The tripeptide glutathione is found in all eukaryotic cells, and due to the
compartmentalization of biochemical processes, its synthesis takes place exclusively in the …

Epidemiological studies established that elevated homocysteine, an important intermediate
in folate, vitamin B12, and one carbon metabolism, is associated with poor health, including …

Electron deficient, bivalent sulfur atoms have two areas of positive electrostatic potential, a
consequence of the low-lying σ* orbitals of the C–S bond that are available for interaction …

Cysteine is the most intrinsically nucleophilic amino acid in proteins, where its reactivity is
tuned to perform diverse biochemical functions. The absence of a consensus sequence that …

▪ Abstract This review describes the three mammalian glutathione transferase (GST)
families, namely cytosolic, mitochondrial, and microsomal GST, the latter now designated …

BACKGROUND: The cytosolic glutathione transferases (GSTs) comprise a super family of
proteins that can be categorized into multiple classes with a mixture of highly specific and …

The glutathione transferases (GSTs) are one of the most important families of detoxifying
enzymes in nature. The classic activity of the GSTs is conjugation of compounds with …

Most cells contain high levels of glutathione and multiple glutaredoxins, which utilize the
reducing power of glutathione to catalyze disulfide reductions in the presence of NADPH …

Thioredoxins are ubiquitous antioxidant enzymes that play important roles in many health-
related cellular processes. As such, the fundamental knowledge of how these enzymes work …

In the last decade the tumultuous development of “omics” greatly improved our ability to
understand protein structure, function and evolution, and to define their roles and networks …