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Literature summary for 1.8.1.9 extracted from

  • Liao, X.; Yang, F.; Li, H.; So, P.K.; Yao, Z.; Xia, W.; Sun, H.
    Targeting the thioredoxin reductase-thioredoxin system from Staphylococcus aureus by silver ions (2017), Inorg. Chem., 56, 14823-14830 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli BL21 Staphylococcus aureus

Inhibitors

Inhibitors Comment Organism Structure
Ag+ silver ions bind to the active sites of thioredoxin reductase with dissociation constants of 0.0014 mM and stoichiometries of 1 Ag+ ion per protein Staphylococcus aureus

Organism

Organism UniProt Comment Textmining
Staphylococcus aureus
-
-
-
Staphylococcus aureus Newman
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Staphylococcus aureus

Synonyms

Synonyms Comment Organism
TrxR
-
Staphylococcus aureus

General Information

General Information Comment Organism
drug target drug-resistant Staphylococcus aureus, especially methicillin-resistant (MRSA) and vancomycin-resistant Staphylococcus aureus (VRSA), pose a great threat to human health globally. The Trx system in GSH-deficient pathogens is a viable antibacterial drug target Staphylococcus aureus
physiological function the thioredoxin system, which is composed of NADPH, thioredoxin reductase (TrxR), and thioredoxin (Trx), is one of the major disulfide reductase systems used by bacteria against oxidative stress. This reductase system is crucial for the survival of the pathogenic bacterium Staphylococcus aureus, which lacks a natural glutathione/glutaredoxin (Grx) system Staphylococcus aureus