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Literature summary for 1.8.1.9 extracted from

  • Wang, P.; Wu, Y.; Li, X.; Ma, X.; Zhong, L.
    Thioredoxin and thioredoxin reductase control tissue factor activity by thiol redox-dependent mechanism (2013), J. Biol. Chem., 288, 3346-3358 .
No PubMed abstract available
Search for more literature for 1.8.1.9

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
 Homo sapiens 5829
-

Organism

Organism UniProt Comment Textmining
Homo sapiens Q16881
-
-

Source Tissue

Source Tissue Comment Organism Textmining
blood plasma
-
 Homo sapiens
-
serum
-
 Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
reduced tissue factor + NADP+
-
 Homo sapiens tissue factor + NADPH + H+
-
 r
tissue factor + NADPH + H+
-
 Homo sapiens reduced tissue factor + NADP+
-
 r

Synonyms

Synonyms Comment Organism
Trx1
-
 Homo sapiens
Txnrd1
-
 Homo sapiens

General Information

General Information Comment Organism
physiological function Trx1 shows reversible association with tissue factor in human serum and plasma samples. The association is dependent on Trx1 residue Cys73 that bridges tissue factor residue Cys209 via a disulfide bond. Trx1 Cys73 is absolutely required for Trx1 to interfere with factor FVIIa binding to purified and cell-surface tissue factor, consequently suppressing tissue factor-dependent procoagulant activity and proteinase-activated receptor-2 activation. Trx1/TrxR plays an important role in sensing the alterations of NADPH/NADP+ states and transducing this redox-sensitive signal into changes in tissue factor activity. With NADPH, Trx1/TrxR facilitates the reduction of tissue factor, causing a decrease in tissue factor activity, with NADP+, Trx1/TrxR promotes the oxidation of tissue factor, leading to an increase in its activity Homo sapiens