M. Raices et al., CLONING AND CHARACTERIZATION OF A CDNA-ENCODING A CELLOBIOSE DEHYDROGENASE FROM THE WHITE-ROT FUNGUS PHANEROCHAETE-CHRYSOSPORIUM, FEBS letters, 369(2-3), 1995, pp. 233-238
The cDNA of cellobiose dehydrogenase (CDH) from Phanerochaete chrysosp
orium has been cloned and sequenced. The 5' end was obtained by PCR am
plification. The cDNA contains 2310 translated bases excluding the pol
y(A) tail. The deduced mature protein contains 770 amino acid residues
and is preceded by a 18 residue long signal peptide. The regions of t
he amino acid sequence corresponding to the heme and FAD domains of CD
H were identified as well as the nucleotide-binding motif, the disulfi
de pairing and a methionine residue chelating the heme iron. No homolo
gous sequences mere found for the heme domain, however, the FAD domain
appears to be distantly related to the GMC oxidoreductase family.