Spreadsheet: 57edf586-0b34-4a0a-a1c6-981af60782b3
Sheet: Sheet1

Table S6. Kinetic parameters and conservation scores of mutation sites with experimental references | Unnamed: 1 | Unnamed: 2 | Unnamed: 3 | Unnamed: 4 | Unnamed: 5 | Unnamed: 6 | Unnamed: 7 | Unnamed: 8 | Unnamed: 9
Human Liver FBPase | Mutation | Conservation | Turnover No. | [NAME] | Catalytic efficiency | Ki AMP | [NAME] | Reference
 | Wild type | - | 6.5 | 1.6 | 4.0625 | 9 | 3A29:A | Gidh-Jain, M., [NAME], et [NAME]. (1994). "The allosteric site of human liver fructose-1,6-bisphosphatase. Analysis of six AMP site mutants based on the crystal structure." J Biol Chem 269(44): 27732-27738.
 | A24F | 0.206 | 6 | 2.5 | 2.4 | 187
 | L30F | 0.39 | 6.7 | 2.9 | 2.310344827586207 | 3
 | M177A | 0.399 | 7 | 1.5 | 4.666666666666667 | 9
 | R140A | 0.218 | 8.1 | 2.6 | 3.115384615384615 | 62
 | T31S | 0.48 | 6.2 | 1.7 | 3.647058823529412 | 42
 | T31A | 0.48 | 5.9 | 2 | 2.95 | 1100
 | Y113F | 0.685 | 6.4 | 1.6 | 4 | > 10mM
Porcine FBPase | Mutation |  | kcat | [NAME] | Catalytic efficiency | Ki AMP |  | Reference
 | Wild type | - | 18.4 | 1.7 | 10.8235294117647 | 3.2 | 1CQN:A | Giroux, E., [NAME], et [NAME]. (1994). "Shared active sites of fructose-1,6-bisphosphatase. Arginine 243 mediates substrate binding and fructose 2,6-bisphosphate inhibition." J Biol Chem 269(50): 31404-31409.
 | [NAME] | 0.977 | 8.5 | 35 | 0.2428571428571429 | 19
Porcine Liver FBPase | Mutation |  | kcat | [NAME] | Catalytic efficiency | Ki AMP | [NAME] | Reference
 | Wild type | - | 18 | 3.51 | 5.128205128205129 | 4.52 | 1CQN:A | Shyur, L. F., [NAME], et [NAME]. (1996). "Biochemical properties of mutant and wild-type fructose-1,6-bisphosphatases are consistent with the coupling of intra- and intersubunit conformational changes in the T- and R-state transition." J Biol Chem 271(52): 33301-33307.
 | Q32L | 0.31 | 32.1 | 1.42 | 22.6056338028169 | 37.9
 | K42E | 0.831 | 19.3 | 1.67 | 11.55688622754491 | 17.7
 | K42T | 0.831 | 18.3 | 1.53 | 11.96078431372549 | 12.1
 | I190T | 0.268 | 21.1 | 1.81 | 11.65745856353591 | 10
 | G191A | 0.938 | 23.7 | 0.84 | 28.21428571428572 | 14.7
Porcine Kidney FBPase | Mutation | Conservation | kcat | [NAME] | Catalytic efficiency | Ki AMP |  | Reference
 | Wild type | - | 21 | 1.4 | 15 | 2.8 | 1CQN:A | [NAME], [NAME], B. Stec, et [NAME]. (1996). "Evidence for an active T-state pig kidney fructose 1,6-bisphosphatase: interface residue Lys-42 is important for allosteric inhibition and AMP cooperativity." [NAME]): 2333-2342.
 | K42A | 0.831 | 10.8 | 3.3 | 3.272727272727273 | 18
Porcine Liver FBPase | Mutation |  | kcat | [NAME] | Catalytic efficiency | Ki AMP |  | Reference
pH 7.5 | Wild type | - | 21 | 2.8 | 7.500000000000001 | 20.5 | 1CQN:A | [NAME], F. T., [NAME], et [NAME]. (1998). "Directed mutations in the poorly defined region of porcine liver fructose-1,6-bisphosphatase significantly affect catalysis and the mechanism of AMP inhibition." J Biol Chem 273(28): 17511-17516. | Directed mutations in the poorly defined region of porcine liver fructose-1,6-bisphosphatase significantly affect catalysis and the mechanism of AMP inhibition.
 | K71A | 0.676 | 16 | 2.8 | 5.714285714285714 | 189
 | D68E | 0.816 | 6.4 | 1.31 | 4.885496183206107 | 27.2
pH 8.5 | Wild type | - | 9.1 | 2.2 | 4.136363636363636 | 53.7
 | D74A | 0.977 | 0.0004 | ND | ND | ND
 | D74N | 0.977 | 0.01 | ND | ND | ND
 | D74E | 0.977 | 1.2 | 1.03 | 1.16504854368932 | 5.25
 | N64A | 0.998 | 7.1 | 1.42 | 5 | 12.7
 | N64Q | 0.998 | 5.4 | 1.7 | 3.176470588235294 | 14.1
Porcine Liver FBPase | Mutation |  | kcat | [NAME] | Catalytic efficiency | Ki AMP |  | Reference
 | Wild type | - | 22 | 1.75 | 12.57142857142857 | 1.61 | 1CQN:A | [NAME], [NAME], [NAME], et [NAME]. (2000). "Tryptophan fluorescence reveals the conformational state of a dynamic loop in recombinant porcine fructose-1,6-bisphosphatase." Biochemistry 39(36): 11100-11106.
