Information on EC 4.2.1.11 - phosphopyruvate hydratase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY
4.2.1.11
-
RECOMMENDED NAME
GeneOntology No.
phosphopyruvate hydratase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2-phospho-D-glycerate = phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
2-phospho-D-glycerate = phosphoenolpyruvate + H2O
show the reaction diagram
mechanism
-
2-phospho-D-glycerate = phosphoenolpyruvate + H2O
show the reaction diagram
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
addition
-
-
-
-
elimination
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
1-butanol autotrophic biosynthesis
-
-
Bifidobacterium shunt
-
-
Biosynthesis of antibiotics
-
-
Biosynthesis of secondary metabolites
-
-
Entner-Doudoroff pathway II (non-phosphorylative)
-
-
Entner-Doudoroff pathway III (semi-phosphorylative)
-
-
ethylene biosynthesis V (engineered)
-
-
formaldehyde assimilation I (serine pathway)
-
-
gluconeogenesis I
-
-
gluconeogenesis II (Methanobacterium thermoautotrophicum)
-
-
gluconeogenesis III
-
-
glycerol degradation to butanol
-
-
glycolysis
-
-
Glycolysis / Gluconeogenesis
-
-
glycolysis I (from glucose 6-phosphate)
-
-
glycolysis II (from fructose 6-phosphate)
-
-
glycolysis III (from glucose)
-
-
glycolysis IV (plant cytosol)
-
-
glycolysis V (Pyrococcus)
-
-
glycolysis VI (metazoan)
-
-
heterolactic fermentation
-
-
Metabolic pathways
-
-
Methane metabolism
-
-
Microbial metabolism in diverse environments
-
-
photosynthetic 3-hydroxybutyrate biosynthesis (engineered)
-
-
Rubisco shunt
-
-
superpathway of glucose and xylose degradation
-
-
SYSTEMATIC NAME
IUBMB Comments
2-phospho-D-glycerate hydro-lyase (phosphoenolpyruvate-forming)
Also acts on 3-phospho-D-erythronate.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2-phospho-D-glycerate hydro-lyase
-
-
-
-
2-phosphoglycerate dehydratase
-
-
-
-
2-phosphoglycerate enolase
-
-
-
-
2-phosphoglyceric dehydratase
-
-
-
-
alpha,alpha-enolase
-
-
-
-
Alt a XI
-
-
-
-
beta,beta-enolase
-
-
-
-
Cla h VI
-
-
-
-
enolase
-
-
-
-
gamma,gamma-enolase
-
-
-
-
gamma-enolase
-
-
-
-
HLE1
-
-
-
-
hydratase, phosphoenolpyruvate
-
-
-
-
Laminin binding protein
-
-
-
-
Major allergen Alt a 11
-
-
-
-
MSE
-
-
-
-
Neural enolase
-
-
-
-
neuron-specific enolase
-
-
-
-
NNE
-
-
-
-
Non-neural enolase
-
-
-
-
NSE
-
-
-
-
OSE1
-
-
-
-
phosphoenolpyruvate hydratase
-
-
-
-
Phosphopyruvate hydratase
-
-
-
-
R-NSE
-
-
-
-
Skeletal muscle enolase
-
-
-
-
Tau-crystallin
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9014-08-8
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Archaeoglobus fulgidus 7324
-
-
-
Manually annotated by BRENDA team
strain ATCC 19213
-
-
Manually annotated by BRENDA team
strain 168
SwissProt
Manually annotated by BRENDA team
Bacillus subtilis 168
strain 168
SwissProt
Manually annotated by BRENDA team
strain BE1
Uniprot
Manually annotated by BRENDA team
Bacteroides fragilis BE1
strain BE1
Uniprot
Manually annotated by BRENDA team
Bifidobacterium animalis subsp. lactis BI07
strain BI07
UniProt
Manually annotated by BRENDA team
Bifidobacterium bifidum S16
strain S16
-
-
Manually annotated by BRENDA team
strain BBSF
-
-
Manually annotated by BRENDA team
Bifidobacterium breve BBSF
strain BBSF
-
-
Manually annotated by BRENDA team
strain S123
UniProt
Manually annotated by BRENDA team
Bifidobacterium longum S123
strain S123
UniProt
Manually annotated by BRENDA team
Borrelia burgdorferi B31-MI-16
-
-
-
Manually annotated by BRENDA team
cow
-
-
Manually annotated by BRENDA team
strain strain BO5.10
-
-
Manually annotated by BRENDA team
strain 2308, 100% sequence identity with strain A19
UniProt
Manually annotated by BRENDA team
Brucella abortus A19
strain 2308, 100% sequence identity with strain A19
UniProt
Manually annotated by BRENDA team
gene LOS2
UniProt
Manually annotated by BRENDA team
propagated in livers of male Sprague-Dawley rats
-
-
Manually annotated by BRENDA team
enolase 1 and 2
-
-
Manually annotated by BRENDA team
isolated from sheep in Qinghai province of China
-
-
Manually annotated by BRENDA team
strain PaPt36
SwissProt
Manually annotated by BRENDA team
Eimeria tenella PaPt36
strain PaPt36
SwissProt
Manually annotated by BRENDA team
Entamoeba histolytica HM-1-IMSS
-
-
-
Manually annotated by BRENDA team
strain IP-1
-
-
Manually annotated by BRENDA team
Entamoeba invadens IP-1
strain IP-1
-
-
Manually annotated by BRENDA team
gram-positive bacteria, ATCC9790
SwissProt
Manually annotated by BRENDA team
JA 200 pLC 11-8
-
-
Manually annotated by BRENDA team
the enzyme binds to human plasminogen
Uniprot
Manually annotated by BRENDA team
gamma-enolase
-
-
Manually annotated by BRENDA team
strain HTA426
SwissProt
Manually annotated by BRENDA team
clone RRIM 600
SwissProt
Manually annotated by BRENDA team
2 forms: homdimeric form and heterodimeric form
-
-
Manually annotated by BRENDA team
recombinant alpha-enolase
-
-
Manually annotated by BRENDA team
three genes, ENO1, ENO2 and ENO3 encoding for three isoforms of the enzyme, alpha-enolase, gamma-enolase, and beta-enolase, respectively
-
-
Manually annotated by BRENDA team
O3 strain 1069
-
-
Manually annotated by BRENDA team
Lactobacillus plantarum LM3
-
-
-
Manually annotated by BRENDA team
Lactobacillus plantarum LM3
strain LM3
-
-
Manually annotated by BRENDA team
strain AZV
SwissProt
Manually annotated by BRENDA team
Leishmania mexicana AZV
strain AZV
SwissProt
Manually annotated by BRENDA team
serovar Lai
-
-
Manually annotated by BRENDA team
Leptospira interrogans 56601
serovar Lai
-
-
Manually annotated by BRENDA team
strain B-512FMCM, constitutively secreting dextransucrase
SwissProt
Manually annotated by BRENDA team
Leuconostoc mesenteroides B-512FMCM
strain B-512FMCM, constitutively secreting dextransucrase
SwissProt
Manually annotated by BRENDA team
alpha,alpha-enolase
SwissProt
Manually annotated by BRENDA team
beta,beta-enolase
SwissProt
Manually annotated by BRENDA team
Paracoccidioides brasiliensis 18
strain 18
UniProt
Manually annotated by BRENDA team
Paracoccidioides brasiliensis ATCC MYA-826
-
UniProt
Manually annotated by BRENDA team
Peptoclostridium difficile MC201
-
-
-
Manually annotated by BRENDA team
strain 3D7
SwissProt
Manually annotated by BRENDA team
strain NF54
-
-
Manually annotated by BRENDA team
strain 17XL
SwissProt
Manually annotated by BRENDA team
Plasmodium yoelii 17XL
strain 17XL
SwissProt
Manually annotated by BRENDA team
3 forms of the enzyme: enolase I, enolase II and enolase III
-
-
Manually annotated by BRENDA team
spontaneously hypertensive rats (SHR) and Wistar Kyoto (WKY) rats
SwissProt
Manually annotated by BRENDA team
L. Cv. Baker 296
-
-
Manually annotated by BRENDA team
enolase 1 and mutant E168Q of enolase 1
-
-
Manually annotated by BRENDA team
exists in at least 3 distinct forms
-
-
Manually annotated by BRENDA team
mutant S39A of isoenzyme 1
-
-
Manually annotated by BRENDA team
strain BY4741 and strain DELTAGLO1
SwissProt
Manually annotated by BRENDA team
strain cat 1.S3-14A
-
-
Manually annotated by BRENDA team
serovar Typhi Ty2
-
-
Manually annotated by BRENDA team
isolate not clearly defined
TREMBL
Manually annotated by BRENDA team
isolates SFCornell, SF-Daft, SF-Florida
TREMBL
Manually annotated by BRENDA team
isolates SN-UCD1, SN-37R, SN-MU1, SN-MU2, SN-MUCAT2, SN-OT1
TREMBL
Manually annotated by BRENDA team
Anhui isolate, Chinese mainland strain, propagated in BALB/c mice
UniProt
Manually annotated by BRENDA team
Staphylococcus aureus RN4220
-
-
-
Manually annotated by BRENDA team
Staphylococcus aureus Wood 46
Wood 46
Uniprot
Manually annotated by BRENDA team
Steinernema glaseri NC
-
UniProt
Manually annotated by BRENDA team
DSM 320523
-
-
Manually annotated by BRENDA team
strain R36A
GenBank
Manually annotated by BRENDA team
Streptococcus pneumoniae R36A
strain R36A
GenBank
Manually annotated by BRENDA team
M6 strain D471; type M6 strain D471
-
-
Manually annotated by BRENDA team
Streptococcus ratti FA-1
FA-1
-
-
Manually annotated by BRENDA team
serotype 2
UniProt
Manually annotated by BRENDA team
serotype 2, strain ZYS
-
-
Manually annotated by BRENDA team
strain 05ZYH33, serotype 2
UniProt
Manually annotated by BRENDA team
strain 05ZYH33, serotype 2
UniProt
Manually annotated by BRENDA team
Streptomyces mutans
-
-
-
Manually annotated by BRENDA team
Streptomyces pneumoniae
-
-
-
Manually annotated by BRENDA team
3 enolase isoforms
-
-
Manually annotated by BRENDA team
strain ISS413
-
-
Manually annotated by BRENDA team
Trichinella spiralis ISS413
strain ISS413
-
-
Manually annotated by BRENDA team
Vibrio parahaemolyticus ATCC33847
-
UniProt
Manually annotated by BRENDA team
Xanthomonas oryzae pv. oryzae
UniProt
Manually annotated by BRENDA team
5 isoenzymes
-
-
Manually annotated by BRENDA team
3 isoelectric forms
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
enolase 1 and calreticulin siRNA reduce the [Ca2+]i levels, amounts of total TNF-alpha, and the release of TNF-alpha and leukotrienes, all of which are increased in the bone marrow-derived mast cells activated with antigen/antibody reaction
malfunction
-
the down-regulation of enolase selectively increases the susceptibility to phosphomycin
malfunction
Staphylococcus aureus RN4220
-
the down-regulation of enolase selectively increases the susceptibility to phosphomycin
-
metabolism
-
alpha-enolase is involved in glucose metabolism in Alzheimer's disease brain
metabolism
-
enolase 1 is a glycolytic enzyme expressed in most tissues
metabolism
Q5DDV5
enolase is a key enzyme in the glycolytic pathway
metabolism
-
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
metabolism
-
in the glycolysis-related energy pathway, enolase might be involved in higher metabolic activity during the day than at night, at least in part, overview
physiological function
-
alfa-enolase is a fibronectin-binding protein
physiological function
