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2. 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. Cárcamo JG, Yañez AJ, Ludwig HC, León O, Pinto RO, Reyes AM, Slebe JC. Eur J Biochem; 2000 Apr; 267(8):2242-51. PubMed ID: 10759847 [Abstract] [Full Text] [Related]
6. Replacement of glutamic acid 29 with glutamine leads to a loss of cooperativity for AMP with porcine fructose-1,6-bisphosphatase. Chen M, Chen L, Fromm HJ. J Biol Chem; 1994 Feb 25; 269(8):5554-8. PubMed ID: 7907084 [Abstract] [Full Text] [Related]
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12. Mutations in the hinge of a dynamic loop broadly influence functional properties of fructose-1,6-bisphosphatase. Nelson SW, Choe JY, Honzatko RB, Fromm HJ. J Biol Chem; 2000 Sep 29; 275(39):29986-92. PubMed ID: 10896931 [Abstract] [Full Text] [Related]
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15. Evidence for an active T-state pig kidney fructose 1,6-bisphosphatase: interface residue Lys-42 is important for allosteric inhibition and AMP cooperativity. Lu G, Stec B, Giroux EL, Kantrowitz ER. Protein Sci; 1996 Nov 20; 5(11):2333-42. PubMed ID: 8931152 [Abstract] [Full Text] [Related]
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