ENO2/YHR174W Literature Guide Help

Other names published for ENO2: enolase, phosphopyruvate hydratase ENO2, YHR174W

ENO2 - Substrates/Ligands/Cofactors (38)

Results: 1 - 30 of 38 records
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ReferenceOther Genes Addressed
Moreno-Vargas LM, et al.  (2011) Thermal unfolding of apo- and holo-enolase from Saccharomyces cerevisiae: different mechanisms, similar activation enthalpies. Int J Biol Macromol 49(5):871-8
Fendt SM, et al.  (2010) Tradeoff between enzyme and metabolite efficiency maintains metabolic homeostasis upon perturbations in enzyme capacity. Mol Syst Biol 6():356
Moravcevic K, et al.  (2010) Kinase associated-1 domains drive MARK/PAR1 kinases to membrane targets by binding acidic phospholipids. Cell 143(6):966-77
De D, et al.  (2005) Inactive enzymatic mutant proteins (phosphoglycerate mutase and enolase) as sugar binders for ribulose-1,5-bisphosphate regeneration reactors. Microb Cell Fact 4(1):5
Kornblatt MJ, et al.  (2004) Use of hydrostatic pressure to produce 'native' monomers of yeast enolase. Eur J Biochem 271(19):3897-904
Sims PA, et al.  (2003) Reverse protonation is the key to general acid-base catalysis in enolase. Biochemistry 42(27):8298-306
Poyner RR, et al.  (2001) Role of metal ions in catalysis by enolase: an ordered kinetic mechanism for a single substrate enzyme. Biochemistry 40(27):8009-17
Cabiscol E, et al.  (2000) Oxidative stress promotes specific protein damage in Saccharomyces cerevisiae. J Biol Chem 275(35):27393-8
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
Teusink B, et al.  (2000) Can yeast glycolysis be understood in terms of in vitro kinetics of the constituent enzymes? Testing biochemistry. Eur J Biochem 267(17):5313-29
Vinarov DA and Nowak T  (1999) Role of His159 in yeast enolase catalysis. Biochemistry 38(37):12138-49
Vinarov DA and Nowak T  (1998) pH dependence of the reaction catalyzed by yeast Mg-enolase. Biochemistry 37(43):15238-46
Larsen TM, et al.  (1996) A carboxylate oxygen of the substrate bridges the magnesium ions at the active site of enolase: structure of the yeast enzyme complexed with the equilibrium mixture of 2-phosphoglycerate and phosphoenolpyruvate at 1.8 A resolution. Biochemistry 35(14):4349-58
Reed GH, et al.  (1996) Structural and mechanistic studies of enolase. Curr Opin Struct Biol 6(6):736-43
Lee BH and Nowak T  (1992) Influence of pH on the Mn2+ activation of and binding to yeast enolase: a functional study. Biochemistry 31(7):2165-71
Lee ME and Nowak T  (1992) 25Mg NMR studies of yeast enolase and rabbit muscle pyruvate kinase. Arch Biochem Biophys 293(2):264-73
Poyner RR and Reed GH  (1992) Structure of the bis divalent cation complex with phosphonoacetohydroxamate at the active site of enolase. Biochemistry 31(31):7166-73
al-Giery AG and Brewer JM  (1992) Characterization of the interaction of yeast enolase with polynucleotides. Biochim Biophys Acta 1159(2):134-40
Lebioda L and Stec B  (1991) Mechanism of enolase: the crystal structure of enolase-Mg2(+)-2-phosphoglycerate/phosphoenolpyruvate complex at 2.2-A resolution. Biochemistry 30(11):2817-22
Lebioda L, et al.  (1991) Inhibition of enolase: the crystal structures of enolase-Ca2(+)- 2-phosphoglycerate and enolase-Zn2(+)-phosphoglycolate complexes at 2.2-A resolution. Biochemistry 30(11):2823-7
Anderson VE and Cleland WW  (1990) Phosphonate analogue substrates for enolase. Biochemistry 29(46):10498-503
Kornblatt MJ and Musil R  (1990) The inhibition of yeast enolase by Li+ and Na+1. Arch Biochem Biophys 277(2):301-5
Entian KD, et al.  (1987) Studies on the regulation of enolases and compartmentation of cytosolic enzymes in Saccharomyces cerevisiae. Biochim Biophys Acta 923(2):214-21
Sinha U and Brewer JM  (1986) Yeast enolase carboxyl modification using Woodward's reagent K. Biochem Cell Biol 64(10):970-5
Spencer SG, et al.  (1985) Cadmium(II)-113 NMR studies of the mechanism of metal ion activation of yeast enolase. J Inorg Biochem 24(1):47-57
Anderson VE, et al.  (1984) Reaction intermediate analogues for enolase. Biochemistry 23(12):2779-86
Rose SL, et al.  (1984) Kinetic and physical properties of Co2+ enolase. J Biol Chem 259(7):4405-13
Spencer SG and Brewer JM  (1984) Activation of yeast enolase by Cd(II). J Inorg Biochem 20(1):39-52
Brewer JM, et al.  (1983) Studies of activating and nonactivating metal ion binding to yeast enolase. J Inorg Biochem 19(3):255-67
Results: 1 - 30 of 38 records
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