Pathways & interactions
Pyridine nucleotide-disulphide oxidoreductase, class I (IPR001100)
Short name: Pyr_nuc-diS_OxRdtase
- Pyridine nucleotide-disulphide oxidoreductase, class I (IPR001100)
- Dihydrolipoamide dehydrogenase (IPR006258)
- Glutathione reductase, eukaryote/bacterial (IPR006322)
- Glutathione-disulphide reductase (IPR006324)
- Mercury(II) reductase (IPR021179)
- Mycothione reductase (IPR017817)
- Soluble pyridine nucleotide transhydrogenase (IPR022962)
- Thioredoxin/glutathione reductase selenoprotein (IPR006338)
- Trypanothione reductase (IPR001864)
The pyridine nucleotide-disulphide reductases (PNDR) use the isoalloxazine ring of FAD to shuttle reducing equivalents from NAD(P)H to a Cys residue that is usually a part of a redox-active disulphide bridge. In a second step, the reduced disulphide reduces the substrate. On the basis of sequence and structural similarities [PMID: 2067578], PNDR can be categorised into 2 groups.
Class I includes glutathione reductase, trypanothione reductase, lipoamide dehydrogenase and mercuric reductase. They cover a wide range of catalytic functions: glutathione reductase ensures that the cell has enough reduced glutathione to maintain protein thiol groups in the reduced state [PMID: 2241146]; trypanothione reductase carries out the analogous reaction in trypanosomal cells (trypanothione is an analogue of glutathione) [PMID: 3718941]; lipoamide dehydrogenase, the E3 component of alpha-ketoacid dehydrogenase multienzyme complex, oxidises the dihydrolypoyl groups of lipoate acyltransferase, and so couples glycolysis to the tricarboxylic acid cycle [PMID: 2643922]; and mercuric reductase enables bacteria to detoxify the mercuric ion by reducing it to elemental mercury, which evaporates from the cell [PMID: 1311113].
- PIRSF000350 (Mercury_reductase_MerA)