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.

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.

journal_name

Planta

journal_title

Planta

authors

Porchia AC,Curatti L,Salerno GL

doi

10.1007/s004250050651

subject

Has Abstract

pub_date

1999-11-01 00:00:00

pages

34-40

issue

1

eissn

0032-0935

issn

1432-2048

pii

10.1007/s004250050651

journal_volume

210

pub_type

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