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 Unraveling multistate unfolding of pig kidney fructose-1,6-bisphosphatase using single tryptophan mutants

FEBS Journal ◽  
2007 ◽  
Vol 274 (20) ◽  
pp. 5337-5349 ◽  
Author(s):  
Heide C. Ludwig ◽  
Fabian N. Pardo ◽  
Joel L. Asenjo ◽  
Marco A. Maureira ◽  
Alejandro J. Yañez ◽  
...  
Keyword(s):  
Pig Kidney ◽  
Fructose 1,6 Bisphosphatase

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.

Subunit interactions in pig-kidney fructose-1,6-bisphosphatase: Binding of substrate induces a second class of site with lowered affinity and catalytic activity

2014 ◽  
Vol 1840 (6) ◽  
pp. 1798-1807 ◽  
Author(s):  
Joel L. Asenjo ◽  
Heide C. Ludwig ◽  
Cristian A. Droppelmann ◽  
Juan G. Cárcamo ◽  
Ilona I. Concha ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Subunit Interactions ◽  
Pig Kidney ◽  
Fructose 1,6 Bisphosphatase
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