You are using an unsupported browser. Please upgrade your browser to a newer version to get the best experience on Yeast Metabolome Database.
Identification
NameEnolase 1
Synonyms
  • 2-phospho-D-glycerate hydro-lyase 1
  • 2-phosphoglycerate dehydratase 1
Gene NameENO1
Enzyme Class
Biological Properties
General FunctionInvolved in magnesium ion binding
Specific Function2-phospho-D-glycerate = phosphoenolpyruvate + H(2)O
Cellular LocationCytoplasm
SMPDB PathwaysNot Available
KEGG Pathways
Glycolysis / Gluconeogenesisec00010 Map00010
Methane metabolismec00680 Map00680
SMPDB ReactionsNot Available
KEGG Reactions
2-phospho-D-glyceric acidPhosphoenolpyruvic acid + water
Metabolites
YMDB IDNameView
YMDB00276Phosphoenolpyruvic acidShow
YMDB006752-phospho-D-glyceric acidShow
YMDB00890waterShow
YMDB009852-phospho-d-glycerateShow
GO Classification
Component
phosphopyruvate hydratase complex
macromolecular complex
protein complex
Function
catalytic activity
lyase activity
phosphopyruvate hydratase activity
binding
ion binding
cation binding
metal ion binding
magnesium ion binding
carbon-oxygen lyase activity
hydro-lyase activity
Process
glucose metabolic process
glucose catabolic process
metabolic process
glycolysis
small molecule metabolic process
alcohol metabolic process
monosaccharide metabolic process
hexose metabolic process
Gene Properties
Chromosome Locationchromosome 7
LocusYGR254W
Gene Sequence>1314 bp ATGGCTGTCTCTAAAGTTTACGCTAGATCCGTCTACGACTCCCGTGGTAACCCAACCGTC GAAGTCGAATTAACCACCGAAAAGGGTGTTTTCAGATCCATTGTCCCATCTGGTGCTTCT ACCGGTGTCCACGAAGCTTTGGAAATGAGAGATGGTGACAAATCCAAGTGGATGGGTAAG GGTGTTTTGCACGCTGTTAAGAACGTCAACGATGTCATTGCTCCAGCTTTCGTTAAGGCT AACATTGATGTTAAGGACCAAAAGGCCGTCGATGACTTCTTGATTTCTTTGGACGGTACT GCCAACAAATCCAAGTTGGGTGCTAACGCTATCTTGGGTGTTTCTTTGGCTGCTTCCAGA GCTGCCGCTGCTGAAAAGAATGTCCCATTATACAAGCACTTGGCTGACTTGTCTAAGTCC AAGACCTCTCCATACGTTTTGCCAGTTCCATTCTTGAACGTTTTGAACGGTGGTTCCCAC GCTGGTGGTGCTTTGGCTTTGCAAGAATTTATGATTGCTCCAACTGGTGCTAAGACCTTC GCTGAAGCTTTGAGAATTGGTTCCGAAGTTTACCACAACTTGAAGTCTTTGACCAAGAAG AGATACGGTGCTTCTGCCGGTAACGTCGGTGACGAAGGTGGTGTTGCTCCAAACATTCAA ACTGCTGAAGAAGCTTTGGACTTGATTGTTGACGCTATCAAGGCCGCTGGTCACGACGGT AAGGTCAAGATCGGTTTGGACTGTGCTTCCTCTGAATTCTTCAAGGACGGTAAGTACGAC TTGGACTTCAAGAATCCAAACTCTGACAAATCCAAGTGGTTGACTGGTCCTCAATTGGCT GACTTGTACCACTCCTTGATGAAGAGATACCCAATTGTCTCCATCGAAGATCCATTTGCT GAAGATGACTGGGAAGCTTGGTCTCACTTCTTCAAGACCGCTGGTATTCAAATTGTTGCT GATGACTTGACTGTCACCAACCCAAAGAGAATTGCTACCGCTATCGAAAAGAAGGCTGCC GACGCTTTGTTGTTGAAGGTCAACCAAATCGGTACCTTGTCTGAATCCATCAAAGCTGCT CAAGACTCTTTCGCTGCCGGTTGGGGTGTTATGGTTTCCCACAGATCTGGTGAAACTGAA GACACTTTCATTGCTGACTTGGTCGTCGGTTTGAGAACTGGTCAAATCAAGACTGGTGCT CCAGCTAGATCCGAAAGATTGGCTAAATTGAACCAATTGTTGAGAATCGAAGAAGAATTG GGTGACAACGCTGTTTTCGCTGGTGAAAACTTCCACCACGGTGACAAATTATAA
Protein Properties
Pfam Domain Function
Protein Residues437
Protein Molecular Weight46815.69922
Protein Theoretical pI6.6
PDB Fileshow
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Enolase 1 MAVSKVYARSVYDSRGNPTVEVELTTEKGVFRSIVPSGASTGVHEALEMRDGDKSKWMGK GVLHAVKNVNDVIAPAFVKANIDVKDQKAVDDFLISLDGTANKSKLGANAILGVSLAASR AAAAEKNVPLYKHLADLSKSKTSPYVLPVPFLNVLNGGSHAGGALALQEFMIAPTGAKTF AEALRIGSEVYHNLKSLTKKRYGASAGNVGDEGGVAPNIQTAEEALDLIVDAIKAAGHDG KIKIGLDCASSEFFKDGKYDLDFKNPNSDKSKWLTGPQLADLYHSLMKRYPIVSIEDPFA EDDWEAWSHFFKTAGIQIVADDLTVTNPKRIATAIEKKAADALLLKVNQIGTLSESIKAA QDSFAAGWGVMVSHRSGETEDTFIADLVVGLRTGQIKTGAPARSERLAKLNQLLRIEEEL GDNAVFAGENFHHGDKL
References
External Links
ResourceLink
Saccharomyces Genome Database ENO1
Uniprot IDP00924
Uniprot NameENO1_YEAST
GenBank Gene IDJ01322
Genebank Protein ID171455
PDB ID
2ONE
General Reference
  • Holland, M. J., Holland, J. P., Thill, G. P., Jackson, K. A. (1981). "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 256:1385-1395.6256394
  • Mazzoni, C., Ruzzi, M., Rinaldi, T., Solinas, F., Montebove, F., Frontali, L. (1997). "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 13:369-372.9133741
  • Tettelin, H., Agostoni Carbone, M. L., Albermann, K., Albers, M., Arroyo, J., Backes, U., Barreiros, T., Bertani, I., Bjourson, A. J., Bruckner, 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., Kleine, K., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII." Nature 387:81-84.9169869
