title: Diphosphonucleotide phosphatase/phosphodiesterase (PPD1) from yellow lupin (Lupinus luteus L.) contains an iron-manganese center.
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 approximately 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 approximately 55-kDa purple acid phosphatases, their overall fold, topology of active center and metal content are highly similar.
authors.affiliation: Laboratory of Biochemistry, Faculty of Biotechnology, University of Wroclaw, Tamka 2, 50-137 Wroclaw, Poland. Mariusz.Olczak@biotech.uni.wroc.pl
authors.forename: Mariusz
authors.initials: M
authors.lastname: Olczak
authors.forename: Justyna
authors.initials: J
authors.lastname: Ciuraszkiewicz
authors.forename: Halina
authors.initials: H
authors.lastname: Wójtowicz
authors.forename: Dorota
authors.initials: D
authors.lastname: Maszczak
authors.forename: Teresa
authors.initials: T
authors.lastname: Olczak
mesh_terms: D000595:Amino Acid Sequence; D017124:Conserved Sequence; D007501:Iron / Q000737:chemistry / Q000378:metabolism*; D031297:Lupinus / Q000201:enzymology*; D008345:Manganese / Q000737:chemistry / Q000378:metabolism*; D013058:Mass Spectrometry; D008958:Models, Molecular; D010727:Phosphoric Diester Hydrolases / Q000737:chemistry / Q000378:metabolism*; D011487:Protein Conformation; D011755:Pyrophosphatases / Q000737:chemistry / Q000378:metabolism*
chemical_list: D008345:Manganese; D007501:Iron; D010727:Phosphoric Diester Hydrolases; D011755:Pyrophosphatases; C457079:diphosphonucleotide phosphatase-phosphodiesterase 1