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Plant and Cell Physiology, 2003, Vol. 44, No. 3 326-333
© 2003 Oxford University Press

Purification and Characterization of Class-I and Class-II Fructose-1,6-bisphosphate Aldolases from the Cyanobacterium Synechocystis sp. PCC 6803

Ken Nakahara1, Hiroshi Yamamoto2,3, Chikahiro Miyake1,4 and Akiho Yokota1,2,5

1 Graduate School of Biological Sciences, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara, 630-0101 Japan
2 Plant Molecular Physiology Laboratory, Research Institute of Innovate Technology for the Earth (RITE), 9-2 Kizugawadai, Kizu, Sorakugun, Kyoto, 619-0292 Japan

The whole genome sequence database for Synechocystis sp. PCC 6803 has revealed the presence of genes encoding class-I (CI) and class-II (CII) fructose-1,6-bisphosphate aldolases (FBAs) in this organism. Two types of FBA from Synechocystis sp. PCC 6803 were separated by chromatography on phenyl-Sepharose. The activity of the enzyme in the major peak was inhibited by the presence of 25 mM EDTA; however, the activity in the minor peak was not. Therefore, the FBA in the former fractions was designated as CII-FBA, and in the latter designated as CI-FBA. CI-FBA was functionally redundant in Synechocystis sp. PCC 6803, while no disruptant for the gene encoding CII-FBA was obtained under photoautotrophic conditions. The kinetic parameters of CI- and CII-FBAs purified from Synechocystis sp. PCC 6803 in the cleavage reaction of FBP were generally similar, except in their reactivity for SBP. The SBP/FBP activity ratio of the CII-FBA was two times higher than that of the CI-FBA.

3 Present address: Department of Regulation Biology, National Institute for Basic Biology, Myodaiji, Okazaki, 444-8585 Japan.

4 Present address: Graduate School of Bioresource and Bioenvironmental Sciences, Kyushu University, 6-10-1, Hakozaki, Higashi-ku, Fukuoka, 812-8581 Japan.

5 Corresponding author: E-mail, yokota{at}bs.aist-nara.ac.jp; Fax, +81-743-72-5569.


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