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 degrees C. When this unique disulfide bond is cleaved the enzyme is stable up to 40 degrees 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 degrees C. Thus, the N-terminal is important for the stability of the enzyme because of the presence of a disulfide bond.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Ballicora MA,Fu Y,Frueauf JB,Preiss Jdoi
10.1006/bbrc.1999.0469subject
Has Abstractpub_date
1999-04-21 00:00:00pages
782-6issue
3eissn
0006-291Xissn
1090-2104pii
S0006-291X(99)90469-2journal_volume
257pub_type
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