EC 1 - Oxidoreductases
EC 1.8 - Acting on a sulfur group of donors
EC 1.8.1 - With NAD+ or NADP+ as acceptor
EC 1.8.1.9 - Thioredoxin-disulfide reductase
IntEnz view
ENZYME view
IntEnz Enzyme Nomenclature
EC 1.8.1.9
Names
Accepted name:
thioredoxin-disulfide reductase
Other
names:
NADP—thioredoxin reductase
NADPH—thioredoxin reductase
NADPH2:oxidized thioredoxin oxidoreductase
thioredoxin reductase (NADPH)
NADPH—thioredoxin reductase
NADPH2:oxidized thioredoxin oxidoreductase
thioredoxin reductase (NADPH)
Systematic name:
thioredoxin:NADP+ oxidoreductase
Reaction
-
20345 [IUBMB]+[thioredoxin]-dithiolGENERIC:10698Is ROOT: no
ROOT compound: GENERIC:10697Number of residues: 2NADP+Name origin: UniProt - CHECKED (C)Formula: C21H25N7O17P3
Charge: -3ChEBI compound status: CHECKED (C)=+[thioredoxin]-disulfideGENERIC:10700Is ROOT: no
ROOT compound: GENERIC:10697Number of residues: 1+H+Name origin: UniProt - CHECKED (C)Formula: H
Charge: 1ChEBI compound status: CHECKED (C)
Comments:
A flavoprotein (FAD).
Links to other databases
Enzymes and pathways:
NC-IUBMB
,
BRENDA
,
ExplorEnz
,
ENZYME@ExPASy
,
KEGG
,
MetaCyc
,
NIST 74
,
UniPathway
Protein domains and families:
PROSITE:PDOC00496
Gene Ontology:
GO:0004791
CAS Registry Number:
9074-14-0
References
-
Enzymatic synthesis of deoxyribonucleotides. V. Purification and properties of thioredoxin reductase from Escherichia coli B.J. Biol. Chem. 239 : 3445-3452 (1964).
-
Purification and characterization of yeast thioredoxin reductase.Biochim. Biophys. Acta 327 : 274-281 (1973). [PMID: 4149839]
-
Physiological functions of thioredoxin and thioredoxin reductase.Eur. J. Biochem. 267 : 6102-6109 (2000). [PMID: 11012661]
[EC 1.8.1.9 created 1972 as EC 1.6.4.5, transferred 2002 to EC 1.8.1.9]