Abnormal muscle fructose bisphosphatase activity in malnourished cancer patients
نویسندگان
چکیده
منابع مشابه
Rabbit muscle fructose-1,6-bisphosphatase is phosphorylatedin vivo.
Phosphorylated fructose-1,6-bisphosphatase (FBPase) was isolated from rabbit muscle in an SDS/PAGE homogeneous form. Its dephosphorylation with alkaline phosphatase revealed 2.8 moles of inorganic phosphate per mole of FBPase. The phosphorylated FBPase (P-FBPase) differs from the dephosphorylated enzyme in terms of its kinetic properties like K(m) and k(cat), which are two times higher for the ...
متن کاملCrystallographic data for chicken liver fructose bisphosphatase.
Large, single crystals of fructose bisphosphatase have been obtained under a variety of conditions. Preliminary crystallographic analysis reveals that the space group is R3, the cell dimensions on the hexagonal axes are a = b = 304 A and c = 80.4 A, and there is one tetramer per asymmetric unit.
متن کاملDimeric and tetrameric forms of muscle fructose-1,6-bisphosphatase play different roles in the cell
Muscle fructose 1,6-bisphosphatase (FBP2), besides being a regulatory enzyme of glyconeogenesis also protects mitochondria against calcium stress and plays a key role in regulation of the cell cycle, promoting cardiomyocytes survival. However, in cancer cells, FBP2 acts as an anti-oncogenic/anti-proliferative protein. Here, we show that the physiological function of FBP2 depends both on its lev...
متن کاملTwo enzymes with redundant fructose bisphosphatase activity sustain gluconeogenesis and virulence in Mycobacterium tuberculosis
The human pathogen Mycobacterium tuberculosis (Mtb) likely utilizes host fatty acids as a carbon source during infection. Gluconeogenesis is essential for the conversion of fatty acids into biomass. A rate-limiting step in gluconeogenesis is the conversion of fructose 1,6-bisphosphate to fructose 6-phosphate by a fructose bisphosphatase (FBPase). The Mtb genome contains only one annotated FBPas...
متن کاملThe Mechanism of Calcium-Induced Inhibition of Muscle Fructose 1,6-bisphosphatase and Destabilization of Glyconeogenic Complex
The mechanism by which calcium inhibits the activity of muscle fructose 1,6-bisphosphatase (FBPase) and destabilizes its interaction with aldolase, regulating glycogen synthesis from non-carbohydrates in skeletal muscle is poorly understood. In the current paper, we demonstrate evidence that Ca(2+) affects conformation of the catalytic loop 52-72 of muscle FBPase and inhibits its activity by co...
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ژورنال
عنوان ژورنال: Cancer
سال: 1986
ISSN: 0008-543X,1097-0142
DOI: 10.1002/1097-0142(19861201)58:11<2448::aid-cncr2820581116>3.0.co;2-7