Literature summary for 1.8.1.9 extracted from

Bauer, H.; Massey, V.; Arscott, L.D.; Schirmer, R.H.; Ballou, D.P.; Williams, C.H., Jr.
The mechanism of high Mr thioredoxin reductase from Drosophila melanogaster (2003), J. Biol. Chem., 278, 33020-33028.

Search for more literature for 1.8.1.9

Protein Variants

Protein Variants	Comment	Organism
C489S	mutant is incapable of reducing thioredoxin and can only be reduced to the 2-electron-state of enzyme	Drosophila melanogaster
C489S/C490S	mutant is incapable of reducing thioredoxin and can only be reduced to the 2-electron-state of enzyme	Drosophila melanogaster
C490S	mutant is incapable of reducing thioredoxin and can only be reduced to the 2-electron-state of enzyme	Drosophila melanogaster

Organism

Organism	UniProt	Comment	Textmining
Drosophila melanogaster	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
NADPH + thioredoxin disulfide	mechanism, Cys57 attacks Cys490 in the interchange reaction between the N-terminal dithiol and the C-terminal disulfide	Drosophila melanogaster	NADP+ + thioredoxin	-	?

Synonyms

Synonyms	Comment	Organism
DmTrxR-1	-	Drosophila melanogaster
thioredoxin reductase-1	-	Drosophila melanogaster

Cofactor

Cofactor	Comment	Organism	Structure
NADPH	-	Drosophila melanogaster

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)