Function and Biology Details
Reaction catalysed:
Trypanothione + NADP(+) = trypanothione disulfide + NADPH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Trypanothione reductase
- FAD/NAD(P)-binding domain superfamily
- FAD/NAD-linked reductase, dimerisation domain superfamily
- Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain
- Pyridine nucleotide-disulphide oxidoreductase, class I, active site
- Glutathione reductase/thioredoxin reductase-like
- FAD/NAD(P)-binding domain
- Pyridine nucleotide-disulphide oxidoreductase, class I
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
Trypanothione reductase (preferred)
PDBe Complex ID:
PDB-CPX-107319 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Trypanothione reductase
Molecule details ›
Chain: A
Length: 489 amino acids
Theoretical weight: 52.87 KDa
Source organism: Leishmania infantum
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 489 amino acids
Theoretical weight: 52.87 KDa
Source organism: Leishmania infantum
Expression system: Escherichia coli
UniProt:
- Canonical:
A4HSF7 (Residues: 1-488; Coverage: 99%)
Sequence domains:
