PMID: 70226Sep 15, 1977Paper

Two Escherichia coli fructose-6-phosphate kinases. Preparative purification, oligomeric structure and immunological studies

Biochimica Et Biophysica Acta
D Kotlarz, H Buc

Abstract

Two isoenzymes of fructose-6-phosphate kinase (ATP: D-fructose-6-phosphate 1-phosphotransferase, EC 2.7.1.11) are present in Escherichia coli K12. One isoenzyme is allosterically inhibited by phosphoenolpyruvate and activated by nucleoside diphosphates, and is a tetramer composed of four subunits of molecular weight 35 000. A simple method for the purification of this enzyme is reported. Equilibrium dialysis indicates that there are four ATP sites and four GDP sites per tetramer. The second isoenzyme is present in low quantity in wild type bacteria. This enzyme is devoid of allosteric properties. A complete method of purification is described. Determination of its molecular weight under native and denaturing conditions indicates that this protein is a dimer composed of two subunits of molecular weight 36 000. Antisera have been produced against both isoenzymes. The antiserum against one isoenzyme does not cross-react with the other. Discrepancies between our results and those of other workers are discussed.

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Citations

Oct 18, 2001·Protein Science : a Publication of the Protein Society·J L JohnsonG D Reinhart
Apr 14, 1978·Biochemical and Biophysical Research Communications·J P Robinson, D G Fraenkel
Jun 3, 1985·European Journal of Biochemistry·H W Hellinga, P R Evans
Aug 2, 2016·Archives of Biochemistry and Biophysics·Amy M Whitaker, Gregory D Reinhart
Sep 4, 2008·Journal of Bioinformatics and Computational Biology·Kirill PeskovOleg Demin
Feb 12, 1991·Biochemistry·C E Kundrot, P R Evans
Jul 1, 1981·European Journal of Biochemistry·D Kotlarz, H Buc
May 1, 1979·International Journal of Peptide and Protein Research·D M Kirschenbaum
Oct 1, 1979·Journal of Chromatography·P D Dean, D H Watson
Sep 1, 1981·Journal of Bacteriology·F Daldal, D G Fraenkel

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