scholarly journals Directed Mutations in the Poorly Defined Region of Porcine Liver Fructose-1,6-bisphosphatase Significantly Affect Catalysis and the Mechanism of AMP Inhibition

1998 ◽  
Vol 273 (28) ◽  
pp. 17511-17516 ◽  
Author(s):  
Feruz T. Kurbanov ◽  
Jun-yong Choe ◽  
Richard B. Honzatko ◽  
Herbert J. Fromm
Keyword(s):  
Porcine Liver ◽  
Fructose 1,6 Bisphosphatase ◽  
Amp Inhibition

Different Sensitivities of Mutants and Chimeric Forms of Human Muscle and Liver Fructose- 1,6-Bisphosphatases towards AMP

2003 ◽  
Vol 384 (1) ◽  
pp. 51-58 ◽  
Author(s):  
D. Rakus ◽  
H. Tillmann ◽  
R. Wysocki ◽  
S. Ulaszewski ◽  
K. Eschrich ◽  
...  
Keyword(s):  
Liver Enzyme ◽  
Human Liver ◽  
Human Muscle ◽  
Wild Type ◽  
Muscle Enzyme ◽  
Double Mutation ◽  
Binding Domains ◽  
Fructose 1,6 Bisphosphatase ◽  
Amp Inhibition ◽  
Acid Exchange

Abstract AMP is an allosteric inhibitor of human muscle and liver fructose-1,6-bisphosphatase (FBPase). Despite strong similarity of the nucleotide binding domains, the muscle enzyme is inhibited by AMP approximately 35 times stronger than liver FBPase: I0.5 for muscle and for liver FBPase are 0.14 uM and 4.8 uM, respectively. Chimeric human muscle (L50M288) and chimeric human liver enzymes (M50L288), in which the N-terminal residues (1-50) were derived from the human liver and human muscle FBPases, respectively, were inhibited by AMP 2-3 times stronger than the wild-type liver enzyme. An amino acid exchange within the Nterminal region of the muscle enzyme towards liver FBPase (Lys20→Glu) resulted in 13-fold increased I0.5 values compared to the wild-type muscle enzyme. However, the opposite exchanges in the liver enzyme (Glu20→Lys and double mutation Glu19→Asp/Glu20→Lys) did not change the sensitivity for AMP inhibition of the liver mutant (I0.5 value of 4.9 uM). The decrease of sensitivity for AMP of the muscle mutant Lys20→Glu, as well as the lack of changes in the inhibition by AMP of liver mutants Glu20→Lys and Glu19→Asp/Glu20→Lys, suggest a different mechanism of AMP binding to the muscle and liver enzyme.

scholarly journals The C1-C2 interface residue lysine 50 of pig kidney fructose-1,6-bisphosphatase has a crucial role in the cooperative signal transmission of the AMP inhibition

2000 ◽  
Vol 267 (8) ◽  
pp. 2242-2251 ◽  
Author(s):  
Juan G. Cárcamo ◽  
Alejandro J. Yañez ◽  
Heide C. Ludwig ◽  
Oscar León ◽  
Rodrigo O. Pinto ◽  
...  
Keyword(s):  
Crucial Role ◽  
Signal Transmission ◽  
Interface Residue ◽  
Pig Kidney ◽  
Fructose 1,6 Bisphosphatase ◽  
Amp Inhibition

scholarly journals Spontaneous subunit exchange in porcine liver fructose-1,6-bisphosphatase

FEBS Letters ◽  
2001 ◽  
Vol 492 (3) ◽  
pp. 254-258 ◽  
Author(s):  
Scott W Nelson ◽  
Richard B Honzatko ◽  
Herbert J Fromm
Keyword(s):  
Porcine Liver ◽  
Subunit Exchange ◽  
Fructose 1,6 Bisphosphatase

scholarly journals Inactivation precedes changes in allosteric properties and conformation of d-glyceraldehyde-3-phosphate dehydrogenase and fructose-1,6-bisphosphatase during denaturation by guanidinium chloride

1994 ◽  
Vol 303 (1) ◽  
pp. 241-245 ◽  
Author(s):  
R F Jiang ◽  
C L Tsou
Keyword(s):  
Conformational Changes ◽  
Enzyme Molecule ◽  
Guanidinium Chloride ◽  
Fructose 1,6 Bisphosphatase ◽  
Enzyme Molecules ◽  
Amp Inhibition ◽  
Allosteric Properties

It has been shown that inactivation of several enzymes precedes overall conformational changes of the enzyme molecules as a whole during denaturation [Tsou (1993) Science, 262, 380-381]. However, the relation between inactivation, loss of allosteric properties of oligomeric enzymes and unfolding of the enzyme molecule during denaturation remain little explored. These have now been compared for D-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and fructose-1,6-bisphosphatase (FruP2ase) during denaturation by guanidinium chloride (GdmCl). GAPDH is completely inactivated at 0.3 M GdmCl but at this GdmCl concentration it still binds NAD+ with negative co-operativity. At 0.4 M GdmCl, inactivation of FruP2ase reaches completion whereas its allosteric properties, including the heterotropic effect of AMP inhibition and K+ activation with positive co-operativity, are only partially affected. Much higher GdmCl concentrations are required to bring about unfolding of the overall structures of both enzymes.

Kinetics and Mechanisms of Activation and Inhibition of Porcine Liver Fructose-1,6-bisphosphatase by Monovalent Cations†

Biochemistry ◽  
1996 ◽  
Vol 35 (9) ◽  
pp. 3038-3043 ◽  
Author(s):  
Rulin Zhang ◽  
Vincent Villeret ◽  
William N. Lipscomb ◽  
Herbert J. Fromm
Keyword(s):  
Monovalent Cations ◽  
Porcine Liver ◽  
Fructose 1,6 Bisphosphatase

scholarly journals Major Changes in the Kinetic Mechanism of AMP Inhibition and AMP Cooperativity Attend the Mutation of Arg49in Fructose-1,6-bisphosphatase

1997 ◽  
Vol 272 (42) ◽  
pp. 26295-26299 ◽  
Author(s):  
Lie-Fen Shyur ◽  
Bradley W. Poland ◽  
Richard B. Honzatko ◽  
Herbert J. Fromm
Keyword(s):  
Kinetic Mechanism ◽  
Fructose 1,6 Bisphosphatase ◽  
Amp Inhibition

scholarly journals Rabbit muscle fructose-1,6-bisphosphatase is phosphorylatedin vivo.

2003 ◽  
Vol 50 (1) ◽  
pp. 115-121 ◽  
Author(s):  
Dariusz Rakus ◽  
Marek Zarzycki ◽  
Andrzej Dzugaj
Keyword(s):  
Alkaline Phosphatase ◽  
Protein Kinase ◽  
Inorganic Phosphate ◽  
Kinetic Properties ◽  
Rabbit Muscle ◽  
Activity Regulation ◽  
Sds Page ◽  
Fructose 1,6 Bisphosphatase ◽  
Amp Inhibition ◽  
Kinase A

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 phosphorylated FBPase, and in the affinity for aldolase, which is three times lower for the dephosphorylated enzyme. Dephosphorylated FBPase can be a substrate for protein kinase A and the amount of phosphate incorporated per FBPase monomer can reach 2-3 molecules. Since interaction of muscle aldolase with muscle FBPase results in desensitisation of the latter toward AMP inhibition (Rakus & Dzugaj, 2000, Biochem. Biophys. Res. Commun. 275, 611-616), phosphorylation may be considered as a way of muscle FBPase activity regulation.

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