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Pro With Crack + Product Key .Isolation and analysis of the type IIa isozyme of fructose-1,6-bisphosphatase in theolfactory ensheathing glia of the mouse. Fructose-1,6-bisphosphatase (FBPase, EC 3.1.3.11) is a key enzyme in theglycolytic pathway. It catalyzes the conversion of fructose-1,6-bisphosphate to fructose 6-phosphate and inorganic
orthophosphate. FBPase is encoded by a single gene in mammals and, like other metabolic enzymes involved in energy
metabolism, it is expressed in a variety of tissues and cells. Type IIa isozyme of FBPase (FBPAIIa) has unique properties
among isozymes, particularly among the liver isoforms. It has a weaker affinity for fructose-1,6-bisphosphate (Km = 7-8mM) and a lower specific activity in liver mitochondria than the liver type IIa isozyme, which has Km values of 8-13 mM
and specific activity of 200-300 nmol/min/mg protein. The purified FBPAIIa has optimum pH, Km forfructose-1,6-bisphosphate and Mg2+ between 7.4 and 8.0, and optimum temperature at 30-35 degrees C. It is present inbrain with high concentration in the olfactory ensheathing cells (OECs). The purified enzyme binds topyridoxal-5'-phosphate (PLP) specifically, in a highly cooperative manner. Treatment of OECs with neural growth factor(NGF) decreases the specific FBPAIIa activity and causes a significant shift of type IIa to type I isozyme in mitochondria.
The decrease in the enzyme activity correlates with a significant shift of FBPase activity from type IIa to I isozyme. Thus,
neural regulation of FBPase activity in brain may occur at a post-translational level. Moreover, the type IIa isozyme appears
to be the predominant form in cultured OECDownload
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