TY - JOUR
T1 - Purification and properties of a nucleotide pyrophosphatase from lentil seedlings.
AU - Medda, Rosaria
AU - Padiglia, Alessandra
AU - Lorrai, Anita
AU - Finazzi Agrò, Alessandro
AU - Castagnola, Massimo
AU - Floris, Giovanni
PY - 2000
Y1 - 2000
N2 - A nucleotide pyrophosphatase (EC 3.6.1.9) was purified to homogeneity from lentil seedlings. The enzyme is a single polypeptide chain of 75 +/- 2 kDa that exhibits hydrolytic activities toward pyrophosphate linkages of several substrates. Reduced and oxidized forms of NAD(P) were shown to be hydrolyzed to nicotinamide mononucleotide and AMP. Other dinucleotides such as FAD and dinucleoside oligophosphates were hydrolyzed as well, but with lower efficiency. Pyrophosphatase activity was increased in the presence of divalent cations such as Ca2+, Mg2+, and Mn2+, whereas Cu2+, Zn2+, and Ni2+ ions inhibited this activity. The active site in the enzyme was not defined, bur histidine residue(s) seemed to be crucial for the enzymatic activity.
AB - A nucleotide pyrophosphatase (EC 3.6.1.9) was purified to homogeneity from lentil seedlings. The enzyme is a single polypeptide chain of 75 +/- 2 kDa that exhibits hydrolytic activities toward pyrophosphate linkages of several substrates. Reduced and oxidized forms of NAD(P) were shown to be hydrolyzed to nicotinamide mononucleotide and AMP. Other dinucleotides such as FAD and dinucleoside oligophosphates were hydrolyzed as well, but with lower efficiency. Pyrophosphatase activity was increased in the presence of divalent cations such as Ca2+, Mg2+, and Mn2+, whereas Cu2+, Zn2+, and Ni2+ ions inhibited this activity. The active site in the enzyme was not defined, bur histidine residue(s) seemed to be crucial for the enzymatic activity.
KW - Enzimi
KW - Purificazione
KW - biochimica
KW - Enzimi
KW - Purificazione
KW - biochimica
UR - http://hdl.handle.net/10807/25513
M3 - Article
SP - 209
EP - 214
JO - Journal Protein Chemistry
JF - Journal Protein Chemistry
ER -