Use of an Escherichia coli recombinant producing thermostable polyphosphate kinase as an ATP regenerator to produce fructose 1,6-diphosphate.
نویسندگان
چکیده
Heat-treated Escherichia coli producing Thermus polyphosphate kinase regenerated ATP by using exogenous polyphosphate. This recombinant could be used as a platform to produce valuable compounds in combination with thermostable phosphorylating or energy-requiring enzymes. In this work, we demonstrated the production of fructose 1,6-diphosphate from fructose and polyphosphate.
منابع مشابه
Polyphosphate kinase as a nucleoside diphosphate kinase in Escherichia coli and Pseudomonas aeruginosa.
Generation of a wide variety of nucleoside (and deoxynucleoside) triphosphates (NTPs) from their cognate nucleoside diphosphates (NDPs) is of critical importance in virtually every aspect of cellular life. Their function is fulfilled largely by the ubiquitous and potent nucleoside diphosphate kinase (NDK), most commonly using ATP as the donor. Considerable interest is attached to the consequenc...
متن کاملAllosteric regulation of glycerol kinase by enzyme IIIglc of the phosphotransferase system in Escherichia coli and Salmonella typhimurium.
The mechanism by which enzyme IIIglc of the bacterial phosphotransferase system regulates the activity of crystalline glycerol kinase from Escherichia coli has been studied, and the inhibitory effects have been compared with those produced by fructose-1,6-diphosphate. It was shown that the free, but not the phosphorylated, form of enzyme IIIglc inhibits the kinase. Mutants of Salmonella typhimu...
متن کاملEffect of a nonmetabolizable analog of fructose-1,6-bisphosphate on glycolysis and ethanol production in strains of Saccharomyces cerevisiae and Escherichia coli.
Fructose-1,6-bisphosphate (F-1,6-P2) is an allosteric activator of two key enzymes of glycolysis: phosphofructokinase and pyruvate kinase. Regulation of glycolysis in a wild-type Saccharomyces cerevisiae and a recombinant Escherichia coli by a dead-end structural analog of F-1,6-P2 was studied. 2,5-Anhydromannitol (2,5-AM), a structural analog of beta-d-fructose, was used. On being taken up by ...
متن کاملThe control of pyruvate kinases of Escherichia coli. I. Physicochemical and regulatory properties of the enzyme activated by fructose 1,6-diphosphate.
The pyruvate kinase of Escherichia coli activated by fructose 1,6-diphosphate has been purified to homogeneity. It is a tetramer of molecular weight about 240,000. By electrophoresis on sodium dodecyl sulfate polyacrylamide gels, Sephadex gel filtration in denaturing solvents, and ultracentrifugational experiments, the monomer molecular weight is found to be 60,000. Tryptophan is absent from th...
متن کاملThe Control of Pyruvate Kinases of Escherichia coli I. PHYSICOCHEMICAL AND REGULATORY PROPERTIES OF THE ENZYME ACTIVATED BY FRUCTOSE
The pyruvate kinase of Escherichia coli activated by fructose 1,6-diphosphate has been purified to homogeneity. It is a tetramer of molecular weight about 240,000. By electrophoresis on sodium dodecyl sulfate polyacrylamide gels, Sephadex gel filtration in denaturing solvents, and ultracentrifugational experiments, the monomer molecular weight is found to be 60,000. Tryptophan is absent from th...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Applied and environmental microbiology
دوره 73 17 شماره
صفحات -
تاریخ انتشار 2007