Adenosine diphosphate sugar pyrophosphatase prevents glycogen biosynthesis in Escherichia coli

被引：50

作者：

Moreno-Bruna, B ^{[1
]}

Baroja-Fernández, E ^{[1
]}

Muñoz, FJ ^{[1
]}

Bastarrica-Berasategui, A ^{[1
]}

Zandueta-Criado, A ^{[1
]}

Rodriguez-López, M ^{[1
]}

Lasa, I ^{[1
]}

Akazawa, T ^{[1
]}

Pozueta-Romero, J ^{[1
]}

机构：

[1] Univ Publ Navarra, Consejo Super Invest Cientifacs, Inst Agrobiotecnol & Recursos Nat, Navarra 31192, Spain

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2001年 / 98卷 / 14期

关键词：

D O I：

10.1073/pnas.131214098

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

An adenosine diphosphate sugar pyrophosphatase (ASPPase, EC 3.6.1.21) has been characterized by using Escherichia coli. This enzyme, whose activities in the cell are inversely correlated with the intracellular glycogen content and the glucose concentration in the culture medium, hydrolyzes ADP-glucose, the precursor molecule of glycogen biosynthesis. ASPPase was purified to apparent homogeneity (over 3,000-fold), and sequence analyses revealed that it is a member of the ubiquitously distributed group of nucleotide pyrophosphatases designated as "nudix" hydrolases. Insertional mutagenesis experiments leading to the inactivation of the ASPPase encoding gene, aspP, produced cells with marginally low enzymatic activities and higher glycogen content than wildtype bacteria, aspP was cloned into an expression vector and introduced into E. coli. Transformed cells were shown to contain a dramatically reduced amount of glycogen, as compared with the untransformed bacteria. No pleiotropic changes in the bacterial growth occurred in both the aspP-overexpressing and aspP-deficient strains. The overall results pinpoint the reaction catalyzed by ASPPase as a potential step of regulating glycogen biosynthesis in E. coli.

引用

页码：8128 / 8132

页数：5