The principal mechanism of reducing sulfur into organic compounds is via the synthesis of l-
cysteine. Cysteine is used for protein and glutathione synthesis, as well as being the primary …

Trichomonas vaginalis is an early divergent eukaryote with many unusual biochemical
features. It is an anaerobic protozoan parasite of humans that is thought to rely heavily on …

In most bacteria, inorganic sulfur is assimilated into cysteine, which provides sulfur for
methionine biosynthesis via transsulfurylation. Here, cysteine is transferred to the terminal …

Sulfur is necessary for the synthesis of cysteine. Microorganisms can use sulfate, thiosulfate
or sulfonates as sole sulfur sources. These compounds are taken up by specific transporters …

Most Neisseria strains are able to grow with sulphate as a unique source of sulphur.
Nevertheless, a cysteine requirement was present in a few strains of N. meningitidis and in …

Antibiotics are the cornerstone of modern medicine and agriculture, and rising antibiotic
resistance is one the biggest threats to global health and food security. Identifying new and …

Cysteine is an essential requirement in living organisms. However, due to its reactive thiol
side chain, elevated levels of intracellular cysteine can be toxic and therefore need to be …

Serine acetyltransferase (SAT) catalyzes the first step in the two-step pathway to synthesize l-
cysteine in bacteria and plants. SAT synthesizes O-acetylserine from substrates l-serine and …

CysK (O-acetylserine sulfhydrylase) is a pyridoxal-5′ phosphate-dependent enzyme which
catalyzes the second step of the de novo cysteine biosynthesis pathway by converting O …

In the enteric bacteria Escherichia coli and Salmonella enterica, sulfate is reduced to sulfide
and assimilated into the amino acid cysteine; in turn, cysteine provides the sulfur atom for …