Person:
Moreno Bruna, Beatriz

Profile Picture

Email Address

person.page.identifierURI

https://academica-e.unavarra.es/handle/2454/49614

Birth Date

Research Projects

Organizational Units

Job Title

Last Name

Moreno Bruna

First Name

Beatriz

person.page.departamento

Instituto de Agrobiotecnología (IdAB)

person.page.instituteName

ORCID

person.page.upna

5495

Name

Filters

20011
Reset filters

Settings

Search Results

Now showing 1 - 1 of 1
  • Thumbnail Image
    PublicationOpen Access
    Adenosine diphosphate sugar pyrophosphatase prevents glycogen biosynthesis in Escherichia coli
    (National Academy of Sciences, 2001) Moreno Bruna, Beatriz; Baroja Fernández, Edurne; Muñoz Pérez, Francisco José; Bastarrica Berasategui, Ainara; Zandueta Criado, Aitor; Rodríguez López, Milagros; Lasa Uzcudun, Íñigo; Akazawa, Takashi; Pozueta Romero, Javier; IdAB. Instituto de Agrobiotecnología / Agrobioteknologiako Institutua
    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.