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2. The stereochemical course of phosphoryl transfer catalysed by Bacillus stearothermophilus and rabbit skeletal-muscle phosphofructokinase with a chiral [16O,17O,18O]phosphate ester. Jarvest RL; Lowe G; Potter BV Biochem J; 1981 Nov; 199(2):427-32. PubMed ID: 6462132 [TBL] [Abstract][Full Text] [Related]
3. Stereochemical course of a phosphokinase using a chiral [18O]phosphorothioate. Comparison with the transfer of a chiral [16O,17O,18O]phosphoryl group. Pliura DH; Schomburg D; Richard JP; Frey PA; Knowles JR Biochemistry; 1980 Jan; 19(2):325-9. PubMed ID: 6243477 [TBL] [Abstract][Full Text] [Related]
4. Evidence that catalysis by yeast inorganic pyrophosphatase proceeds by direct phosphoryl transfer to water and not via a phosphoryl enzyme intermediate. Gonzalez MA; Webb MR; Welsh KM; Cooperman BS Biochemistry; 1984 Feb; 23(5):797-801. PubMed ID: 6143570 [TBL] [Abstract][Full Text] [Related]
5. Interaction of fructose 2,6-bisphosphate and AMP with fructose-1,6-bisphosphatase as studied by nuclear magnetic resonance spectroscopy. Liu F; Fromm HJ J Biol Chem; 1988 Jul; 263(19):9122-8. PubMed ID: 2837477 [TBL] [Abstract][Full Text] [Related]
6. The stereochemical course of yeast hexokinase-catalysed phosphoryl transfer by using adenosine 5'[gamma(S)-16O,17O,18O]triphosphate as substrate. Lowe G; Potter BV Biochem J; 1981 Oct; 199(1):227-33. PubMed ID: 7039616 [TBL] [Abstract][Full Text] [Related]
7. The site of substrate and fructose 2,6-bisphosphate binding to rabbit liver fructose-1,6-bisphosphatase. Liu F; Roy M; Fromm HJ Biochem Biophys Res Commun; 1989 Jun; 161(2):689-95. PubMed ID: 2544170 [TBL] [Abstract][Full Text] [Related]
8. Regulation of rabbit liver fructose-1,6-bisphosphatase by metals, nucleotides, and fructose 2,6-bisphosphate as determined from fluorescence studies. Scheffler JE; Fromm HJ Biochemistry; 1986 Oct; 25(21):6659-65. PubMed ID: 3024716 [TBL] [Abstract][Full Text] [Related]
9. 31P nuclear magnetic resonance spectroscopy studies of substrate and product binding to fructose-1,6-bisphosphatase. Liu F; Fromm HJ J Biol Chem; 1991 Jun; 266(18):11774-8. PubMed ID: 1646815 [TBL] [Abstract][Full Text] [Related]
10. The stereochemical course of phosphoric residue transfer during the myosin ATPase reaction. Webb MR; Trentham DR J Biol Chem; 1980 Sep; 255(18):8629-32. PubMed ID: 6447698 [TBL] [Abstract][Full Text] [Related]
11. The stereochemical course of phosphoryl transfer catalysed by glucokinase. Pollard-Knight D; Potter BV; Cullis PM; Lowe G; Cornish-Bowden A Biochem J; 1982 Feb; 201(2):421-3. PubMed ID: 6896275 [TBL] [Abstract][Full Text] [Related]
12. The stereochemical course of phospho group transfer catalyzed by rat liver 6-phosphofructo-2-kinase. Kountz PD; Freeman S; Cook AG; el-Maghrabi MR; Knowles JR; Pilkis SJ J Biol Chem; 1988 Nov; 263(31):16069-72. PubMed ID: 2972703 [TBL] [Abstract][Full Text] [Related]
13. Specific, reversible inactivation of phosphofructokinase by fructose-1,6-bisphosphatase. Involvement of adenosine 5'-triphosphate, oleate, and 3-phosphoglycerate. Proffitt RT; Sankaran L Biochemistry; 1976 Jun; 15(13):2918-25. PubMed ID: 181051 [TBL] [Abstract][Full Text] [Related]