Pathways & interactions
Pyridine nucleotide-disulphide oxidoreductase, class I, active site (IPR012999)
Short name: Pyr_OxRdtase_I_AS
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 [PMID: 2067578] these enzymes can be classified into two categories. The first category groups together the following enzymes [PMID: 6546954, PMID: 2643922, PMID: 1957352, PMID: 7589432]:
- Glutathione reductase (EC:18.104.22.168) (GR).
- Higher eukaryotes thioredoxin reductase (EC:22.214.171.124).
- Trypanothione reductase (EC:126.96.36.199).
- Lipoamide dehydrogenase (EC:188.8.131.52), the E3 component of alpha-ketoacid dehydrogenase complexes.
- Mercuric reductase (EC:184.108.40.206).
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 [PMID: 1303792].
- PS00076 (PYRIDINE_REDOX_1)