  • Chin, C. C., Brewer, J. M., Wold, F. (1981). "The amino acid sequence of yeast enolase." J Biol Chem 256:1377-1384.7005235
  • Garrels, J. I., Futcher, B., Kobayashi, R., Latter, G. I., Schwender, B., Volpe, T., Warner, J. R., McLaughlin, C. S. (1994). "Protein identifications for a Saccharomyces cerevisiae protein database." Electrophoresis 15:1466-1486.7895733
  • Norbeck, J., 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 16:149-156.7737086
  • Poyner, R. R., Laughlin, L. T., Sowa, G. A., Reed, G. H. (1996). "Toward identification of acid/base catalysts in the active site of enolase: comparison of the properties of K345A, E168Q, and E211Q variants." Biochemistry 35:1692-1699.8634301
  • Brewer, J. M., Holland, M. J., Lebioda, L. (2000). "The H159A mutant of yeast enolase 1 has significant activity." Biochem Biophys Res Commun 276:1199-1202.11027610
  • Grandier-Vazeille, X., Bathany, K., Chaignepain, S., Camougrand, N., Manon, S., Schmitter, J. M. (2001). "Yeast mitochondrial dehydrogenases are associated in a supramolecular complex." Biochemistry 40:9758-9769.11502169
  • Ficarro, S. B., McCleland, M. L., Stukenberg, P. T., Burke, D. J., Ross, M. M., Shabanowitz, J., Hunt, D. F., White, F. M. (2002). "Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae." Nat Biotechnol 20:301-305.11875433
  • Brewer, J. M., Glover, C. V., Holland, M. J., Lebioda, L. (2003). "Enzymatic function of loop movement in enolase: preparation and some properties of H159N, H159A, H159F, and N207A enolases." J Protein Chem 22:353-361.13678299
  • Ghaemmaghami, S., Huh, W. K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., Weissman, J. S. (2003). "Global analysis of protein expression in yeast." Nature 425:737-741.14562106
  • Gruhler, A., Olsen, J. V., Mohammed, S., Mortensen, P., Faergeman, N. J., Mann, M., Jensen, O. N. (2005). "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Mol Cell Proteomics 4:310-327.15665377
  • Li, X., Gerber, S. A., Rudner, A. D., Beausoleil, S. A., Haas, W., Villen, J., Elias, J. E., Gygi, S. P. (2007). "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." J Proteome Res 6:1190-1197.17330950
  • Chi, A., Huttenhower, C., Geer, L. Y., Coon, J. J., Syka, J. E., Bai, D. L., Shabanowitz, J., Burke, D. J., Troyanskaya, O. G., Hunt, D. F. (2007). "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Proc Natl Acad Sci U S A 104:2193-2198.17287358
  • Smolka, M. B., Albuquerque, C. P., Chen, S. H., Zhou, H. (2007). "Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Proc Natl Acad Sci U S A 104:10364-10369.17563356
  • Albuquerque, C. P., Smolka, M. B., Payne, S. H., Bafna, V., Eng, J., Zhou, H. (2008). "A multidimensional chromatography technology for in-depth phosphoproteome analysis." Mol Cell Proteomics 7:1389-1396.18407956
  • Lebioda, L., Stec, B. (1988). "Crystal structure of enolase indicates that enolase and pyruvate kinase evolved from a common ancestor." Nature 333:683-686.3374614
  • Lebioda, L., Stec, B., Brewer, J. M. (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 264:3685-3693.2645275
  • Stec, B., Lebioda, L. (1990). "Refined structure of yeast apo-enolase at 2.25 A resolution." J Mol Biol 211:235-248.2405163
  • Larsen, T. M., Wedekind, J. E., Rayment, I., Reed, G. H. (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 35:4349-4358.8605183
  • Zhang, E., Brewer, J. M., Minor, W., Carreira, L. A., Lebioda, L. (1997). "Mechanism of enolase: the crystal structure of asymmetric dimer enolase-2-phospho-D-glycerate/enolase-phosphoenolpyruvate at 2.0 A resolution." Biochemistry 36:12526-12534.9376357
  • Poyner, R. R., Larsen, T. M., Wong, S. W., Reed, G. H. (2002). "Functional and structural changes due to a serine to alanine mutation in the active-site flap of enolase." Arch Biochem Biophys 401:155-163.12054465
  • Sims, P. A., Larsen, T. M., Poyner, R. R., Cleland, W. W., Reed, G. H. (2003). "Reverse protonation is the key to general acid-base catalysis in enolase." Biochemistry 42:8298-8306.12846578