Heat stability of the potato tuber ADP-glucose pyrophosphorylase: Role of Cys residue 12 in the small subunit

Miguel A. Ballicora, Yingbin Fu, Jeremiah B. Frueauf, Jack Preiss

Research output: Contribution to journalArticlepeer-review

Abstract

Most of the ADP-glucose pyrophosphorylases from different sources are stable to a heat treatment. We found that in the potato (Solanum tuberosum L.) tuber enzyme, the intermolecular disulfide bridge located between Cys12 of the small subunits is responsible for the stability at 60°C. When this unique disulfide bond is cleaved the enzyme is stable up to 40°C. Mutation of Cys12 in the small subunit into either Ala or Ser yielded enzymes with stability similar to the reduced form of the wild type. Concurrently, the enzyme with a truncated small subunit on the N-terminal was stable only up to 40°C. Thus, the N-terminal is important for the stability of the enzyme because of the presence of a disulfide bond.

Original languageEnglish (US)
Pages (from-to)782-786
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume257
Issue number3
DOIs
StatePublished - Apr 21 1999
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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