-
alpha-enolase is a glycolytic enzyme that also acts as a surface plasminogen receptor, alpha-enolase elicits a pancreatic ductal adenocarcinoma cell-specific, integrated humoral and cellular response
physiological function
-
ENO-1 binds plasminogen at the cell surface, enhancing local plasmin production, overexpression of ENO-1 in U937 cells increases their migratory and matrix-penetrating capacity
physiological function
-
enolase from Botrytis is cold responsive, influenced by cAMP and acts putatively as a transcriptional regulator of the zinc-C6 protein family and calpain like proteases
physiological function
C6GGT7
enolase functions as a protective antigen displayed on the bacterial cell surface
physiological function
-
enolase is a conserved putative human plasminogen receptor in Bifidobacterium
physiological function
Q45RT9
enolase is a conserved putative human plasminogen receptor in Bifidobacterium
physiological function
Q8G5I9
enolase is a conserved putative human plasminogen receptor in Bifidobacterium
physiological function
-
enolase is a multifunctional protein that participates in glycolysis and gluconeogenesis and can act as a plasminogen receptor on the cell surface
physiological function
-
enolase is involved in bacterial adhesion to host epithelial cells
physiological function
-
enolase plays a role in encystation
physiological function
-
glycolytic/gluconeogenesis enzyme, eye lens tau-crystallin protein, plasminogen binding protein, c-Myc binding protein and transcription factor in tumor formationk
physiological function
-
cell surface ENOA is one of the many plasminogen-binding molecules, interaction of the plasminogen lysinebinding sites with ENOA is dependent upon recognition of ENOA C-terminal lysines K420, K422 and K434, and also K256. Binding with ENOA lysyl residues leads to activation of plasminogen to plasmin by the proteolytic action of either tissue-type or urokinase-type plasminogen activators, overview. ENOA takes part, together with urokinase plasminogen activator receptor, integrins and some cytoskeletal proteins, in a multiprotein complex, called metastasome, responsible for adhesion, migration and proliferation in ovarian cancer cells
physiological function
-
enolase 1 and calreticulin are important proteins in regulating the differentiation and functions of bone marrow-derived mast cells
physiological function
A5JQI1
enolase acts as a fibronectin binding protein in Paracoccidioides brasiliensis. Association between recombinant PbEno and plasminogen is lysine-dependent and is dependent on cell surface localization of PbENo, since purified rPbEno, in its soluble form, inhibits plasminogen binding to fixed cells, interaction analysis, overview. Exposure of epithelial cells and phagocytes to enolase is associated with an increased expression of surface sites of adhesion. In fact, the association of Paracoccidioides brasiliensis with epithelial cells and phagocytes is increased in the presence of rPbEno
physiological function
-
enolase can act as a plasminogen-binding protein
physiological function
-
enolase can act as a plasminogen-binding protein, an internal motif, FYDAEKKEY, is responsible for the plasminogen recognition
physiological function
Streptomyces pneumoniae
-
enolase can act as a plasminogen-binding protein, an internal motif, FYDKERKVYD, is responsible for the plasminogen recognition
physiological function
-
enolase is a multifunctional enzyme that is involved in the reversible dehydration of 2-phospho-D-glycerate to phosphoenolpyruvate in glycolytic and gluconeogenesis pathways. Csenolase might play key roles in the growth of the parasites. Csenolase is an important glycolytic enzyme required for the development of Clonorchis sinensis
physiological function
-
enolase is found both in the secretome and in association with the surface of Leishmania spp. where it probably functions as plasminogen receptor, playing a role in the parasite's invasiveness and virulence, a function possibly also present in the other trypanosomatids
physiological function
-
enolase is found both in the secretome and in association with the surface of Leishmania spp. where it probably functions as plasminogen receptor, playing a role in the parasite's invasiveness and virulence, a function possibly also present in the other trypanosomatids. Enolase can act as a plasminogen-binding protein, an internal motif, AYDAERKMY, is responsible for the plasminogen recognition
physiological function
-
enolase plays an important role in glycolysis. It also binds RNA, overview
physiological function
-
main physiological role of enolase is the reversible conversion of 2-phospho-D-glycerate and to phosphoenolpyruvate within the glycolytic pathway. Enolases play an important role in Cyclamen embryogenesis, overview
physiological function
Q5DDV5
recombinant SjENO binds to human plasminogen as its receptor
physiological function
Q2YPV0
the recombinant enolase exhibits fibronectin-binding ability in immunoblotting assay, suggesting that enolase may play a role in Brucella abortus colonization, persistence, and invasion of host tissue
physiological function
-
the enzyme is involved in the modified Embden-Meyerhof pathway
physiological function
Q9UWJ5
the enzyme probably functions in sugar fermentation pathway
physiological function
-
the enzyme is involved in glycogen catabolism
physiological function
-
enolase is a moonlighting cytoplasmic protein which also associates with the bacterial outer surface and facilitates binding to host plasminogen
physiological function
-
enolase is essential for Staphylococcus aureus and involved in the process of bacterial autolysis
physiological function
-
the enzyme plays a role in pathogen interaction with host molecules like plasminogen, which may contribute to the pathogenesis of leptospirosis
physiological function
B8Q027
the enzyme promotes infection by Xenorhabdus poinarii and Metarhizium anisopliae
physiological function
-
the plasminogen-enolase association may play a critical role in the virulence of Salmonella Typhi by causing direct damage to the host cell extracellular matrix
physiological function
Leptospira interrogans 56601
-
the enzyme plays a role in pathogen interaction with host molecules like plasminogen, which may contribute to the pathogenesis of leptospirosis
-
physiological function
Bifidobacterium animalis subsp. lactis BI07, Bifidobacterium bifidum S16
-
enolase is a conserved putative human plasminogen receptor in Bifidobacterium
-
physiological function
Paracoccidioides brasiliensis ATCC MYA-826
-
enolase acts as a fibronectin binding protein in Paracoccidioides brasiliensis. Association between recombinant PbEno and plasminogen is lysine-dependent and is dependent on cell surface localization of PbENo, since purified rPbEno, in its soluble form, inhibits plasminogen binding to fixed cells, interaction analysis, overview. Exposure of epithelial cells and phagocytes to enolase is associated with an increased expression of surface sites of adhesion. In fact, the association of Paracoccidioides brasiliensis with epithelial cells and phagocytes is increased in the presence of rPbEno
-
physiological function
Bifidobacterium breve BBSF
-
enolase is a conserved putative human plasminogen receptor in Bifidobacterium
-
physiological function
Borrelia burgdorferi B31-MI-16
-
enolase is a moonlighting cytoplasmic protein which also associates with the bacterial outer surface and facilitates binding to host plasminogen
-
physiological function
Archaeoglobus fulgidus 7324
-
the enzyme is involved in the modified Embden-Meyerhof pathway
-
physiological function
Steinernema glaseri NC
-
the enzyme promotes infection by Xenorhabdus poinarii and Metarhizium anisopliae
-
physiological function
Entamoeba invadens IP-1
-
enolase plays a role in encystation
-
physiological function
Bifidobacterium longum S123
-
enolase is a conserved putative human plasminogen receptor in Bifidobacterium
-
physiological function
Brucella abortus A19
-
the recombinant enolase exhibits fibronectin-binding ability in immunoblotting assay, suggesting that enolase may play a role in Brucella abortus colonization, persistence, and invasion of host tissue
-
physiological function
Lactobacillus plantarum LM3
-
alfa-enolase is a fibronectin-binding protein
-
physiological function
Staphylococcus aureus RN4220
-
enolase is essential for Staphylococcus aureus and involved in the process of bacterial autolysis
-
physiological function
-
enolase functions as a protective antigen displayed on the bacterial cell surface
-
metabolism
-
in tumor cells, ENOA is upregulated and supports anaerobic proliferation, cf. Warburg effect, it is expressed at the cell surface, where it promotes cancer invasion, and is subjected to a specific array of post-translational modifications, namely acetylation, methylation and phosphorylation
additional information
-
circadian rhythm of enolase in suprachiasmatic nucleus depends on mitochondrial function. Enolase activity, coupled with lactate dehydrogenase, is higher during the light period than that in the dark. However, enolase mRNA, analyzed by RT-PCR, shows higher levels during the dark period than in the light
additional information
-
overexpression of ENOA is associated with tumor development through a process known as aerobic glycolysis or the Warburg effect. ENOA induces autoantibody production and induces a specific immune response in tumors, overview
additional information
-
proteomic analysis and peptide mapping, 2D isoelectric focusing and mass spectrometry, overview
additional information
-
proteomic analysis, peptide mapping, 2D isoelectric focusing, overview
additional information
-
the human muscle-specific enolase is less susceptible to inactivation by reactive aldehydes than the pig enzyme
additional information
Q5DDV5
