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
Plantajournal_title
Plantaauthors
Porchia AC,Curatti L,Salerno GLdoi
10.1007/s004250050651subject
Has Abstractpub_date
1999-11-01 00:00:00pages
34-40issue
1eissn
0032-0935issn
1432-2048pii
10.1007/s004250050651journal_volume
210pub_type
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