Characterization of diphosphonucleotide phosphatase/phosphodiesterase from yellow lupin (Lupinus luteus) seeds.
A phosphatase cleaving the pyrophosphate bond in diphosphonucleotides and phosphodiester bond in various phosphodiesters (pH optimum at 6.25) was purified from yellow lupin (Lupinus luteus L.) seeds. The enzyme is 75 kDa monomeric glycoprotein (pI=6.4) with 4.4% of carbohydrate (mannose, N-acetylglucosamine, fucose and xylose). Analysis of its partial amino acid sequence (8 peptides, 101 amino acid residues) together with no divalent cation requirements for catalysis points out that the purified enzyme is different from known plant pyrophosphate cleaving enzymes (apyrases and inorganic pyrophosphatases). Its physiological role could be related to a regulation of diphosphonucleotides level in plant metabolism.
Olczak
M
M
Institute of Biochemistry and Molecular Biology, Wroclaw University, Tamka 2, 50-137, Wroclaw, Poland.
Kobiałka
M
M
Watorek
W
W
D000595:Amino Acid Sequence; D002846:Chromatography, Affinity; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D004492:Edetic Acid; D004591:Electrophoresis, Polyacrylamide Gel; D008670:Metals; D008969:Molecular Sequence Data; D009708:Nucleotidases / Q000737:chemistry; D010446:Peptide Fragments; D010744:Phosphoric Monoester Hydrolases / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D010944:Plants / Q000201:enzymology*; D012639:Seeds / Q000201:enzymology; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity
D008670:Metals; D010446:Peptide Fragments; D004492:Edetic Acid; D009708:Nucleotidases; D010744:Phosphoric Monoester Hydrolases