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Sequence of ENO1_YEAST

EC Number:4.2.1.11

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
4.2.1.11
phosphopyruvate hydratase
P00924
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
437
46816
Swiss-Prot
Reaction
2-phospho-D-glycerate = phosphoenolpyruvate + H2O
Other sequences found for EC No. 4.2.1.11

General information:

Sequence
show sequence in fasta format
  0 MAVSKVYARS VYDSRGNPTV EVELTTEKGV FRSIVPSGAS TGVHEALEMR DGDKSKWMGK
 60 GVLHAVKNVN DVIAPAFVKA NIDVKDQKAV DDFLISLDGT ANKSKLGANA ILGVSLAASR
120 AAAAEKNVPL YKHLADLSKS KTSPYVLPVP FLNVLNGGSH AGGALALQEF MIAPTGAKTF
180 AEALRIGSEV YHNLKSLTKK RYGASAGNVG DEGGVAPNIQ TAEEALDLIV DAIKAAGHDG
240 KIKIGLDCAS SEFFKDGKYD LDFKNPNSDK SKWLTGPQLA DLYHSLMKRY PIVSIEDPFA
300 EDDWEAWSHF FKTAGIQIVA DDLTVTNPKR IATAIEKKAA DALLLKVNQI GTLSESIKAA
360 QDSFAAGWGV MVSHRSGETE DTFIADLVVG LRTGQIKTGA PARSERLAKL NQLLRIEEEL
420 GDNAVFAGEN FHHGDKL
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
30278
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
6256394
30279
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
9133741
30280
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
9169869
30281
Engel S.R.,Dietrich F.S.,Fisk D.G.,Binkley G.,Balakrishnan R.,Costanzo M.C.,Dwight S.S.,Hitz B.C.,Karra K.,Nash R.S.,Weng S.,Wong E.D.,Lloyd P.,Skrzypek M.S.,Miyasato S.R.,Simison M.,Cherry J.M.
The reference genome sequence of Saccharomyces cerevisiae: Then and now.
G3 (Bethesda)
4
389-398
2014
24374639
30282
Chin C.C.Q.,Brewer J.M.,Wold F.
The amino acid sequence of yeast enolase.
J. Biol. Chem.
256
1377-1384
1981
7005235
30284
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
7895733
30285
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
7737086
30286
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
8634301
30287
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
11027610
30288
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
11502169
30289
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
13678299
30290
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
14562106
30291
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
17287358
30292
Starita L.M.,Lo R.S.,Eng J.K.,von Haller P.D.,Fields S.
Sites of ubiquitin attachment in Saccharomyces cerevisiae.
Proteomics
12
236-240
2012
22106047
30293
Lebioda L.,Stec B.
Crystal structure of enolase indicates that enolase and pyruvate kinase evolved from a common ancestor.
Nature
333
683-686
1988
3374614
30294
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
2645275
30295
Stec B.,Lebioda L.
Refined structure of yeast apo-enolase at 2.25-A resolution.
J. Mol. Biol.
211
235-248
1990
2405163
30296
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
8605183
30297
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
9376357
30298
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
12054465
30299
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
12846578