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

被引：41

作者：

Cumino, A ^{[1
]}

Curatti, L ^{[1
]}

Giarrocco, L ^{[1
]}

Salerno, GL ^{[1
]}

机构：

[1] FIBA, Ctr Invest Biol, Mar Del Plata, Argentina

来源：

FEBS LETTERS | 2002年 / 517卷 / 1-3期

关键词：

cyanobacterium; sucrose-phosphate synthase; sucrose-phosphate phosphatase; sucrose synthase; modular arrangement; phylogenetic analysis;

D O I：

10.1016/S0014-5793(02)02516-4

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

引用

页码：19 / 23

页数：5

共 36 条

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