Planta

, Volume 210, Issue 1, pp 34–40

Sucrose metabolism in cyanobacteria: sucrose synthase from Anabaena sp. strain PCC 7119 is remarkably different from the plant enzymes with respect to substrate affinity and amino-terminal sequence

Authors

  • Andrea C. Porchia
    • Centro de Investigaciones Biológicas, Fundación para Investigaciones Biológicas Aplicadas (FIBA)-PROBIOP (CONICET), C.C. 1348, 7600 Mar del Plata, Argentina
  • Leonardo Curatti
    • Centro de Investigaciones Biológicas, Fundación para Investigaciones Biológicas Aplicadas (FIBA)-PROBIOP (CONICET), C.C. 1348, 7600 Mar del Plata, Argentina
  • Graciela L. Salerno
    • Centro de Investigaciones Biológicas, Fundación para Investigaciones Biológicas Aplicadas (FIBA)-PROBIOP (CONICET), C.C. 1348, 7600 Mar del Plata, Argentina
Article

DOI: 10.1007/s004250050651

Cite this article as:
Porchia, A., Curatti, L. & Salerno, G. Planta (1999) 210: 34. doi:10.1007/s004250050651

Abstract.

The pathway of sucrose metabolism in cyanobacteria is just starting to be elucidated. The present study describes the first isolation and biochemical characterization of a prokaryotic sucrose synthase (SS, EC 2.4.1.13). Two SS forms (SS-I and SS-II) were detected in Anabaena sp. strain PCC 7119. The isoform SS-II was purified 457-fold and its amino-terminal portion sequenced. Substrate specificity, kinetic constants, native protein and subunit molecular masses, and the effect of different ions and metabolites were studied for SS-II. Anabaena SS was shown to be a tetramer with a 92-kDa polypeptide that was recognized by maize SS polyclonal antibodies. Some striking differences from plant enzymes were demonstrated with respect to substrate affinities, regulation by metal ions and ATP, and the amino-acid sequence of the N-terminal region.

Key words:Anabaena sp. (sucrose metabolism)CyanobacteriumSucroseSucrose synthase

Copyright information

© Springer-Verlag Berlin Heidelberg 1999