The pyridine nucleotide-disulphide oxidoreductases are FAD flavoproteins which
contains 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 [1] these enzymes can be classified into two
categories. The first category groups together the following enzymes [2,3,4,5,6]:
The sequence around the two cysteines involved in the redox-active disulfide
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 [7].
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