the recombinant enolase is recognized by rabbit sera directed against an antigen preparation from adult worms. 24.28% reduction in the liver egg count and a reduction of 21.45% in the fecal egg count occur in BALB/c mice vaccinated with recombinant SjENO compared with control mice
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(Z)-3-chloro-2-phosphoenolpyruvate + OH-
?
show the reaction diagram
-
wild-type enzyme catalyzes hydrolysis of (Z)-3-chloro-2-phosphoenolpyruvate by addition of OH- and elimination of Cl- at C-3
-
-
?
2,3-diketo-5-methylthiopentane 1-phosphate
2-hydroxy-3-keto-5-methylthiopent-1-ene 1-phosphate
show the reaction diagram
Q5KVE7
methionine salvage pathway
-
-
?
2,3-diketo-5-methylthiopentane 1-phosphate
2-hydroxy-3-keto-5-methylthiopent-1-ene 1-phosphate
show the reaction diagram
P37869
methionine salvage pathway
-
-
?
2,3-diketo-5-methylthiopentane 1-phosphate
2-hydroxy-3-keto-5-methylthiopent-1-ene 1-phosphate
show the reaction diagram
Q5KVE7
methionine salvage pathway, stereochemical course of the reaction catalyzed by enolase determined, C1 proton abstraction
-
-
?
2,3-diketo-5-methylthiopentane 1-phosphate
2-hydroxy-3-keto-5-methylthiopent-1-ene 1-phosphate
show the reaction diagram
P37869
methionine salvage pathway, stereochemical course of the reaction catalyzed by enolase determined, C1 proton abstraction
-
-
?
2,3-diketo-5-methylthiopentane 1-phosphate
2-hydroxy-3-keto-5-methylthiopent-1-ene 1-phosphate
show the reaction diagram
Bacillus subtilis 168
P37869
methionine salvage pathway, methionine salvage pathway, stereochemical course of the reaction catalyzed by enolase determined, C1 proton abstraction
-
-
?
2,3-diketohexane 1-phosphate
?
show the reaction diagram
Q5KVE7
alternate substrate, C1 proton abstraction
-
-
?
2,3-diketohexane 1-phosphate
?
show the reaction diagram
Bacillus subtilis, Bacillus subtilis 168
P37869
alternate substrate, C1 proton abstraction
-
-
?
2,3-dioxo-5-methylthio-1-phosphopentane + 4 H+
3-hydroxy-5-methyl-thio-pent-2-en-1-yl-phosphate + H2O
show the reaction diagram
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
-
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
-
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
-
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
-
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
P00924
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
-
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
-
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
-
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
-
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
Q27655
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
Q8GR70
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
Q9NDH8
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
Q9LEJ0
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
Q97QS2
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
P25704
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
Streptococcus pneumoniae R36A
Q97QS2
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
Streptococcus ratti FA-1
-
-
-
?
2-phospho-D-glycerate
?
show the reaction diagram
-
age-related changes in the properties of the enzyme
-
-
-
2-phospho-D-glycerate
?
show the reaction diagram
-
enzyme of glycolysis
-
-
-
2-phospho-D-glycerate
?
show the reaction diagram
-
beta,beta-enolase binds with high affinity the adjacent enzymes in the glycolytic pathway (pyruvate kinase and phosphoglycerate mutase), beta,beta-enolase binds with high affinity sarcomeric troponin but not actin and tropomyosin
-
-
-
2-phospho-D-glycerate
?
show the reaction diagram
-
the enzyme is a plasminogen binding protein
-
-
-
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
O69174
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
P09104
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
P04764
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Q97QS2
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Q8KNX9
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Streptomyces mutans
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Streptomyces pneumoniae
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Q1ET73
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
P00925
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Q8IJN7
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Q7RA60
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Q967Y8
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Q96VP4
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
P0A6P9
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Q8MU59
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Q3HL75
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
P17182, P21550
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
A1J8J9
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Q27727
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
C9YSH7
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
C6GGT7
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
A5JQI1
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Q45RT9
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Q8G5I9
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Q5H0Y0
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Q2YPV0
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
C4LXE8
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Q5DDV5
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
D7NHW9
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Q9UWJ5
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
K7N5M7
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
W6ABG9
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Q042F4
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
B8Q027
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
E9NJD0
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Q8IJN7
additional functions apart from glycolytic function of enolase tested
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Q7RA60
additional functions apart from glycolytic function of enolase tested, vaccination studies in mice
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
direct transfer mechanisms of substrates between enolase and phosphoglycerate mutase predicted by molecular dynamics simulation
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
in vitro studies on catalytic, divalent cation binding sites
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
influence on exchange of amino acid residues on structure, dissociation and function of enolase analyzed
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
P17182, P21550
interaction studies between alpha,alpha enolase and tubulin, co-localization studies with microtubules
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Q27727
kinetic and structural properties of monomeric and dimeric forms of recombinant enolase of Plasmodium falciparum compared
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
plasminogen-binding activity besides metabolic function
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
P00925
separated role of enolase besides function in glycolysis, stimulation of vacuole fusion and involvement in protein trafficking to vacuoles determined
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
structural analysis
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
A1J8J9
studies on host-trematode relationships, properties of enolase as a host-interacting molecule analyzed
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
analysis of pathogenesis of Streptococcus suis: rSsEno binds to fibronectin and plasminogen
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
C4LXE8
substrate binding in pre-catalytic state and during catalysis, recombinant enzyme, overview
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
the enzyme is involved in the modified Embden-Meyerhof pathway
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Q9UWJ5
the enzyme probably functions in sugar fermentation pathway
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Leptospira interrogans 56601
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Trichinella spiralis ISS413
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Bifidobacterium animalis subsp. lactis BI07
Q45RT9
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Eimeria tenella PaPt36
Q967Y8
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Bifidobacterium bifidum S16, Bifidobacterium breve BBSF
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Paracoccidioides brasiliensis 18
A5JQI1
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Borrelia burgdorferi B31-MI-16
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Leuconostoc mesenteroides B-512FMCM
Q1ET73
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Vibrio parahaemolyticus ATCC33847
W6ABG9
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Leishmania mexicana AZV
Q3HL75
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Leishmania mexicana AZV
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Steinernema glaseri NC
B8Q027
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Bifidobacterium longum S123
Q8G5I9
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Brucella abortus A19
Q2YPV0
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Peptoclostridium difficile MC201
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Lactobacillus plantarum LM3
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Lactobacillus plantarum LM3
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Plasmodium yoelii 17XL
Q7RA60
additional functions apart from glycolytic function of enolase tested, vaccination studies in mice
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Staphylococcus aureus RN4220
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
C6GGT7
-
-
-
r
3-phospho-D-erythronate
?
show the reaction diagram
-
-
-
-
?
