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ADP-glucose pyrophosphorylase, a regulatory enzyme for bacterial glycogen synthesis.
Ballicora, Miguel A; Iglesias, Alberto A; Preiss, Jack.
Afiliação
  • Ballicora MA; Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, Michigan 48824, USA.
Microbiol Mol Biol Rev ; 67(2): 213-25, table of contents, 2003 Jun.
Article em En | MEDLINE | ID: mdl-12794190
The accumulation of alpha-1,4-polyglucans is an important strategy to cope with transient starvation conditions in the environment. In bacteria and plants, the synthesis of glycogen and starch occurs by utilizing ADP-glucose as the glucosyl donor for elongation of the alpha-1,4-glucosidic chain. The main regulatory step takes place at the level of ADP-glucose synthesis, a reaction catalyzed by ADP-Glc pyrophosphorylase (PPase). Most of the ADP-Glc PPases are allosterically regulated by intermediates of the major carbon assimilatory pathway in the organism. Based on specificity for activator and inhibitor, classification of ADP-Glc PPases has been expanded into nine distinctive classes. According to predictions of the secondary structure of the ADP-Glc PPases, they seem to have a folding pattern common to other sugar nucleotide pyrophosphorylases. All the ADP-Glc PPases as well as other sugar nucleotide pyrophosphorylases appear to have evolved from a common ancestor, and later, ADP-Glc PPases developed specific regulatory properties, probably by addition of extra domains. Studies of different domains by construction of chimeric ADP-Glc PPases support this hypothesis. In addition to previous chemical modification experiments, the latest random and site-directed mutagenesis experiments with conserved amino acids revealed residues important for catalysis and regulation.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Bactérias / Glicogênio / Nucleotidiltransferases Idioma: En Revista: Microbiol Mol Biol Rev Assunto da revista: BIOLOGIA MOLECULAR / MICROBIOLOGIA Ano de publicação: 2003 Tipo de documento: Article País de afiliação: Estados Unidos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Bactérias / Glicogênio / Nucleotidiltransferases Idioma: En Revista: Microbiol Mol Biol Rev Assunto da revista: BIOLOGIA MOLECULAR / MICROBIOLOGIA Ano de publicação: 2003 Tipo de documento: Article País de afiliação: Estados Unidos