Pyridine nucleotide-disulphide oxidoreductase, class I (IPR001100)

Short name: Pyr_nuc-diS_OxRdtase

Overlapping homologous superfamilies

Family relationships


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].

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0009055 electron transfer activity
GO:0016491 oxidoreductase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.