3-phospho-D-glycerate
?
show the reaction diagram
-
-
-
-
?
D-tartronate semialdehyde phosphate
?
show the reaction diagram
-
slowly-reacting strongly bound chromophoric substrate
-
-
?
phosphoenolpyruvate
2-phospho-D-glycerate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate
2-phospho-D-glycerate
show the reaction diagram
-
-
-
r
phosphoenolpyruvate
2-phospho-D-glycerate
show the reaction diagram
-
-
-
r
phosphoenolpyruvate
2-phospho-D-glycerate
show the reaction diagram
-
-
-
r
phosphoenolpyruvate
2-phospho-D-glycerate
show the reaction diagram
-
-
-
r
phosphoenolpyruvate
2-phospho-D-glycerate
show the reaction diagram
-
-
-
r
phosphoenolpyruvate
2-phospho-D-glycerate
show the reaction diagram
-
-
-
r
phosphoenolpyruvate + H2O
2-phospho-D-glycerate
show the reaction diagram
P00924
-
-
-
r
phosphoenolpyruvate + H2O
2-phospho-D-glycerate
show the reaction diagram
P04764
-
-
-
r
phosphoenolpyruvate + H2O
2-phospho-D-glycerate
show the reaction diagram
-
analysis of pathogenesis of Bacillus anthracis: binding of human plasminogen and laminin
-
-
r
D-tartronate semialdehyde-2-phosphate
?
show the reaction diagram
-
substrate analogue that changes its spectrum while bound to the enzyme
-
?
additional information
?
-
-
enolase acts as a DNA methyltransferase 2 inhibitor. Enolase interacts with Ehmeth, and modulates its activity under conditions of glucose starvation inhibiting the binding of Ehmeth and human DNA methyltransferase 2 to Entamoeba histolytica MRS2 DNA
-
-
-
additional information
?
-
-
His-tagged recombinant enolase protein shows a high affinity for human plasminogen
-
-
-
additional information
?
-
Q45RT9
His-tagged recombinant enolase protein shows a high affinity for human plasminogen
-
-
-
additional information
?
-
Q8G5I9
His-tagged recombinant enolase protein shows a high affinity for human plasminogen
-
-
-
additional information
?
-
-
ENOA has C-terminal lysines predominantly responsible for plasminogen activation, interaction of the plasminogen lysinebinding sites with ENOA is dependent upon recognition of ENOA C-terminal lysines K420, K422 and K434, and also K256
-
-
-
additional information
?
-
-
enolase shows plasminogen-binding activity
-
-
-
additional information
?
-
-
plasminogen bound to recombinant enolase can be converted to active plasmin
-
-
-
additional information
?
-
-
enolase binds plasminogen in a lysine-dependent manner but not through ionic interactions
-
-
-
additional information
?
-
-
the enzyme binds plasminogen
-
-
-
additional information
?
-
W6ABG9
the enzyme binds to plasminogen
-
-
-
additional information
?
-
Bifidobacterium animalis subsp. lactis BI07
Q45RT9
His-tagged recombinant enolase protein shows a high affinity for human plasminogen
-
-
-
additional information
?
-
Bifidobacterium bifidum S16, Bifidobacterium breve BBSF
-
His-tagged recombinant enolase protein shows a high affinity for human plasminogen
-
-
-
additional information
?
-
Borrelia burgdorferi B31-MI-16
-
plasminogen bound to recombinant enolase can be converted to active plasmin
-
-
-
additional information
?
-
Vibrio parahaemolyticus ATCC33847
W6ABG9
the enzyme binds to plasminogen
-
-
-
additional information
?
-
Bifidobacterium longum S123
Q8G5I9
His-tagged recombinant enolase protein shows a high affinity for human plasminogen
-
-
-
additional information
?
-
-
enolase binds plasminogen in a lysine-dependent manner but not through ionic interactions
-
-
-
additional information
?
-
Lactobacillus plantarum LM3
-
the enzyme binds plasminogen
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2,3-diketo-5-methylthiopentane 1-phosphate
2-hydroxy-3-keto-5-methylthiopent-1-ene 1-phosphate
show the reaction diagram
Q5KVE7
methionine salvage pathway
-
-
?
2,3-diketo-5-methylthiopentane 1-phosphate
2-hydroxy-3-keto-5-methylthiopent-1-ene 1-phosphate
show the reaction diagram
Bacillus subtilis, Bacillus subtilis 168
P37869
methionine salvage pathway
-
-
?
2,3-dioxo-5-methylthio-1-phosphopentane + 4 H+
3-hydroxy-5-methyl-thio-pent-2-en-1-yl-phosphate + H2O
show the reaction diagram
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
?
show the reaction diagram
-
age-related changes in the properties of the enzyme
-
-
-
2-phospho-D-glycerate
?
show the reaction diagram
-
enzyme of glycolysis
-
-
-
2-phospho-D-glycerate
?
show the reaction diagram
-
beta,beta-enolase binds with high affinity the adjacent enzymes in the glycolytic pathway (pyruvate kinase and phosphoglycerate mutase), beta,beta-enolase binds with high affinity sarcomeric troponin but not actin and tropomyosin
-
-
-
2-phospho-D-glycerate
?
show the reaction diagram
-
the enzyme is a plasminogen binding protein
-
-
-
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
O69174
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Q97QS2
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Q8KNX9
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Streptomyces mutans
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Streptomyces pneumoniae
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Q1ET73
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
P00925
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Q8IJN7
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Q7RA60
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Q967Y8
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Q96VP4
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
P0A6P9
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Q8MU59
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Q3HL75
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
P17182, P21550
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
A1J8J9
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Q27727
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Q45RT9
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Q8G5I9
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Q5H0Y0
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Q2YPV0
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
C4LXE8
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Q5DDV5
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
D7NHW9
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
K7N5M7
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
W6ABG9
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Q042F4
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
B8Q027
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
E9NJD0
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
analysis of pathogenesis of Streptococcus suis: rSsEno binds to fibronectin and plasminogen
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
the enzyme is involved in the modified Embden-Meyerhof pathway
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Q9UWJ5
the enzyme probably functions in sugar fermentation pathway
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Leptospira interrogans 56601
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Trichinella spiralis ISS413
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Bifidobacterium animalis subsp. lactis BI07
Q45RT9
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Eimeria tenella PaPt36
Q967Y8
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Bifidobacterium bifidum S16, Bifidobacterium breve BBSF
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Borrelia burgdorferi B31-MI-16
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Leuconostoc mesenteroides B-512FMCM
Q1ET73
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Vibrio parahaemolyticus ATCC33847
W6ABG9
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Leishmania mexicana AZV
Q3HL75
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Leishmania mexicana AZV
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Steinernema glaseri NC
B8Q027
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Bifidobacterium longum S123
Q8G5I9
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Brucella abortus A19
Q2YPV0
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Lactobacillus plantarum LM3
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Lactobacillus plantarum LM3
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Plasmodium yoelii 17XL
Q7RA60
-
-
-
r
phosphoenolpyruvate + H2O
2-phospho-D-glycerate
show the reaction diagram
-
analysis of pathogenesis of Bacillus anthracis: binding of human plasminogen and laminin
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
Staphylococcus aureus RN4220
-
-
-
-
?
additional information
?
-
-
enolase acts as a DNA methyltransferase 2 inhibitor. Enolase interacts with Ehmeth, and modulates its activity under conditions of glucose starvation inhibiting the binding of Ehmeth and human DNA methyltransferase 2 to Entamoeba histolytica MRS2 DNA
-
-
-
additional information
?
-
-
ENOA has C-terminal lysines predominantly responsible for plasminogen activation, interaction of the plasminogen lysinebinding sites with ENOA is dependent upon recognition of ENOA C-terminal lysines K420, K422 and K434, and also K256
-
-
-
additional information
?
