| Type: | Active_site | Name: | Pyridine nucleotide-disulphide oxidoreductase, class I, active site |
| Description: | The pyridine nucleotide-disulphide oxidoreductases are FAD flavoproteins which contain a pair of redox-active cysteines involved in the transfer of reducing equivalents from the FAD cofactor to the substrate. On the basis of sequence and structural similarities [] these enzymes can be classified into two categories. The first category groups together the following enzymes [, , , ]:Glutathione reductase () (GR).Higher eukaryotes thioredoxin reductase ().Trypanothione reductase (). Lipoamide dehydrogenase (), the E3 component of alpha-ketoacid dehydrogenase complexes.Mercuric reductase ().The sequence around the two cysteines involved in the redox-active disulphide bond is conserved and can be used as a signature pattern.Note: In positions 6 and 7 of the pattern all known sequences have Asn-(Val/ Ile) with the exception of GR from plant chloroplasts and from cyanobacteria which have Ile-Arg []. | Short Name: | Pyr_OxRdtase_I_AS |
| DB identifier | Type | Name |
|---|---|---|
| IPR006258 | Family | Dihydrolipoamide dehydrogenase |
| IPR006324 | Family | Glutathione-disulphide reductase |
| IPR006338 | Family | Thioredoxin/glutathione reductase selenoprotein |
| IPR021179 | Family | Mercury(II) reductase |
| IPR006322 | Family | Glutathione reductase, eukaryote/bacterial |
| IPR017817 | Family | Mycothione reductase |
| IPR001864 | Family | Trypanothione reductase |