 | Y57W | 0.197 | 24 | 3.39 | 7.079646017699115 | 8.5
Porcine Kidney FBPase | Mutation |  | kcat | [NAME] | Catalytic efficiency | Ki AMP |  | Reference
 | Wild type | - | 21 | 1.4 | 15 | 2.8 | 1CQN:A | Kelley-Loughnane, N. and [NAME] (2001). "Binding of AMP to two of the four subunits of pig kidney fructose-1,6-bisphosphatase induces the allosteric transition." Proteins 44(3): 255-261.
 | E98Q | 0.959 | 0.013 | 10.2 | 0.001274509803921569 | 5.5
 | Y113F | 0.777 | 16.2 | 4.5 | 3.6 | 4400
Porcine Kidney FBPase | Mutation |  | kcat | [NAME] | Catalytic efficiency | Ki AMP |  | Reference
 | Wild type | - | 21 | 1.4 | 15 | 2.8 | 1CQN:A | Kelley-Loughnane, N. and [NAME] (2001). "AMP inhibition of pig kidney fructose-1,6-bisphosphatase." [NAME] 1548(1): 66-71.
 | K112Q | 0.37 | 22 | 5.6 | 3.928571428571429 | 3600
 | Y113F | 0.777 | 16.2 | 4.5 | 3.6 | 4400
Porcine FBPase | Mutation |  | kcat | [NAME] | Catalytic efficiency | Ki AMP |  | Reference
 | Wild type | - | 22 | 1.8 | 12.22222222222222 | 1.61 | 1CQN:A | [NAME], [NAME], [NAME], et [NAME]. (2001). "The N-terminal segment of recombinant porcine fructose-1,6-bisphosphatase participates in the allosteric regulation of catalysis." J Biol Chem 276(9): 6119-6124.
 | F6W | 0.102 | 18 | 1.58 | 11.39240506329114 | 2.87
 | I10M | 0.286 | 15.3 | 2 | 7.65 | 2.85
 | I10D | 0.286 | 16.7 | 1.2 | 13.91666666666667 | 2.75
Porcine Liver FBPase | Mutation |  | kcat | [NAME] | Catalytic efficiency | Ki AMP |  | Reference
 | Wild type | - | 22 | 1.8 | 12.22222222222222 | 1.61 | 1CQN:A | [NAME], [NAME], [NAME], et [NAME]. (2002). "Hybrid tetramers of porcine liver fructose-1,6-bisphosphatase reveal multiple pathways of allosteric inhibition." J Biol Chem 277(18): 15539-15545.
 | Y57W | 0.197 | 24 | 3.4 | 7.058823529411764 | 8.5
Porcine FBPase | Mutation |  | kcat | [NAME] | Catalytic efficiency | Ki AMP |  | Reference
 | Wild type | - | 22 | 1.8 | 12.22222222222222 | 1.6 | 1CQN:A | [NAME], [NAME], [NAME], et [NAME]. (2004). "Origin of cooperativity in the activation of fructose-1,6-bisphosphatase by Mg2+." J Biol Chem 279(18): 18481-18487.
 | E97A | 0.959 | 5.3 | 1.8 | 2.944444444444444 | 3.8
 | D118A | 0.977 | 5.9 | 1.3 | 4.538461538461538 | 6.9
 | D121A | 0.977 | 5.8 | 1.1 | 5.272727272727272 | 7.4
Porcine FBPase | Mutation |  | kcat | [NAME] | Catalytic efficiency | Ki AMP |  | Reference
 | Wild type | - | 20 | 1.2 | 16.66666666666667 | 0.6 | 1CQN:A | Iancu, C. V., [NAME], et [NAME]. (2005). "R-state AMP complex reveals initial steps of the quaternary transition of fructose-1,6-bisphosphatase." J Biol Chem 280(20): 19737-19745.
 | A54L | 0.277 | 11.3 | 0.94 | 12.02127659574468 | 3000
S. enterica FBPase | Mutation |  | kcat | [NAME] | Catalytic efficiency | Ki AMP |  | Reference
 | Wild type | - | 24.3 | 10.8 | 2.25 | 1.31 | 2Q8N:A | [NAME], M. J., [NAME], et [NAME]. (2006). "Inhibition of fructose-1,6-bisphosphatase by aminoimidazole carboxamide ribotide prevents growth of Salmonella enterica purH mutants on glycerol." J Biol Chem 281(45): 33892-33899.
 | T19I | 0.39 | 26.8 | 9.5 | 2.821052631578947 | 155
 | G20D | 0.463 | 15 | 20.1 | 0.7462686567164178 | 1360
 | T23I | 0.547 | 20.4 | 8.5 | 2.4 | 1450