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Sucrose metabolism: Anabaena sucrose-phosphate synthase and sucrose-phosphate phosphatase define minimal functional domains shuffled during evolution

Based on the functional characterization of sucrose biosynthesis related proteins [SBP: sucrose-phosphate synthase (SPS), sucrose-phosphate phosphatase (SPP), and sucrose synthase (SuS)] in Anabaena sp. PCC7120 and sequence analysis, we have shown that SBP are restricted to cyanobacterium species an...

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Bibliographic Details
Published in:FEBS letters 2002-04, Vol.517 (1), p.19-23
Main Authors: Cumino, Andrea, Curatti, Leonardo, Giarrocco, Laura, Salerno, Graciela L.
Format: Article
Language:English
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Summary:Based on the functional characterization of sucrose biosynthesis related proteins [SBP: sucrose-phosphate synthase (SPS), sucrose-phosphate phosphatase (SPP), and sucrose synthase (SuS)] in Anabaena sp. PCC7120 and sequence analysis, we have shown that SBP are restricted to cyanobacterium species and plants, and that they are multidomain proteins with modular architecture. Anabaena SPS, a minimal catalytic SPS unit, defines a glucosyltransferase domain present in all SPSs and SuSs. Similarly, Anabaena SPP defines a phosphohydrolase domain characteristic of all SPPs and some SPSs. Phylogenetic analysis points towards the evolution of modern cyanobacterial and plant SBP from a bidomainal common ancestral SPS-like gene.
ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(02)02516-4