Synthesis of glutathione a low-molecular-weight peptide thiol was thought to occur solely through the consecutive action of two physically separate enzymes, gamma-glutamylcysteine ligase and glutathione synthetase. But it has been identified that L. monocytogenes contains a novel multidomain protein (termed GshF) that carries out complete synthesis of glutathione. It is a 776 amino acid fusion protein and fusion occurs in 338 to 580 amino acids.It is coded by the gene Lmo 2770 in L. monocytogenes.
Thiol:disulfide redox metabolism (TDRM) is a central metabolic network in all living cells. In L.monocytogenes, we have identified 26 genes that belong thiol disulphide network. L. monocytogenes-Thiol: Disulphide Redox Metabolism database provides information on Thiol disulphide redox gene and gene products. This database also provides information about the Gene and Domain Annotation, Clustering, Structure Details. TDRM analysis gives detailed analysis of the similar cluster of these TDRM genes across bacterial species consisting 82 bacterial strains. With the help genome browser, user can view the TDRM genes on the genomic scale and analyze the same.
- Understanding TDRM genes on the genomic scale with reference to other GshF containing bacteria
- Finding the genes which have probable role in thiolomics in L. monocytogenes EGD-e
- Genetic context of the relevant genes in Listeria with other bacteria and their annotations