Purification and properties of a nucleotide pyrophosphatase from lentil seedlings

被引：5

作者：

Medda, R ^{[1
]}

Padiglia, A ^{[1
]}

Lorrai, A ^{[1
]}

Murgia, B ^{[1
]}

Agrò, AF ^{[1
]}

Castagnola, M ^{[1
]}

Floris, G ^{[1
]}

机构：

[1] Univ Cagliari, Dept Sci Appl Biosyst, Sez Biochim & Biol Mol, Monserrato, CA, Italy

来源：

JOURNAL OF PROTEIN CHEMISTRY | 2000年 / 19卷 / 03期

关键词：

Lens esculenta; Leguminosae; nucleotide pyrophosphatase; nucleotides;

D O I：

10.1023/A:1007007803996

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：209 / 214

页数：6

共 31 条

[1] NICOTINAMIDE-ADENINE DINUCLEOTIDE PYROPHOSPHATASE IN GROWING AND AGING MOSQUITO [J].