Protein topology determines cysteine oxidation fate: the case of sulfenyl amide formation among protein families.

ABSTRACT: Cysteine residues have a rich chemistry and play a critical role in the catalytic activity of a plethora of enzymes. However, cysteines are susceptible to oxidation by Reactive Oxygen and Nitrogen Species, leading to a loss of their catalytic function. Therefore, cysteine oxidation is emerging as a relevant physiological regulatory mechanism. Formation of a cyclic sulfenyl amide residue at the active site of redox-regulated proteins has been proposed as a protection mechanism against irreversible oxidation as the sulfenyl amide intermediate has been identified in several proteins. However, how and why only some specific cysteine residues in particular proteins react to form this intermediate is still unknown. In the present work using in-silico based tools, we have identified a constrained

SUBMITTER: Defelipe LA 

PROVIDER: S-EPMC4351059 | biostudies-literature | 2015 Mar

REPOSITORIES: biostudies-literature