Other names published for PGK1: phosphoglycerate kinase, YCR012W
PGK1 LITERATURE TOPICS
- Curated Literature
- Genetics/Cell Biology
- Nucleic Acid Information
- Gene Product Information
- Related Genes/Proteins
- Research Aids
- Genome-wide Analysis
- Proteome-wide Analysis
- Other Topics
- Additional Information
PGK1 - Substrates/Ligands/Cofactors (58)
| Reference | Other Genes Addressed |
|---|---|
| Fendt SM, et al. (2010) Tradeoff between enzyme and metabolite efficiency maintains metabolic homeostasis upon perturbations in enzyme capacity. Mol Syst Biol 6():356 | |
| Inoue R, et al. (2010) Large domain fluctuations on 50-ns timescale enable catalytic activity in phosphoglycerate kinase. Biophys J 99(7):2309-17 | |
| Irazusta V, et al. (2010) Yeast frataxin mutants display decreased superoxide dismutase activity crucial to promote protein oxidative damage. Free Radic Biol Med 48(3):411-420 | |
| Hurth C, et al. (2007) Enzymatic activity of immobilized yeast phosphoglycerate kinase. Biosens Bioelectron 22(11):2449-55 | |
| Kotsikorou E, et al. (2006) Bisphosphonate inhibition of phosphoglycerate kinase: quantitative structure-activity relationship and pharmacophore modeling investigation. J Med Chem 49(23):6692-703 | |
| Geerlof A, et al. (2005) Perturbation of yeast 3-phosphoglycerate kinase reaction mixtures with ADP: transient kinetics of formation of ATP from bound 1,3-bisphosphoglycerate. Biochemistry 44(45):14948-55 | |
| Varga A, et al. (2005) Correlation between conformational stability of the ternary enzyme-substrate complex and domain closure of 3-phosphoglycerate kinase. FEBS J 272(8):1867-85 | |
| Van Hoek P, et al. (2001) Human acylphosphatase cannot replace phosphoglycerate kinase in Saccharomyces cerevisiae. Antonie Van Leeuwenhoek 80(1):11-7 | |
| Gonzalez B, et al. (2000) Dynamic in vivo (31)P nuclear magnetic resonance study of Saccharomyces cerevisiae in glucose-limited chemostat culture during the aerobic-anaerobic shift. Yeast 16(6):483-97 | |
| Peter Smits H, et al. (2000) Simultaneous overexpression of enzymes of the lower part of glycolysis can enhance the fermentative capacity of Saccharomyces cerevisiae. Yeast 16(14):1325-34 | |
| Damaschun G, et al. (1999) Proteins can adopt totally different folded conformations. J Mol Biol 291(3):715-25 | |
| McHarg J, et al. (1999) Site-directed mutagenesis of proline 204 in the 'hinge' region of yeast phosphoglycerate kinase. Eur J Biochem 259(3):939-45 | |
| Raghunathan V, et al. (1999) Structural characterization of manganese(II)-nucleotide complexes bound to yeast 3-phosphoglycerate kinase: 13C relaxation measurements using [U-13C]ATP and [U-13C]ADP. Biochemistry 38(47):15597-605 | |
| Sherman MA, et al. (1997) An engineered amino-terminal domain of yeast phosphoglycerate kinase with native-like structure. Protein Sci 6(4):882-91 | |
| Cheung CW and Mas MT (1996) Substrate-induced conformational changes in yeast 3-phosphoglycerate kinase monitored by fluorescence of single tryptophan probes. Protein Sci 5(6):1144-9 | |
| Pappu KM and Serpersu EH (1994) Proton NMR studies of a large protein. pH, substrate titrations, and NOESY experiments with perdeuterated yeast phosphoglycerate kinase containing [1H]histidine residues. J Magn Reson B 105(2):157-66 | |
| Barber MD, et al. (1993) Site-directed mutagenesis of yeast phosphoglycerate kinase. Arginines 65, 121 and 168. FEBS Lett 320(3):193-7 | |
| Cioni P, et al. (1993) Tryptophan phosphorescence as a monitor of the solution structure of phosphoglycerate kinase from yeast. Biophys Chem 46(1):47-55 | |
| Damaschun G, et al. (1993) Cold denaturation-induced conformational changes in phosphoglycerate kinase from yeast. Biochemistry 32(30):7739-46 | |
| Vlasova II and Kuprin SP (1992) [Evaluation of distances in yeast phosphoglycerate kinase molecules using saturation effect ESR spectra at 77 K] Biofizika 37(5):927-34 | |
| Walker PA, et al. (1992) Characterisation of yeast phosphoglycerate kinase modified by mutagenesis at residue 21. Eur J Biochem 207(1):29-37 | |
| Desmadril M, et al. (1991) Conformational changes in yeast phosphoglycerate kinase upon ligand binding: fluorescence of a linked probe and chemical reactivity of genetically introduced cysteinyl residues. Proteins 10(4):315-24 | |
| Graham HC and Williams RJ (1991) The roles of ADP2- and Mg2+ in control steps of phosphoglycerate kinase. Eur J Biochem 197(1):81-91 | |
| Graham HC, et al. (1991) A proton-NMR study of a site-directed mutation (His388----Glu) in the interdomain region of yeast phosphoglycerate kinase. Implications for domain movement. Eur J Biochem 196(2):261-9 | |
| LaDine JR and Cross RL (1991) The adenine nucleotide-binding site on yeast 3-phosphoglycerate kinase. Affinity labeling of Lys-131 by pyridoxal 5'-diphospho-5'-adenosine. J Biol Chem 266(11):7194-8 | |
| Varley PG, et al. (1991) Resolution of the fluorescence of the buried tryptophan in yeast 3-phosphoglycerate kinase using succinimide. Biochim Biophys Acta 1077(1):19-24 | |
| Ballery N, et al. (1990) Introduction of internal cysteines as conformational probes in yeast phosphoglycerate kinase. Protein Eng 3(3):199-204 | |
| Fairbrother WJ, et al. (1990) An NMR study of anion binding to yeast phosphoglycerate kinase. Eur J Biochem 190(1):161-9 | |
| Fairbrother WJ, et al. (1990) The roles of ATP4- and Mg2+ in control steps of phosphoglycerate kinase. Eur J Biochem 190(2):407-14 | |
| Dryden DT and Pain RH (1989) Assignment of the heterogeneous static and time-resolved tryptophan fluorescence of 3-phosphoglycerate kinase. Biochim Biophys Acta 997(3):313-21 | |



