[1]
|
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6256394 [NCBI, ExPASy, EBI, Israel, Japan]
Holland M.J.,
Holland J.P.,
Thill G.P.,
Jackson K.A.;
"The primary structures of two yeast enolase genes. Homology between the 5' noncoding flanking regions of yeast enolase and glyceraldehyde-3-phosphate dehydrogenase genes.";
J. Biol. Chem. 256:1385-1395(1981).
|
[2]
|
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
DOI=10.1002/(SICI)1097-0061(19970330)13:4<369::AID-YEA81>3.3.CO;2-M; PubMed=9133741 [NCBI, ExPASy, EBI, Israel, Japan]
Mazzoni C.,
Ruzzi M.,
Rinaldi T.,
Solinas F.,
Montebove F.,
Frontali L.;
"Sequence analysis of a 10.5 kb DNA fragment from the yeast chromosome VII reveals the presence of three new open reading frames and of a tRNAThr gene.";
Yeast 13:369-372(1997).
|
[3]
|
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=9169869 [NCBI, ExPASy, EBI, Israel, Japan]
Tettelin H.,
Agostoni-Carbone M.L.,
Albermann K.,
Albers M.,
Arroyo J.,
Backes U.,
Barreiros T.,
Bertani I.,
Bjourson A.J.,
Brueckner M.,
Bruschi C.V.,
Carignani G.,
Castagnoli L.,
Cerdan E.,
Clemente M.L.,
Coblenz A.,
Coglievina M.,
Coissac E.,
Defoor E., ![]()
Del Bino S.,
Delius H.,
Delneri D.,
de Wergifosse P.,
Dujon B.,
Durand P.,
Entian K.-D.,
Eraso P.,
Escribano V.,
Fabiani L.,
Fartmann B.,
Feroli F.,
Feuermann M.,
Frontali L.,
Garcia-Gonzalez M.,
Garcia-Saez M.I.,
Goffeau A.,
Guerreiro P.,
Hani J.,
Hansen M.,
Hebling U.,
Hernandez K.,
Heumann K.,
Hilger F.,
Hofmann B.,
Indge K.J.,
James C.M.,
Klima R.,
Koetter P.,
Kramer B.,
Kramer W.,
Lauquin G.,
Leuther H.,
Louis E.J.,
Maillier E.,
Marconi A.,
Martegani E.,
Mazon M.J.,
Mazzoni C.,
McReynolds A.D.K.,
Melchioretto P.,
Mewes H.-W.,
Minenkova O.,
Mueller-Auer S.,
Nawrocki A.,
Netter P.,
Neu R.,
Nombela C.,
Oliver S.G.,
Panzeri L.,
Paoluzi S.,
Plevani P.,
Portetelle D.,
Portillo F.,
Potier S.,
Purnelle B.,
Rieger M.,
Riles L.,
Rinaldi T.,
Robben J.,
Rodrigues-Pousada C.,
Rodriguez-Belmonte E.,
Rodriguez-Torres A.M.,
Rose M.,
Ruzzi M.,
Saliola M.,
Sanchez-Perez M.,
Schaefer B.,
Schaefer M.,
Scharfe M.,
Schmidheini T.,
Schreer A.,
Skala J.,
Souciet J.-L.,
Steensma H.Y.,
Talla E.,
Thierry A.,
Vandenbol M.,
van der Aart Q.J.M.,
Van Dyck L.,
Vanoni M.,
Verhasselt P.,
Voet M.,
Volckaert G.,
Wambutt R.,
Watson M.D.,
Weber N.,
Wedler E.,
Wedler H.,
Wipfli P.,
Wolf K.,
Wright L.F.,
Zaccaria P.,
Zimmermann M.,
Zollner A.,
Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
Nature 387:81-84(1997).
|
[4]
|
PROTEIN SEQUENCE OF 2-437.
PubMed=7005235 [NCBI, ExPASy, EBI, Israel, Japan]
Chin C.C.Q.,
Brewer J.M.,
Wold F.;
"The amino acid sequence of yeast enolase.";
J. Biol. Chem. 256:1377-1384(1981).
|
[5]
|
PROTEIN SEQUENCE OF 2-12.
