ENO2/YHR174W Literature Guide Help

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

ENO2 - Protein Sequence Features (23)

ReferenceOther Genes Addressed
Lesur A, et al.  (2012) Peptides quantification by liquid chromatography with matrix-assisted laser desorption/ionization and selected reaction monitoring detection. J Proteome Res 11(10):4972-82
Carroll KM, et al.  (2011) Absolute quantification of the glycolytic pathway in yeast: deployment of a complete QconCAT approach. Mol Cell Proteomics 10(12):M111.007633
Marino SM, et al.  (2010) Characterization of Surface-Exposed Reactive Cysteine Residues in Saccharomyces cerevisiae. Biochemistry 49(35):7709-21
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
Xie H, et al.  (2009) Characterization of protein impurities and site-specific modifications using peptide mapping with liquid chromatography and data independent acquisition mass spectrometry. Anal Chem 81(14):5699-708
Gomes RA, et al.  (2008) Protein glycation and methylglyoxal metabolism in yeast: finding peptide needles in protein haystacks. FEMS Yeast Res 8(1):174-81
Chakraborty AB, et al.  (2007) Use of an integrated MS - multiplexed MS/MS data acquisition strategy for high-coverage peptide mapping studies. Rapid Commun Mass Spectrom 21(5):730-44
Brandina I, et al.  (2006) Enolase takes part in a macromolecular complex associated to mitochondria in yeast. Biochim Biophys Acta 1757(9-10):1217-1228
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
Gomes RA, et al.  (2006) Yeast protein glycation in vivo by methylglyoxal. FEBS J 273(23):5273-87
Sims PA, et al.  (2003) Reverse protonation is the key to general acid-base catalysis in enolase. Biochemistry 42(27):8298-306
Vinarov DA and Nowak T  (1999) Role of His159 in yeast enolase catalysis. Biochemistry 38(37):12138-49
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
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
Norbeck J and Blomberg A  (1995) Gene linkage of two-dimensional polyacrylamide gel electrophoresis resolved proteins from isogene families in Saccharomyces cerevisiae by microsequencing of in-gel trypsin generated peptides. Electrophoresis 16(1):149-56
Borders CL Jr, et al.  (1994) A structural role for arginine in proteins: multiple hydrogen bonds to backbone carbonyl oxygens. Protein Sci 3(4):541-8
Verma M and Dutta SK  (1994) DNA sequences encoding enolase are remarkably conserved from yeast to mammals. Life Sci 55(12):893-9
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
Stec B and Lebioda L  (1990) Refined structure of yeast apo-enolase at 2.25 A resolution. J Mol Biol 211(1):235-48
Lebioda L, et al.  (1989) The structure of yeast enolase at 2.25-A resolution. An 8-fold beta + alpha-barrel with a novel beta beta alpha alpha (beta alpha)6 topology. J Biol Chem 264(7):3685-93
Sinha U and Brewer JM  (1986) Yeast enolase carboxyl modification using Woodward's reagent K. Biochem Cell Biol 64(10):970-5
Chin CC, et al.  (1981) The amino acid sequence of yeast enolase. Preparation and characterization of peptides produced by chemical and enzymatic fragmentation. J Biol Chem 256(3):1370-6
Hargrave PA and Wold F  (1971) Studies on yeast enolase. Quantitative end group analyses and the effect of exopeptidase digestion. J Biol Chem 246(9):2904-9