| Description | 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 [ ], 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 [ ]; trypanothione reductase carries out the analogous reaction in trypanosomal cells (trypanothione is an analogue of glutathione) []; 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 []; and mercuric reductase enables bacteria to detoxify the mercuric ion by reducing it to elemental mercury, which evaporates from the cell []. | Name | Pyridine nucleotide-disulphide oxidoreductase, class I |
| Short Name | Pyr_nuc-diS_OxRdtase | Type | Family |
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