STRAIN=ATCC 26786 / X2180-1A;
Sanchez J.-C.,
Golaz O.,
Schaller D.,
Morch F.,
Frutiger S.,
Hughes G.J.,
Appel R.D.,
Deshusses J.,
Hochstrasser D.F.;
Submitted (AUG-1995) to UniProtKB.
|
[6]
|
PROTEIN SEQUENCE OF 30-47.
STRAIN=ATCC 204508 / S288c;
PubMed=7895733 [NCBI, ExPASy, EBI, Israel, Japan]
Garrels J.I.,
Futcher B.,
Kobayashi R.,
Latter G.I.,
Schwender B.,
Volpe T.,
Warner J.R.,
McLaughlin C.S.;
"Protein identifications for a Saccharomyces cerevisiae protein database.";
Electrophoresis 15:1466-1486(1994).
|
[7]
|
PROTEIN SEQUENCE OF 69-79.
STRAIN=ATCC 38531 / Y41;
PubMed=7737086 [NCBI, ExPASy, EBI, Israel, Japan]
Norbeck J.,
Blomberg A.;
"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 16:149-156(1995).
|
[8]
|
MUTAGENESIS OF LYS-346.
DOI=10.1021/bi952186y; PubMed=8634301 [NCBI, ExPASy, EBI, Israel, Japan]
Poyner R.R.,
Laughlin L.T.,
Sowa G.A.,
Reed G.H.;
"Toward identification of acid/base catalysts in the active site of enolase: comparison of the properties of K345A, E168Q, and E211Q variants.";
Biochemistry 35:1692-1699(1996).
|
[9]
|
MUTAGENESIS OF HIS-160.
DOI=10.1006/bbrc.2000.3618; PubMed=11027610 [NCBI, ExPASy, EBI, Israel, Japan]
Brewer J.M.,
Holland M.J.,
Lebioda L.;
"The H159A mutant of yeast enolase 1 has significant activity.";
Biochem. Biophys. Res. Commun. 276:1199-1202(2000).
|
[10]
|
SUBCELLULAR LOCATION.
DOI=10.1021/bi010277r; PubMed=11502169 [NCBI, ExPASy, EBI, Israel, Japan]
Grandier-Vazeille X.,
Bathany K.,
Chaignepain S.,
Camougrand N.,
Manon S.,
Schmitter J.-M.;
"Yeast mitochondrial dehydrogenases are associated in a supramolecular complex.";
Biochemistry 40:9758-9769(2001).
|
[11]
|
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND MASS SPECTROMETRY.
DOI=10.1038/nbt0302-301; PubMed=11875433 [NCBI, ExPASy, EBI, Israel, Japan]
Ficarro S.B.,
McCleland M.L.,
Stukenberg P.T.,
Burke D.J.,
Ross M.M.,
Shabanowitz J.,
Hunt D.F.,
White F.M.;
"Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae.";
Nat. Biotechnol. 20:301-305(2002).
|
[12]
|
MUTAGENESIS OF HIS-160 AND ASN-208.
DOI=10.1023/A:1025390123761; PubMed=13678299 [NCBI, ExPASy, EBI, Israel, Japan]
Brewer J.M.,
Glover C.V.,
Holland M.J.,
Lebioda L.;
"Enzymatic function of loop movement in enolase: preparation and some properties of H159N, H159A, H159F, and N207A enolases.";
J. Protein Chem. 22:353-361(2003).
|
[13]
|
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S.,
Huh W.-K.,
Bower K.,
Howson R.W.,
Belle A.,
Dephoure N.,
O'Shea E.K.,
Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
|
[14]
|
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10 AND SER-188, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M400219-MCP200; PubMed=15665377 [NCBI, ExPASy, EBI, Israel, Japan]
Gruhler A.,
Olsen J.V.,
Mohammed S.,
Mortensen P.,
Faergeman N.J.,
Mann M.,
Jensen O.N.;
"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway.";
Mol. Cell. Proteomics 4:310-327(2005).
|
[15]
|
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, AND MASS SPECTROMETRY.
