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    Author(s): Luis F. Larrondo; Angel Gonzalez; Tomas Perez-Acle; Dan Cullen; Rafael Vicuna
    Date: 2005
    Source: Biophysical chemistry. Vol. 116 (2005): pages 167-173
    Publication Series: Miscellaneous Publication
    PDF: View PDF  (373 KB)


    Inspection of the genome of the ligninolytic basidiomycete Phanerochaete chrysosporium revealed an unusual peroxidase-like sequence. The corresponding full length cDNA was sequenced and an archetypal secretion signal predicted. The deduced mature protein (NoP, novel peroxidase) contains 295 aa residues and is therefore considerably shorter than other Class II (fungal) peroxidases, such as lignin peroxidases and manganese peroxidases. Comparative modeling of NoP was conducted using the crystal structures of Coprinus cinereus and Arthromyces ramosus peroxidases as templates. The model was validated by molecular dynamics and showed several novel structural features. In particular, NoP has only three disulfide bridges and tryptophan replaces the distal phenylalanine within the heme pocket.

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    Larrondo, Luis F.; Gonzalez, Angel; Perez-Acle, Tomas; Cullen, Dan; Vicuna, Rafael. 2005. The nop gene from Phanerochaete chrysosporium encodes a peroxidase with novel structural features. Biophysical chemistry. Vol. 116 (2005): pages 167-173


    Oxidoreductase, peroxidase, Phanerochaete chrysosporium, modeling, molecular dynamics

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