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Diphosphonucleotide phosphatase/phosphodiesterase from yellow lupin ( Lupinus luteus L.) belongs to a novel group of specific metallophosphatases
Author(s) -
Olczak Mariusz,
Olczak Teresa
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)02740-0
Subject(s) - biology , gene , complementary dna , phosphatase , open reading frame , genetics , biochemistry , peptide sequence , enzyme
A cDNA encoding previously purified and characterized diphosphonucleotide phosphatase/phosphodiesterase (PPD1) from yellow lupin ( Lupinus luteus L.) was identified. The ppd1 gene encodes a protein containing a cleavable signal sequence. A functional expression of PPD1 in Saccharomyces cerevisiae confirmed the proper gene identification. A gene homologous to ppd1 , encoding a putative membrane protein (PPD2), as well as fragments of two other genes encoding PPD3 and PPD4 proteins were also isolated. Amino acids composing the putative active center of PPD1 and PPD2 are similar to those present in known purple acid phosphatases, which suggests that the reported genes might encode a novel group of specific metallophosphatases. RT‐PCR revealed that the corresponding PPD1 mRNA accumulates in stems and leaves, and PPD2 mRNA in stems, leaves and seedlings.