DOI=10.1021/pr060559j; PubMed=17330950 [NCBI, ExPASy, EBI, Israel, Japan]
Li X.,
Gerber S.A.,
Rudner A.D.,
Beausoleil S.A.,
Haas W.,
Villen J.,
Elias J.E.,
Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
|
[16]
|
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-119 AND SER-404, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0607084104; PubMed=17287358 [NCBI, ExPASy, EBI, Israel, Japan]
Chi A.,
Huttenhower C.,
Geer L.Y.,
Coon J.J.,
Syka J.E.P.,
Bai D.L.,
Shabanowitz J.,
Burke D.J.,
Troyanskaya O.G.,
Hunt D.F.;
"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
|
[17]
|
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104; SER-188 AND SER-404, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0701622104; PubMed=17563356 [NCBI, ExPASy, EBI, Israel, Japan]
Smolka M.B.,
Albuquerque C.P.,
Chen S.H.,
Zhou H.;
"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases.";
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
|
[18]
|
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-14; SER-37; SER-40; THR-41; SER-96; SER-104; SER-143; SER-188 AND THR-324, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P.,
Smolka M.B.,
Payne S.H.,
Bafna V.,
Eng J.,
Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
|
[19]
|
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
DOI=10.1038/333683a0; PubMed=3374614 [NCBI, ExPASy, EBI, Israel, Japan]
Lebioda L.,
Stec B.;
"Crystal structure of enolase indicates that enolase and pyruvate kinase evolved from a common ancestor.";
Nature 333:683-686(1988).
|
[20]
|
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
PubMed=2645275 [NCBI, ExPASy, EBI, Israel, Japan]
Lebioda L.,
Stec B.,
Brewer J.M.;
"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. 264:3685-3693(1989).
|
[21]
|
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
DOI=10.1016/0022-2836(90)90023-F; PubMed=2405163 [NCBI, ExPASy, EBI, Israel, Japan]
Stec B.,
Lebioda L.;
"Refined structure of yeast apo-enolase at 2.25-A resolution.";
J. Mol. Biol. 211:235-248(1990).
|
[22]
|
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND MAGNESIUM IONS.
DOI=10.1021/bi952859c; PubMed=8605183 [NCBI, ExPASy, EBI, Israel, Japan]
Larsen T.M.,
Wedekind J.E.,
Rayment I.,
Reed G.H.;
"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 35:4349-4358(1996).
|
[23]
|
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SUBSTRATE.
DOI=10.1021/bi9712450; PubMed=9376357 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang E.,
Brewer J.M.,
Minor W.,
Carreira L.A.,
Lebioda L.;
"Mechanism of enolase: the crystal structure of asymmetric dimer enolase-2-phospho-D-glycerate/enolase-phosphoenolpyruvate at 2.0-A resolution.";
Biochemistry 36:12526-12534(1997).
|
[24]
|
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANT ALA-40 IN COMPLEX WITH MAGNESIUM IONS AND SUBSTRATE ANALOG.
DOI=10.1016/S0003-9861(02)00024-3; PubMed=12054465 [NCBI, ExPASy, EBI, Israel, Japan]
Poyner R.R.,
Larsen T.M.,
Wong S.-W.,
Reed G.H.;
"Functional and structural changes due to a serine to alanine mutation in the active-site flap of enolase.";
Arch. Biochem. Biophys. 401:155-163(2002).
|
[25]
|
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT GLN-212 AND MUTANT GLN-169.
DOI=10.1021/bi0346345; PubMed=12846578 [NCBI, ExPASy, EBI, Israel, Japan]
Sims P.A.,
Larsen T.M.,
Poyner R.R.,
Cleland W.W.,
Reed G.H.;
"Reverse protonation is the key to general acid-base catalysis in enolase.";
Biochemistry 42:8298-8306(2003).
|
|
ExPASy Home page
