Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2049667 | FEBS Letters | 2009 | 5 Pages |
Abstract
Yellow lupin diphosphonucleotide phosphatase/phosphodiesterase (PPD1) represents a novel group of enzymes. Here we report that it possesses one iron atom and one manganese atom (1:1 molar ratio) per subunit. The enzyme exhibits visible absorption maximum at ∼530 nm. Prolonged oxidation of PPD1 leads to loss of the charge-transfer band and catalytic activity, whereas after reduction PPD1 remains active. Replacement of conserved amino-acid residues coordinating metals results in the loss of enzymatic activity. Despite low amino-acid sequence homology of PPD1 to well-characterized ∼55-kDa purple acid phosphatases, their overall fold, topology of active center and metal content are highly similar.
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Authors
Mariusz Olczak, Justyna Ciuraszkiewicz, Halina Wójtowicz, Dorota Maszczak, Teresa Olczak,