Thioredoxin reductase: Selenotetrapeptide sequences with specificity for thioredoxin and glutathione systems

TRXR) chromosomal position 12q23.3-q24.1 (§, ‡) is a homodimeric selenocysteine-containing enzyme. Secys a selenocysteine residue is an essential TR isozyme component, located near the C-terminus region [cysteine (Cys)-497,Secys-498] of the intracellular, redox cellular environments center in the catalytically active enzyme site, Gly-499 is the actual C-terminal amino acid. In their N-terminal sequences Cys-59, Cys-64 links the thiol/disulfide oxidoreductase dependent pathway reductases from there to the flexible C-terminal part (Secys) of the other sub cellular subunit by which Selenocystine is efficiently reduced and induce RNR (Ribonucleotide reductase) for replication and repair, where Trx reductase (TR) or oxidized GSH (GSSG) reductase further supply electrons for RNR. The protein reversibly modulates specific signal transduction cascades, to regulate multiple downstream intracellular redox-sensitive proteins that links NADPH and thiol-dependent processes which catalyzes NADPH-dependent reduction in the presence of the redox protein-Trx and thioredoxin reductase (TR) maintain cysteine residues in numerous proteins in the reduced state. There are three TXNRD selenoproteins 5-prime end variants essential for mammals, one V3 (TXNRD1) encodes an N-terminal glutaredoxin (GRX) these variants code for thioredoxin glutathione reductases (TGR). V3 associates with and triggers formation of Filopodia (cytoplasmic filaments) can guide actin in migrating cells, the emerging protrusions of cell membrane restructuring involved is in 'deglutathionylation values" for mitochondrial and cytosolic thioredoxin reductase (TR) domains. Characterization of the TR native Thioredoxin and glutathione systems (TGR) suggests that the lifecycle of E. granulosus and Schistosoma mansoni a phylum of Platyhelmintha, involves the TXNRD1_v3 isoform containing a fused (Grx) glutaredoxin domain which is abolished by deglutathionylation' targeted to either mitochondria or the nucleus in the reduction of glutathionylated substrates, in leishmaniasis (disease) glutathione reductase system (TGR) is replaced by the trypanothione reductase (TcTR) system in mammalian cells, essential as these TR3 are significant as a recognized drug target of these (TcTR) human protozoan parasites. Cytosolic TR1, mitochondrial-TR3 and TrxR2 (locus 22q11.21) where TrxR1 and TrxR2 are consdered as the respective cytosolic and mitochondrial thioredoxin reductases, plus the thioredoxin glutathione reductases-TGR systems most likely can reduce (Trx) by fusion of the TR and an N-terminal glutaredoxin domains. As a pyridine nucleotide disulfide oxidoreductase of the oxidized GSH and GSSG (selenodiglutathione) reductase