| Value |
58
µM
|
| Organism |
Bacteria Escherichia coli |
| Reference |
Baez M, Rodríguez PH, Babul J, Guixé V. Structural and functional roles of Cys-238 and Cys-295 in Escherichia coli phosphofructokinase-2. Biochem J. 2003 Nov 15 376(Pt 1):277-83PubMed ID12927023
|
| Method |
ATP and fru-6-P concentrations were estimated spectrophotometrically
by measuring the amount of fru-1,6-bisP formed in the presence
of NADH, using aldolase, triosephosphate isomerase and
a-glycerophosphate dehydrogenase as auxiliary enzymes. PFK activity was determined spectrophotometrically by coupling
the fru-1,6-bisP formation to the oxidation of NADH as described
previously [5]. |
| Comments |
Phosphofructokinase (PFK, EC. 2.7.1.11) is a central enzyme of
glycolysis and is found in almost all organisms, from bacteria to
higher eukaryotes. Owing to its important role in the control of
glycolytic flux and its allosteric properties, PFK has long been
a subject of study in terms of both its enzymology and protein
chemistry. The enzyme catalyses the conversion of fructose 6-
phosphate (fru-6-P) into fructose 1,6-bisphosphate (fru-1,6-bisP),
with associated consumption of ATP. In Escherichia coli, two
different enzymes catalyse this reaction: a Pfk-1,which represents
90% of the total activity and Pfk-2, which accounts for the rest. |
| Entered by |
Uri M |
| ID |
104956 |