Molecular cloning and sequencing of ADP-glucose pyrophosphorylase from Synechocystis PCC 6803
ADPGlc PPase super(3) is the regulatory enzyme for synthesis of starch in plants and glycogen in bacteria. Previous work on cyanobacterial ADPGlc PPase has shown the enzyme to have intermediate characteristics to that of the higher plant and bacterial enzymes. ADPGlc PPase from Synechocystis) PCC 68...
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Veröffentlicht in: | Plant physiology (Bethesda) 1992-05, Vol.99 (1), p.359-361 |
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Sprache: | eng |
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Zusammenfassung: | ADPGlc PPase super(3) is the regulatory enzyme for synthesis of starch in plants and glycogen in bacteria. Previous work on cyanobacterial ADPGlc PPase has shown the enzyme to have intermediate characteristics to that of the higher plant and bacterial enzymes. ADPGlc PPase from Synechocystis) PCC 6803 is allosterically activated by 3-phosphoglycerate and inhibited by Pi, as are the higher plant enzymes. The homotetrameric structure of Synechocystis ADPGlc PPase is similar to the enteric bacterial enzymes, which is in contrast with the heterotetrameric nature of all higher plant enzymes studied. Here we report the nucleotide sequence of ADPGlc PPase from Synechocystis PPC 6803. |
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ISSN: | 0032-0889 1532-2548 |
DOI: | 10.1104/pp.99.1.359 |