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Literature summary extracted from

  • Cheng, Z.; Arscott, L.D.; Ballou, D.P.; Williams, C.H.
    The relationship of the redox potentials of thioredoxin and thioredoxin reductase from Drosophila melanogaster to the enzymatic mechanism: reduced thioredoxin is the reductant of glutathione in Drosophila (2007), Biochemistry, 46, 7875-7885.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.8.1.9 thioredoxin disulfide + NADPH + H+ Drosophila melanogaster DmTrxR catalyzes the reversible transfer of reducing equivalents from NADPH to DmTrx-2. This process is consistent with the corresponding redox potentials and is essential for GSSG/GSH cycling in Drosophila melanogaster, which is deficient in glutathione reductase thioredoxin + NADP+
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.8.1.9 Drosophila melanogaster
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.1.9 thioredoxin disulfide + NADPH + H+ DmTrxR catalyzes the reversible transfer of reducing equivalents from NADPH to DmTrx-2. This process is consistent with the corresponding redox potentials and is essential for GSSG/GSH cycling in Drosophila melanogaster, which is deficient in glutathione reductase Drosophila melanogaster thioredoxin + NADP+
-
 r
1.8.1.9 thioredoxin disulfide + NADPH + H+ DmTrxR catalyzes the reversible transfer of reducing equivalents from NADPH to DmTrx-2 Drosophila melanogaster thioredoxin + NADP+
-
 r

Synonyms

EC Number Synonyms Comment Organism
1.8.1.9 DmTrxR
-
 Drosophila melanogaster

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.1.9 NADPH
-
 Drosophila melanogaster