-
-
enolase shows plasminogen-binding activity
-
-
-
additional information
?
-
Borrelia burgdorferi, Borrelia burgdorferi B31-MI-16
-
plasminogen bound to recombinant enolase can be converted to active plasmin
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
P00925
specific affinity to tRNA imported into mitochondria, involved to direct mitochondrial tRNA import in vitro
-
additional information
-
complex formation between active centers of enolase and phosphoglycerate mutase determined, interaction of enolase with C-terminal tail of phosphoglycerate mutase confirmed
-
additional information
P0A6P9
interaction with RNase E of the RNA degradasome, enolase recognition site for RNase E conserved in gamma-proteobacteria
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Al3+
Q2YPV0
can partially substitute for Mg2+ or Zn2+ at 10 mM showing 68.8% of the maximal activity with 10 mM Mg2+
Cd2+
-
14% of the activation with Mg2+
Co2+
-
absolute requirement for divalent metal ions, 9% of the activity with Mg2+
Co2+
-
activates in 0.1 M KCl, maximum activity at 0.0035 mM. Maximum of 4 Co2+ ions are bound per dimer
Co2+
-
less than 40% of the activation with Mg2+
Cu2+
-
20% of the activiation with Mg2+
K+
-
slightly activating effect
K+
-
activates, best at 2 mM
KBr
Q27727
dimeric form 10-20% activated, monomeric form strongly inhibited
KCl
-
required for maximal activity
KCl
Q27727
dimeric form 10-20% activated, monomeric form strongly inhibited
Mg2+
-
dependent on
Mg2+
-
absolute requirement for divalent metal ions, Mg2+ is most effective
Mg2+
-
Km: 0.43 mM
Mg2+
-
activation
Mg2+
-
Km: 6 mM
Mg2+
-
Km: 0.47 mM; required
Mg2+
-
activation by several divalent cation, Mg2+ is most effective
Mg2+
-
absolute requirement for divalent metal ions, Mg2+ is most effective
Mg2+
-
optimal concentration: 1 mM
Mg2+
-
absolute requirement for divalent metal ions, Mg2+ is most effective; Km: 0.67 mM
Mg2+
-
absolute requirement for divalent metal ions, Mg2+ is most effective; Km: 0.69 mM
Mg2+
-
absolute requirement for divalent metal ions, Mg2+ is most effective; Km: 0.7 mM
Mg2+
-
absolute requirement for divalent metal ions, Mg2+ is most effective; Km: 0.73 mM
Mg2+
-
absolute requirement for divalent metal ions, Mg2+ is most effective; Km: 0.03 mM
Mg2+
-
Km: 0.5 mM
Mg2+
-
at pH 6.8, Km for liver enzyme: 0.67 mM, Km for muscle enzyme: 1.33 mM at pH 7.4, Km for liver enolase: 0.42 mM, Km for muscle enolase: 0.25 mM
Mg2+
-
two ions are necessary for activity, shows inhibition at high concentration
Mg2+
-
three binding sites, binding at the first two is required for activity, binding at the third site is inhibitory
Mg2+
-
required for activity, can be replaced by Mn2+ or Zn2+, but lower activity is observed
Mg2+
-
essential for activity, high concentrations are inhibitory
Mg2+
Q8GR70
two magnesium ions per subunit are required for catalytic activity
Mg2+
P09104
activation by 2 Mg2+ molecules per subunit, one conformational and one catalytic ion
Mg2+
Q5KVE7
activity depends on
Mg2+
-
activity depends on, optimal concentration for activity between 1 mM and 2 mM
Mg2+
Q27727
protects enolases of yeast and of rabbit muscle but not of Plasmodium falciparum from dissociation in presence of imidazol
Mg2+
-
activity depends on
Mg2+
-
activity depends on
Mg2+
Q96VP4
metal-binding
Mg2+
P0A6P9
coordinated in catalytic site of enolase
Mg2+
-
maximal specific activity with respect to 2-phospho-D-glycerate is achieved in the presence of 1 mM Mg2+, in the presence of 0.1 mM MnSO4 or 0.24 mM ZnSO4 (i.e. the optimal concentrations of Mn2+ or Zn2+ ions), only 46% and 14%, respectively, of the activity determined for the Mg2+-stimulated reaction is found
Mg2+
-
required for activity
Mg2+
C9YSH7
the highest activation rate of the enzymatic activity is reached at 5 mM Mg2+ and remains unchanged up to 25 mM
Mg2+
-
required for activity, the optimum concentration is 3 mM
Mg2+
-
activates, best at 10 mM
Mg2+
Q2YPV0
activates, optimally at 10 mM
Mg2+
Q5DDV5
activates
Mg2+
Q9UWJ5
metal ion required, equally active in presence of Mg2+ and Mn2+, 1 mM
Mg2+
Q042F4
each monomer is binding a single Mg2+ cofactor
Mg2+
-
physiological cofactor
Mg2+
-
Mg2+ is the strongest enolase activating metal. Binding of two Mg2+ ions is essential
Mg2+
-
enolase is activated by low concentrations of Mg2+
Mn2+
-
46% of the activation with Mg2+; absolute requirement for divalent metal ions
Mn2+
-
19% of the activation with Mg2+
Mn2+
-
10% of the activation with Mg2+; absolute requirement for divalent metal ions; Km for the cytoplasmic isoenzyme: 1.2 mM; Km for the plastidic isoenzyme: 1.4 mM
Mn2+
-
can partially replace Mg2+ in activation
Mn2+
-
can replace Mg2+, mechanistic study using electron paramagnetic resonance
Mn2+
-
catalytic binding sites analyzed in vitro
Mn2+
Q2YPV0
can partially substitute for Mg2+ or Zn2+ at 10 mM showing 90.4% of the maximal activity with 10 mM Mg2+
Mn2+
Q9UWJ5
metal ion required, equally active in presence of Mg2+ and Mn2+, 1 mM
Mn2+
-
can also bind and activate the enzyme
Ni2+
Q2YPV0
can partially substitute for Mg2+ or Zn2+ at 10 mM showing 90.5% of the maximal activity with 10 mM Mg2+
Zn2+
-
absolute requirement for divalent metal ions, 35% of the activation with Mg2+
Zn2+
-
12% of the activation with Mg2+
Zn2+
-
optimal concentration: 1 mM
Zn2+
-
can partially replace Mg2+ in activation
Zn2+
-
can replace Mg2+, mechanistic study using electron paramagnetic resonance
Zn2+
-
catalytic binding sites analyzed in vitro
Zn2+
Q2YPV0
activates, optimally at 10 mM, best activating metal ion
Zn2+
-
can also bind and activate the enzyme
Mn2+
-
required
additional information
-
enolase 1 is a metalloenzyme with an absolute requirement for divalent metal ions
additional information
Q2YPV0
57% of maximal activity without metal ion compared to Mg2+ at 10 mM
additional information
-
Ca2+, Ba2+, Sr2+, Hg2+, Pb2+, and Be2+ are not capable of activating the enzyme
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-fluoro-2-phosphonoacetohydroxamate
-
competitive inhibitor
2-phosphoglycerate
-
substrate inhibition
2-phosphoglycerate
-
competitive
2-phosphoglycerate
-
competitive
2-phosphoglycerate
P17182, P21550
presence of 0.8 mM 2-phosphoglycerate abolished the binding of beta,beta-enolase to tubulin, kinetics shown
3-aminoenolpyruvate phosphate
-
-
-
3-hydroxy-2-nitro-1-phosphonopropane
-
-
3-hydroxypropionic acid phosphate
-
-
4-hydroxy-2-nonenal
-
-
citrate
Q9UWJ5
competitive
Cr2+
Q2YPV0
leads to complete inhibition at 10 mM
Cu2+
Q2YPV0
leads to complete inhibition at 10 mM
cumene hydroperoxide
-
1% residual activity after treatment with 17 mM cumene hydroperoxide at 50C and pH 7 for 2 h
D-2,3-dihydroxyisobutyric acid 2-phosphate
-
-
D-erythro-2,3-dihydroxybutyric acid 2-phosphate
-
-
D-erythro-2,3-dihydroxybutyric acid 3-phosphate
-
-
D-glycerate-2-phosphate
-
