredoxin complex either a piezosensitive or microorganism confirms its role as protective co-solute. Analysis structures suggests an both presence pressure enzyme from strain. Indeed, large surface pockets could counterbalance overall compression that occurs at maintain activity. A lower isoelectric point greater dipolar moment than strain would allow compensate charged acid interact with partner.