Inhibition by fructose 1,6-bisphosphate of transaldolase from Escherichia coli.
FEMS Microbiol Lett
; 363(17)2016 09.
Article
em En
| MEDLINE
| ID: mdl-27481705
ABSTRACT
The effect of fructose 1,6-bisphosphate (Fru 1,6-P2) on the regulatory enzymes of pentose phosphate pathway of Escherichia coli was examined. Fru 1,6-P2 inhibited E. coli transaldolase (EC 2.2.1.2) competitively against fructose 6-phosphate and uncompetitively against erythrose 4-phosphate, whereas Fru 1,6-P2 did not affect glucose 6-phosphate dehydrogenase (EC 1.1.1.49) and 6-phosphogluconate dehydrogenase (EC 1.1.1.44). Kinetic results can be explained by assuming that transaldolase has two kinds of binding sites for Fru 1,6-P2 a competitive binding site for fructose 6-phosphate and a second binding site on the enzyme-erythrose 4-phosphate complex. Fru 1,6-P2 increased resulting from the stimulation of glycolysis, can inhibit transaldolase and further participates in the elevation of the concentration of ribose 5-phosphate that can be preferentially utilized for anabolic reaction in exponential phase of E. coli.
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Texto completo:
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Base de dados:
MEDLINE
Assunto principal:
Via de Pentose Fosfato
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Transaldolase
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Escherichia coli
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Frutosedifosfatos
Idioma:
En
Ano de publicação:
2016
Tipo de documento:
Article