TPI1/YDR050C Literature Guide Help

Other names published for TPI1: triose-phosphate isomerase TPI1, YDR050C

TPI1 - Substrates/Ligands/Cofactors (17)

ReferenceOther Genes Addressed
Hernandez-Santoyo A, et al.  (2012) Effects of a buried cysteine-to-serine mutation on yeast triosephosphate isomerase structure and stability. Int J Mol Sci 13(8):10010-21
Gruning NM, et al.  (2011) Pyruvate Kinase Triggers a Metabolic Feedback Loop that Controls Redox Metabolism in Respiring Cells. Cell Metab 14(3):415-27
Fendt SM, et al.  (2010) Tradeoff between enzyme and metabolite efficiency maintains metabolic homeostasis upon perturbations in enzyme capacity. Mol Syst Biol 6():356
Go MK, et al.  (2010) Rescue of K12G Triosephosphate Isomerase by Ammonium Cations: The Reaction of an Enzyme in Pieces. J Am Chem Soc 132(38):13525-32
Go MK, et al.  (2010) Role of Lys-12 in catalysis by triosephosphate isomerase: a two-part substrate approach. Biochemistry 49(25):5377-89
Gonzalez-Mondragon E, et al.  (2007) Effect of a specific inhibitor on the unfolding and refolding kinetics of dimeric triosephosphate isomerase: establishing the dimeric and similarly structured nature of the main transition states on the forward and backward reactions. Biophys Chem 125(1):172-8
Gulotta M, et al.  (2007) Effects of cell volume regulating osmolytes on glycerol 3-phosphate binding to triosephosphate isomerase. Biochemistry 46(35):10055-62
Kong DC, et al.  (2007) [Simulation and analysis of ethanol concentration response to enzyme amount changes in Saccharomyces cerevisiae glycolysis pathway model] Sheng Wu Gong Cheng Xue Bao 23(2):332-6
Rozovsky S and McDermott AE  (2007) Substrate product equilibrium on a reversible enzyme, triosephosphate isomerase. Proc Natl Acad Sci U S A 104(7):2080-5
Massi F, et al.  (2006) Solution NMR and computer simulation studies of active site loop motion in triosephosphate isomerase. Biochemistry 45(36):10787-94
Mashego MR, et al.  (2005) Changes in the metabolome of Saccharomyces cerevisiae associated with evolution in aerobic glucose-limited chemostats. FEMS Yeast Res 5(4-5):419-30
Gonzalez-Mondragon E, et al.  (2004) Conserved cysteine 126 in triosephosphate isomerase is required not for enzymatic activity but for proper folding and stability. Biochemistry 43(11):3255-63
Desamero R, et al.  (2003) Active site loop motion in triosephosphate isomerase: T-jump relaxation spectroscopy of thermal activation. Biochemistry 42(10):2941-51
Jogl G, et al.  (2003) Optimal alignment for enzymatic proton transfer: structure of the Michaelis complex of triosephosphate isomerase at 1.2-A resolution. Proc Natl Acad Sci U S A 100(1):50-5
Rozovsky S and McDermott AE  (2001) The time scale of the catalytic loop motion in triosephosphate isomerase. J Mol Biol 310(1):259-70
Garza-Ramos G, et al.  (1996) Species-specific inhibition of homologous enzymes by modification of nonconserved amino acids residues. The cysteine residues of triosephosphate isomerase. Eur J Biochem 241(1):114-20
Maitra PK and Lobo Z  (1971) Control of glycolytic enzyme synthesis in yeast by products of the hexokinase reaction. J Biol Chem 246(2):489-99