ENO2/YHR174W Literature Guide Help

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

ENO2 - Function/Process (42)

ReferenceOther Genes Addressed
Lee SH, et al.  (2011) Global organization of protein complexome in the yeast Saccharomyces cerevisiae. BMC Syst Biol 5(1):126
Rossignol T, et al.  (2009) The proteome of a wine yeast strain during fermentation, correlation with the transcriptome. J Appl Microbiol 107(1):47-55
Gomes RA, et al.  (2008) Protein glycation in vivo: functional and structural effects on yeast enolase. Biochem J 416(3):317-26
Albers E, et al.  (2007) Effect of Nutrient Starvation on the Cellular Composition and Metabolic Capacity of Saccharomyces cerevisiae. Appl Environ Microbiol 73(15):4839-48
Magherini F, et al.  (2007) Protein expression profiles in Saccharomyces cerevisiae during apoptosis induced by H(2)O(2). Proteomics 7(9):1434-45
Pal-Bhowmick I, et al.  (2007) Differential susceptibility of Plasmodium falciparum versus yeast and mammalian enolases to dissociation into active monomers. FEBS J 274(8):1932-45
Decker BL and Wickner WT  (2006) Enolase activates homotypic vacuole fusion and protein transport to the vacuole in yeast. J Biol Chem 281(20):14523-8
Entelis N, et al.  (2006) A glycolytic enzyme, enolase, is recruited as a cofactor of tRNA targeting toward mitochondria in Saccharomyces cerevisiae. Genes Dev 20(12):1609-20
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
Teixeira MC, et al.  (2005) A proteome analysis of the yeast response to the herbicide 2,4-dichlorophenoxyacetic acid. Proteomics 5(7):1889-901
Hannaert V, et al.  (2003) Kinetic characterization, structure modelling studies and crystallization of Trypanosoma brucei enolase. Eur J Biochem 270(15):3205-13
Shenton D and Grant CM  (2003) Protein S-thiolation targets glycolysis and protein synthesis in response to oxidative stress in the yeast Saccharomyces cerevisiae. Biochem J 374(Pt 2):513-9
Nilsson A, et al.  (2001) Fermentative capacity after cold storage of baker's yeast is dependent on the initial physiological state but not correlated to the levels of glycolytic enzymes. Int J Food Microbiol 71(2-3):111-24
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
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
Poyner RR, et al.  (1996) Toward identification of acid/base catalysts in the active site of enolase: comparison of the properties of K345A, E168Q, and E211Q variants. Biochemistry 35(5):1692-9
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
Stec B and Lebioda L  (1990) Refined structure of yeast apo-enolase at 2.25 A resolution. J Mol Biol 211(1):235-48