Phosphorylation of sucrose synthase from maize seedlings

• Autorzy: Lindblom S. , Ek P. , Muszynska G. , Ek B. , Szczegielniak J. , Engstrom L.
• Języki publikacji: EN

Abstrakty

EN

Two isoforms of sucrose synthase (SS1 and SS2) from maize (Zea mays, var. Mona) seedlings co-purified with a calcium and phospholipid dependent protein kinase. The enzymatic preparation obtained gave a positive reaction with the antibody against mammalian protein kinase C. Maize sucrose synthase was phosphorylated by the endogenous protein kinase. Also, mammalian protein kinases (protein kinase C and protein kinase A) were able to phosphorylate the 86 kDa subunit of sucrose synthase. When excised seedlings were fed [32P]orthophosphate, sucrose synthase was also phosphorylated. Microsequencing of in vivo labelled enzyme has shown phosphorylation of Ser-15 in SS2. The present work provides evidence that maize sucrose synthase is the physiological substrate of the endogenous calcium and phospholipid dependent protein kinase(s).

Słowa kluczowe

EN

Zea mays; calcium; sucrose; phosphorylation; sucrose metabolism; transduction; synthase signal; protein kinase C; maize

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 1997
• Tom: 44
• Numer: 4
• Opis fizyczny: p.809-817,fig.

Twórcy

autor

Lindblom S.

• Biomedical Centre, Box 575, S-75123 Uppsala, Sweden

autor

Ek P.

autor

Muszynska G.

autor

Ek B.

autor

Szczegielniak J.

autor

Engstrom L.

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