132 related articles for article (PubMed ID: 9651342)
1. Directed mutations in the poorly defined region of porcine liver fructose-1,6-bisphosphatase significantly affect catalysis and the mechanism of AMP inhibition.
Kurbanov FT; Choe JY; Honzatko RB; Fromm HJ
J Biol Chem; 1998 Jul; 273(28):17511-6. PubMed ID: 9651342
[TBL] [Abstract][Full Text] [Related]
2. A study of subunit interface residues of fructose-1,6-bisphosphatase by site-directed mutagenesis: effects on AMP and Mg2+ affinities.
Shyur LF; Aleshin AE; Fromm HJ
Biochemistry; 1996 Jun; 35(23):7492-8. PubMed ID: 8652527
[TBL] [Abstract][Full Text] [Related]
3. 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
[TBL] [Abstract][Full Text] [Related]
4. Mutation of arginine 276 to methionine changes Mg2+ cooperativity and the kinetic mechanism of fructose-1,6-bisphosphatase.
Zhang R; Fromm HJ
Biochemistry; 1995 Jun; 34(25):8190-5. PubMed ID: 7794933
[TBL] [Abstract][Full Text] [Related]
5. Site-directed mutagenesis of residues at subunit interfaces of porcine fructose-1,6-bisphosphatase.
Shyur LF; Aleshin AE; Honzatko RB; Fromm HJ
J Biol Chem; 1996 Feb; 271(6):3005-10. PubMed ID: 8621693
[TBL] [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; 269(8):5554-8. PubMed ID: 7907084
[TBL] [Abstract][Full Text] [Related]
7. Importance of the dimer-dimer interface for allosteric signal transduction and AMP cooperativity of pig kidney fructose-1,6-bisphosphatase. Site-specific mutagenesis studies of Glu-192 and Asp-187 residues on the 190's loop.
Lu G; Giroux EL; Kantrowitz ER
J Biol Chem; 1997 Feb; 272(8):5076-81. PubMed ID: 9030572
[TBL] [Abstract][Full Text] [Related]
8. Site-directed mutagenesis of the substrate binding site of porcine fructose-1,6-bisphosphatase.
Shyur LF; Zhang R; Fromm HJ
Arch Biochem Biophys; 1995 May; 319(1):123-7. PubMed ID: 7771775
[TBL] [Abstract][Full Text] [Related]
9. 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; 275(39):29986-92. PubMed ID: 10896931
[TBL] [Abstract][Full Text] [Related]
10. The allosteric site of human liver fructose-1,6-bisphosphatase. Analysis of six AMP site mutants based on the crystal structure.
Gidh-Jain M; Zhang Y; van Poelje PD; Liang JY; Huang S; Kim J; Elliott JT; Erion MD; Pilkis SJ; Raafat el-Maghrabi M
J Biol Chem; 1994 Nov; 269(44):27732-8. PubMed ID: 7961695
[TBL] [Abstract][Full Text] [Related]
11. Major changes in the kinetic mechanism of AMP inhibition and AMP cooperativity attend the mutation of Arg49 in fructose-1,6-bisphosphatase.
Shyur LF; Poland BW; Honzatko RB; Fromm HJ
J Biol Chem; 1997 Oct; 272(42):26295-9. PubMed ID: 9334199
[TBL] [Abstract][Full Text] [Related]
12. 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.
Shyur LF; Aleshin AE; Honzatko RB; Fromm HJ
J Biol Chem; 1996 Dec; 271(52):33301-7. PubMed ID: 8969189
[TBL] [Abstract][Full Text] [Related]
13. The N-terminal segment of recombinant porcine fructose-1,6-bisphosphatase participates in the allosteric regulation of catalysis.
Nelson SW; Kurbanov FT; Honzatko RB; Fromm HJ
J Biol Chem; 2001 Mar; 276(9):6119-24. PubMed ID: 11096109
[TBL] [Abstract][Full Text] [Related]
14. Different sensitivities of mutants and chimeric forms of human muscle and liver fructose-1,6-bisphosphatases towards AMP.
Rakus D; Tillmann H; Wysocki R; Ulaszewski S; Eschrich K; Dzugaj A
Biol Chem; 2003 Jan; 384(1):51-8. PubMed ID: 12674499
[TBL] [Abstract][Full Text] [Related]
15. Characterization of recombinant fructose-1,6-bisphosphatase gene mutations: evidence of inhibition/activation of FBPase protein by gene mutation.
Topaz G; Epiter-Smith V; Robalo C; Emad M; Ford V; Daley J; Byron J; Stieglitz KA
Biosci Rep; 2019 Feb; 39(2):. PubMed ID: 30683805
[TBL] [Abstract][Full Text] [Related]
16. AMP inhibition of pig kidney fructose-1,6-bisphosphatase.
Kelley-Loughnane N; Kantrowitz ER
Biochim Biophys Acta; 2001 Jul; 1548(1):66-71. PubMed ID: 11451439
[TBL] [Abstract][Full Text] [Related]
17. The allosteric properties of rat liver fructose-1,6-bisphosphatase.
Meek DW; Nimmo HG
Biochem J; 1984 Aug; 222(1):131-8. PubMed ID: 6089752
[TBL] [Abstract][Full Text] [Related]
18. Fructose-1,6-bisphosphatase: arginine-22 is involved in stabilization of the T allosteric state.
Lu G; Williams MK; Giroux EL; Kantrowitz ER
Biochemistry; 1995 Oct; 34(41):13272-7. PubMed ID: 7577911
[TBL] [Abstract][Full Text] [Related]
19. Glycine 122 is essential for cooperativity and binding of Mg2+ to porcine fructose-1,6-bisphosphatase.
Zhang R; Chen L; Villeret V; Fromm HJ
J Biol Chem; 1995 Jan; 270(1):54-8. PubMed ID: 7814419
[TBL] [Abstract][Full Text] [Related]
20. Glutamic acid residue 98 is critical for catalysis in pig kidney fructose-1,6-bisphosphatase.
Kelley N; Giroux EL; Lu G; Kantrowitz ER
Biochem Biophys Res Commun; 1996 Feb; 219(3):848-52. PubMed ID: 8645268
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]