mixed-type inhibition in the binding of D-glycerate-2-phosphate and D-phosphoglycerate mutase to the D-glycerate-2-phosphate binding site on the enolase in absence of D-glycerate-2,3-diphosphate, inhibition is almost fully reverted by D-glycerate-2,3-diphosphate
D-glyceric acid 3-phosphate
-
-
D-lactic acid phosphate
-
-
D-tartronate semialdehyde phosphate
-
-
diphosphate
-
inhibits natural enolase and recombinant protein
EDTA
Q9UWJ5
1 mM
F-
-
in presence of phosphate, competitive
F-
-
noncompetitive inhibition below 10 mM, competitive above 10 mM
F-
-
quasi-irreverible inhibition above 0.01 mM
F-
-
in absence of phosphate noncompetitive inhibition up to 10 mM F-, competitive inhibition in presence of 0.5 mM phosphate
F-
-
noncompetitive in the presence of phosphate, competitive in the absence of phosphate
F-
P09104
-
F-
Q1ET73
non-competitive inhibition without phosphate and in presence of 1 mM phosphate, competitive inhibition in presence of 20 mM phosphate
fluoride
-
the inhibitory effect of fluoride alone is noncompetitive, but it is competitive in the presence of a low phosphate level
Hg2+
Q2YPV0
leads to complete inhibition at 10 mM
hydrogen peroxide
-
inhibitory at 0.25%, at pH 7
iodoacetamide
-
binds to cysteine residues
KBr
Q27727
monomeric form
KCl
Q27727
monomeric form
Li+
-
noncompetitive with either 2-phosphoglycerate or Mg2+
Li+
-
liver enzyme is severely inhibited, muscle enzyme is moderately inhibited
methylglyoxal
-
incubation of0.015 mM enzyme with 2 mM, 3.1 mM and 4.34 mM methylglyoxal in 100 mM phosphate buffer pH 7.4 for 3 h causes the loss a 32%, 55% and 82% of initial specific activity, respectively. Inhibition of enolase by methylglyoxal and formation of enolase-derived glycation products arises more effectively in slight alkaline conditions and in the presence of inorganic phosphate
methylglyoxal
-
-
Mg2+
-
inhibitor above 1 mM, N207A, H159A, H159N and H159F mutants are stimulated at this concentration
Mg2+
-
inhibitory at higher concentrations
Mg2+
-
at high concentrations
Mg2+
-
above 2 mM
Mg2+
-
inhibitory in excess
Mg2+
-
Mg2+ is inhibitory at 30 mM to the physiological reaction, but not to the reaction with D-tartronate semialdehyde phosphate
Mg2+
-
inhibitory at higher concentrations
Mn2+
-
inhibitory in excess
Na+
-
50% inhibition around 0.3-0.4 M
NaCl
Q27727
inhibits dimeric and monomeric forms of the enzyme, inhibition stronger for the monomeric form
NaClO4
-
inactivation is due to dissociation of the enolase into inactive monomers, 2-phospho-D-glycerate prevents this inactivation
NaClO4
P25704
E414L mutant is more sensitive to inactivation than the wild-type enzyme
NaClO4
-
enolase at 19.4 mM after incubation in 0.2 M NaClO4, has 32% of its original activity and is 21% octameric. Following a 24 h dialysis against buffer, the protein is 77% octameric and has 74% of its original activity
p19ras
-
when full-length p19ras and C-terminal region are bound to NSE, it inhibits the enzymatic activity of NSE, p19ras interacts with enolase alpha and represses its enzymatic activity in vitro
-
peracetic acid
-
1% residual activity after treatment with 4 mM peracetic acid at 25C and pH 7 for 15 min
phosphate
-
-
phosphate
-
competitive inhibition at 2-4 mM phosphate with respect to 2-phosphoglycerate becomes noncompetitive in presence of 20-40 mM phosphate
phosphate
-
-
phosphate
-
at a high phosphate concentration, noncompetitive inhibition is found and at a lower concentration competitive inhibition
phosphate
-
competitive inhibitor of enolase
phosphonoacetohydroxamate
-
-
phosphonoacetohydroxamate
-
retains open tunnel from catalytic site to protein surface, offers possibilities for drug development
phosphonoacetohydroxamate
-
preference for formation of hybrid Zn2+/Mn2+ complexes with enolase, in vitro activity of the complexed enolase in presence of phosphonoacetohydroxamate investigated by crystallography and electron paramagnetic resonance spectroscopy
PO43-
P09104
mimics the phosphate group of substrate
SO42-
-
induces a complete closure of catalytic site loops
tert-butyl hydroperoxide
-
1% residual activity after treatment with 290 mM tert-butyl hydroperoxide at 50C and pH 7 for 3 h
trans-2-nonenal
-
-
Zn2+
-
inhibitory in excess
monofluorophosphate
-
-
additional information
-
no inhibition by SH-reagents
-
additional information
-
-
-
additional information
-
no inhibition by NEM and iodoacetate
-
additional information
-
inhibition of enolase by fluoride in combination with phosphate can influence glycolysis and so reduce acid production of even growth rate, thereby leading to potential anticariogenic effects
-
additional information
Q1ET73
recombinant enolase inhibits activity of purified dextransucrase
-
additional information
-
antibodies against enolase inhibits up to 60% of plasminogen binding
-
additional information
-
the muscle-specific enolase is used as a model enzyme for inhibition analysis by acrolein, 4-hydroxy-2-nonenal, and trans-2-nonenal, incubation for 1-24 h at 25C, 37C, and 45C, overview. The compounds show inhibition effectivity in the following descending order: inhibition degree of enolase activity occurred in following order: 4-hydroxy-2-nonenal, acrolein, methylglyoxal, trans-2-nonenal, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ARP
-
the 26-amino-acid-long acetylcholinesterase C-terminal peptide ARP elevates activity of enolase in dose-dependent manner: 200 nM ARP by 7.1%, 600 nM ARP by 12.5%
-
phosphate
-
slight stimulation without F-
HCO3-
Q5KVE7
Km about 50% increased in presence of sodium bicarbonate, crystallized enzyme structure complexed with HCO3- in its activated form
additional information
-
-SH groups required for activity
-
additional information
-
-
-
additional information
-
contains 23 half-cystines per mol of subunit
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.03205
2-phospho-D-glycerate
-
isoform Eno1p, in 50 mM imidazole, pH 7.1, 250 mM KCl, 1 mM Mg(OAc)2, 0.1 mM EDTA, temperature not specified in the publication
0.04
2-phospho-D-glycerate
-
recombinant, dimeric enzyme; recombinant, His-tagged, hexameric enzyme
0.043
2-phospho-D-glycerate
-
wild type, 25C, Mg2+, pH 7.5
0.04482
2-phospho-D-glycerate
-
isoform Err2p, in 50 mM imidazole, pH 7.1, 250 mM KCl, 1 mM Mg(OAc)2, 0.1 mM EDTA, temperature not specified in the publication
0.05
2-phospho-D-glycerate
-
K345A/N80D/N126D, 25C, Mg2+, pH 7.5
0.05
2-phospho-D-glycerate
-
recombinant protein
0.054
2-phospho-D-glycerate
-
pH 7.6, 25C
0.057
2-phospho-D-glycerate
-
N80D/N126D, 25C, Mg2+, pH 7.5
0.05856
2-phospho-D-glycerate
-
isoform Err3p, in 50 mM imidazole, pH 7.1, 250 mM KCl, 1 mM Mg(OAc)2, 0.1 mM EDTA, temperature not specified in the publication
0.08
2-phospho-D-glycerate
-
natural enolase
0.082
2-phospho-D-glycerate
-
at pH 8.0
0.086
2-phospho-D-glycerate
C9YSH7
in 81 mM triethanolamine/HCl, pH 7.4, at 25C
0.106
2-phospho-D-glycerate
E9NJD0
1.5 mM MgCl2 in 50 mM Tris/HCl (pH 7.4), at 25C
0.149
2-phospho-D-glycerate
-
at pH 7.0
0.199
2-phospho-D-glycerate
-
