| 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 [ ]. | Name | Pyridine nucleotide-disulphide oxidoreductase, class I, active site |
| Short Name | Pyr_OxRdtase_I_AS | Type | Active_site |
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