in 50 mM imidazole-HCl buffer, pH 6.8, with 3 mM MgSO4, 0.4 M KCl
0.2
2-phospho-D-glycerate
-
native enzyme, in the absence of methyglyoxal, in 50 mM imidazole-HCl buffer, pH 6.8, with 0.4 M KCl and 3 mM MgSO4
0.38
2-phospho-D-glycerate
-
pH 6.8, 30C
0.4
2-phospho-D-glycerate
Q9UWJ5
pH 8, 70C
0.425
2-phospho-D-glycerate
-
in 50 mM imidazole-HCl buffer, pH 7.8, with 1 mM MgSO4, 0.4 M KCl
0.66
2-phospho-D-glycerate
-
glycated enzyme, in the presence of 40% (v/v) methyglyoxal, in 50 mM imidazole-HCl buffer, pH 6.8, with 0.4 M KCl and 3 mM MgSO4
1.9
2-phospho-D-glycerate
W6ABG9
in 100 mM HEPES buffer, pH 8.5, 7.7 mM KCl, 10 mM MgSO4, at 25C
2
2-phospho-D-glycerate
Q2YPV0
pH 8.5, 25C, recombinant enzyme
2
2-phospho-D-glycerate
-
50C, pH not specified in the publication
2.47
2-phospho-D-glycerate
C6GGT7
in 100 mM HEPES, 10 mM MgCl2, and 7.7 mM KCl, pH 7.0, at 37C
2.61
2-phospho-D-glycerate
Q1ET73
at pH 6.8
0.025
2-phosphoglycerate
-
plastidic isoenzyme
0.029
2-phosphoglycerate
-
brain enolase I, brain enolase II, brain enolase III
0.031
2-phosphoglycerate
-
at 0.035 mM Co2+
0.032
2-phosphoglycerate
-
in presence of 1 mM Mg2+, native enzyme
0.036
2-phosphoglycerate
-
enolase III
0.038
2-phosphoglycerate
-
muscle enolase
0.038
2-phosphoglycerate
-
-
0.045
2-phosphoglycerate
-
enolase II
0.045
2-phosphoglycerate
-
-
0.05
2-phosphoglycerate
-
-
0.05
2-phosphoglycerate
-
-
0.057
2-phosphoglycerate
-
enolase I
0.061
2-phosphoglycerate
-
cytosolic isoenzyme
0.061
2-phosphoglycerate
-
-
0.069
2-phosphoglycerate
-
-
0.07
2-phosphoglycerate
-
at 75C
0.078
2-phosphoglycerate
-
-
0.09
2-phosphoglycerate
-
pH 6.8, muscle enolase; pH 7.4, liver enolase and muscle enolase
0.11
2-phosphoglycerate
-
mutant E168Q
0.12
2-phosphoglycerate
-
muscle enzyme
0.12
2-phosphoglycerate
-
mutant enzyme E211Q
0.131
2-phosphoglycerate
-
in presence of 1 mM Mg2+, mutant enzyme S39A
0.14
2-phosphoglycerate
-
liver enzyme
0.17
2-phosphoglycerate
-
pH 6.8, liver enolase
0.22
2-phosphoglycerate
-
Y-NSE.H6
0.24
2-phosphoglycerate
-
R-NSE
0.25
2-phosphoglycerate
-
Y-NSE
0.3
2-phosphoglycerate
-
-
0.3
2-phosphoglycerate
-
wild type enzyme
0.44
2-phosphoglycerate
-
in presence of 1 mM Mg2+
0.68
2-phosphoglycerate
-
mutant K345A
0.71
2-phosphoglycerate
-
-
4.35
2-phosphoglycerate
-
-
0.21
2-phosphoglyceric acid
Q8KNX9
37C, in reaction buffer
0.39
3-phospho-D-glycerate
-
at pH 7.0
0.07
phosphoenolpyruvate
Q27727
acitivity for monomers
0.11
phosphoenolpyruvate
-
-
0.11
phosphoenolpyruvate
-
-
0.14
phosphoenolpyruvate
-
enolase III
0.15
phosphoenolpyruvate
-
enolase I
0.17
phosphoenolpyruvate
-
pH 7.4, muscle enolase
0.18
phosphoenolpyruvate
-
at pH 8.0
0.19
phosphoenolpyruvate
-
enolase II
0.19
phosphoenolpyruvate
-
pH 6.8, liver enolase
0.2
phosphoenolpyruvate
-
-
0.2
phosphoenolpyruvate
-
recombinant protein
0.21
phosphoenolpyruvate
-
natural enolase
0.244
phosphoenolpyruvate
-
pH 7.6, 25C
0.25
phosphoenolpyruvate
-
-
0.25
phosphoenolpyruvate
-
-
0.25
phosphoenolpyruvate
-
pH 7.4, liver enolase
0.28
phosphoenolpyruvate
Q27727
activity for dimeric form
0.31
phosphoenolpyruvate
-
liver enzyme
0.33
phosphoenolpyruvate
-
pH 6.8, muscle enolase
0.37
phosphoenolpyruvate
-
muscle enzyme
0.534
phosphoenolpyruvate
-
at pH 7.0
0.58
phosphoenolpyruvate
-
native enzyme, in the absence of methyglyoxal, in 50 mM imidazole-HCl buffer, pH 6.8, with 0.4 M KCl and 3 mM MgSO4
0.657
phosphoenolpyruvate
-
in 50 mM imidazole-HCl buffer, pH 7.8, with 1 mM MgSO4, 0.4 M KCl
0.702
phosphoenolpyruvate
-
in 50 mM imidazole-HCl buffer, pH 6.8, with 3 mM MgSO4, 0.4 M KCl
0.83
phosphoenolpyruvate
-
glycated enzyme, in the presence of 40% (v/v) methyglyoxal, in 50 mM imidazole-HCl buffer, pH 6.8, with 0.4 M KCl and 3 mM MgSO4
0.95
phosphoenolpyruvate
-
pH 6.8, 30C
2.6
phosphoenolpyruvate
-
plastidic isoenzyme
3.3
phosphoenolpyruvate
-
recombinant protein
7.2
phosphoenolpyruvate
-
cytosolic isoenzyme
43
phosphoenolpyruvate
P25704
E414L mutant enzyme, pH 7.1, 25C
additional information
2-phospho-D-glycerate
-
Km ranges between 0.047 mM and 0.130 mM between pH 6.0 and pH 8.6
1.281
3-phospho-D-glycerate
-
at pH 8.0
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
temperature-dependence of Km-values
-
additional information
additional information
Q27727
disruption of subunit-subunit interactions declines enzyme activity 3fold
-
additional information
additional information
Q5DDV5
kinetic analysis, forward and reverse reaction, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
19.4
2-phospho-D-glycerate
-
isoform Err3p, in 50 mM imidazole, pH 7.1, 250 mM KCl, 1 mM Mg(OAc)2, 0.1 mM EDTA, temperature not specified in the publication
19.7
2-phospho-D-glycerate
-
isoform Err2p, in 50 mM imidazole, pH 7.1, 250 mM KCl, 1 mM Mg(OAc)2, 0.1 mM EDTA, temperature not specified in the publication
20.6
2-phospho-D-glycerate
-
recombinant, dimeric enzyme
22.2
2-phospho-D-glycerate
-
recombinant, His-tagged, hexameric enzyme
37
2-phospho-D-glycerate
E9NJD0
1.5 mM MgCl2 in 50 mM Tris/HCl (pH 7.4), at 25C
52.7
2-phospho-D-glycerate
-
in 50 mM imidazole-HCl buffer, pH 7.8, with 1 mM MgSO4, 0.4 M KCl
71.4
2-phospho-D-glycerate
-
isoform Eno1p, in 50 mM imidazole, pH 7.1, 250 mM KCl, 1 mM Mg(OAc)2, 0.1 mM EDTA, temperature not specified in the publication
81.68
2-phospho-D-glycerate
-
in 50 mM imidazole-HCl buffer, pH 6.8, with 3 mM MgSO4, 0.4 M KCl
0.018 - 0.019
2-phosphoglycerate
-
mutant enzyme S39A, pH 7.8, 21-23C
78
2-phosphoglycerate
-
wild-type enzyme
230
2-phosphoglycerate
-
native enolase, pH 7.8, 21-23C
15.47
phosphoenolpyruvate
-
in 50 mM imidazole-HCl buffer, pH 7.8, with 1 mM MgSO4, 0.4 M KCl
34.07
phosphoenolpyruvate
-
in 50 mM imidazole-HCl buffer, pH 6.8, with 3 mM MgSO4, 0.4 M KCl
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
124
2-phospho-D-glycerate
-
in 50 mM imidazole-HCl buffer, pH 7.8, with 1 mM MgSO4, 0.4 M KCl
1023
350
2-phospho-D-glycerate
E9NJD0
1.5 mM MgCl2 in 50 mM Tris/HCl (pH 7.4), at 25C
1023
410
2-phospho-D-glycerate
-
in 50 mM imidazole-HCl buffer, pH 6.8, with 3 mM MgSO4, 0.4 M KCl
1023
520
2-phospho-D-glycerate
-
recombinant, dimeric enzyme
1023
560
2-phospho-D-glycerate
-
recombinant, His-tagged, hexameric enzyme
1023
23.5
phosphoenolpyruvate
-
in 50 mM imidazole-HCl buffer, pH 7.8, with 1 mM MgSO4, 0.4 M KCl
51
48.5
phosphoenolpyruvate
-
in 50 mM imidazole-HCl buffer, pH 6.8, with 3 mM MgSO4, 0.4 M KCl
51
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0014
2-fluoro-2-phosphonoacetohydroxamate
-
at pH 7.2, binds in the same way as phosphoenolpyruvate and phosphonoacetohydroxamate
0.13
citrate
Q9UWJ5
pH 8, 70C
0.127
diphosphate
-
recombinant protein, substrate 2-phospho-D-glycerate
0.232
diphosphate
-
natural enolase, substrate 2-phospho-D-glycerate
0.238
diphosphate
-
natural enolase, substrate phosphoenolpyruvate
0.26
diphosphate
-
recombinant protein, substrate 2-phospho-D-glycerate
4.6
F-
Q1ET73
in presence of 1 mM phosphate
5.4
F-
Q1ET73
in absence of phosphate
9.2
F-
Q1ET73
in presence of 20 mM phosphate
10
F-
-
pH 6.8, 30C, in the absence of phosphate
2.2
fluoride
-
at low phosphate concentrations (4-6 mM), in 50 mM imidazole-HCl buffer, pH 7.8, with 1 mM MgSO4, 0.4 M KCl
18.8
fluoride
-
at low phosphate concentrations (4-6 mM), in 50 mM imidazole-HCl buffer, pH 6.8, with 3 mM MgSO4, 0.4 M KCl
0.327
Mg2+
-
isoform Err2p, in 50 mM imidazole, pH 7.1, 250 mM KCl, 1 mM Mg(OAc)2, 0.1 mM EDTA, temperature not specified in the publication
0.695
Mg2+
-
isoform Err3p, in 50 mM imidazole, pH 7.1, 250 mM KCl, 1 mM Mg(OAc)2, 0.1 mM EDTA, temperature not specified in the publication
2.1
Mg2+
-
isoform Eno1p, in 50 mM imidazole, pH 7.1, 250 mM KCl, 1 mM Mg(OAc)2, 0.1 mM EDTA, temperature not specified in the publication
3.249
Mg2+
-
in 50 mM imidazole-HCl buffer, pH 7.8, with 1 mM MgSO4, 0.4 M KCl
14.37
Mg2+
-
in 50 mM imidazole-HCl buffer, pH 6.8, with 3 mM MgSO4, 0.4 M KCl
1.266
Mn2+
-
in 50 mM imidazole-HCl buffer, pH 7.8, with 1 mM MgSO4, 0.4 M KCl
3.04
Mn2+
-
in 50 mM imidazole-HCl buffer, pH 6.8, with 3 mM MgSO4, 0.4 M KCl
0.32
phosphate
-
in 50 mM imidazole-HCl buffer, pH 6.8, with 3 mM MgSO4, 0.4 M KCl
0.9
phosphate
-
in 50 mM imidazole-HCl buffer, pH 7.8, with 1 mM MgSO4, 0.4 M KCl
0.015
phosphonoacetohydroxamate
-
-
1.58
Zn2+
-
in 50 mM imidazole-HCl buffer, pH 6.8, with 3 mM MgSO4, 0.4 M KCl
2.34
Zn2+
-
in 50 mM imidazole-HCl buffer, pH 7.8, with 1 mM MgSO4, 0.4 M KCl
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
60
NaClO4
-
mutant enzyme F137L/E363G, in 50 mM HEPES, pH 7.5, 1 mM Mg(OAc)2
200
NaClO4
-
wild type enzyme, in 50 mM HEPES, pH 7.5, 1 mM Mg(OAc)2
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.107
-
pH 7.5, 37C, activity in undialyzed cell extracts
0.41
-
crude extract, at pH 7.8
0.79
-
substrate: 2-phospho-D-glycerate, 50C, pH not specified in the publication, enzyme from starch-grown cells
0.9
-
crude extract, at pH 6.8
1.1
-
H159N mutant, pH 7.8, 21C
1.9
-
H159F mutant, pH 7.8, 21C
3.3
-
H159A mutant, pH 7.8, 21C
10.3
-
-
13.8
Q9UWJ5
pH 8, 70C
15.87
Q5DDV5
purified recombinant enzyme, substrate phosphoenolpyruvate, pH 7.4, 20C
22
Q9LEJ0
pH 7.4, 25C
23.2
-
SPM2, 0.25% Triton X-100
30
-
2-phospho-D-glycerate, pH 7.4, 20C, Tris/HCl
31.2
-
after 76.1fold purification, at pH 7.8
35
-
pH 6.8, 30C
35.81
Q5DDV5
purified recombinant enzyme, substrate 2-phospho-D-glycerate, pH 7.4, 20C
51
-
enolase III
64.6
-
liver enolase
67
P25704
recombinant wild-type enzyme, pH 7.1, 25C
67.4
-
enolase from synaptosomal cytoplasm
68
-
enolase II
69.6
-
-
75
-
after 83fold purification, at pH 6.8
76.2
-
-
77
P25704
recombinant E414L mutant, pH 7.1, 25C
79.8
-
brain enolase III
82.2
-
-
82.8
-
brain enolase I
85
-
pH 7.6, 25C
86.54
-
-
87
-
muscle enolase
87
-
enolase I
91
-
muscle enolase
92.3
-
muscle enolase
111
-
room temperature, pH 7.5, MgCl2, KCl, 2-phosphoglyceric acid
120
-
muscle enolase
124
Q8GR70
pH 7.5, 22C
197.4
-
plastidic isoenzyme
248
-
N207A mutant, pH 7.8, 21C
252.4
-
cytosolic isoenzyme
260
-
pH 8.1, room temperature
442
-
wild type, pH 7.8, 21C
700
-
pH 7.6, temperature not specified in the publication
918
-
monomeric enzyme form
1118
-
dimeric enzyme form
3909
Q2YPV0
purifed recombinant enzyme, pH 8.5, 37C, no metal ion added
9091
Q2YPV0
purifed recombinant enzyme, pH 8.5, 37C, 10 mM Mg2+
10050
Q2YPV0
purifed recombinant enzyme, pH 8.5, 37C, 10 mM Zn2+
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
his-tagged recombinant protein has the same activity than the wild type
additional information
Q967Y8
multifunctional role of enolase, participation in the parasitic invasion process and in the control of gene regulation
additional information
P37869
spectrophotometric assay described, generation of reaction products determined by NMR
additional information
Q5KVE7
spectrophotometric assay described, D-ribulose 1-phosphate and 5-methylthio-D-ribulose 1-phosphate in the presence of limiting 5-methylthio-D-ribulose 1-phosphate dehydratase analyzed, enzyme concentrations from 0.1 to 10 microM used
additional information
P17182, P21550
enzyme activity measured with the natural substrate 2-phospho-D-glycerate, conversion of reaction products determined by spectroscopy, kinetics of binding studies to tubulin by ELISA and surface plasmon resonance; enzyme activity tested, kinetics of binding studies to tubulin estimated by ELISA and surface plasmon resonance, association of beta,beta enolase to microtubules in differentiating myotubes but not in myoblasts
additional information
-
enolase activity measured spectrophotometrically by following the change in phosphoenolpyruvate concentration, substrate concentrations up to 0.3 mM for 2-phospho-D-glycerate and up to 2 mM for phosphoenolpyruvate
additional information
A1J8J9
binding studies of recombinant protein to human plasminogen confirms properties as host-interacting molecule
additional information
Q27727
kinetic properties of monomeric and dimeric forms of recombinant enolase compared, enzyme activity measured spectrophotometrically by monitoring formation of 2-phospho-D-glycerate, dimeric structure not essential for catalysis, monomeric form indicates a 3fold lower activity
additional information
-
activity assay of recombinant protein
additional information
-
enzyme activity monitored by following the conversion of phosphoenolpyruvate to 2-phospho-D-glycerate, specific activities of the variants, relative to wildtype enolase, are 0.1% for G157D and 0.01% for G376E
additional information
Q1ET73
activity of recombinant protein spectrophotometrically measured by conversion of 2-phospho-D-glycerate to phosphoenolpyruvate, substrate concentrations of 3 mM
additional information
P00925
additional and independent function beyond glycolytic enzyme function, involvement in mitochondrial tRNA targeting, depletion of enolase inhibits tRNA import in vivo, activity of enolase as an alternative molecular chaperone suggested
additional information
Q8IJN7
recombinant enolase protein of Plasmodium falciparum can protect mice against malaria, assay described
additional information
Q7RA60
the recombinant enolase of Plasmodium falciparum can protect mice infected with the lethal strain 17XL against malaria, assay described
additional information
P00925
in vitro stimulation of vacuole fusion by recombinant enolase determined, no stimulation solely by addition of substrate or product of enolase, catalytic activity independent of role in vacuole fusion, enolase-deficient vacuoles lack in vitro stimulation, enolase deficiency prevents normal protein sorting to the vacuole; in vitro stimulation of vacuole fusion by recombinant enolase determined, no stimulation solely by addition of substrate or product of enolase, catalytic activity independent of role in vacuole fusion, enolase-deficient vacuoles lack in vitro stimulation, enolase deficiency prevents normal protein sorting to the vacuole
additional information
-
binding affinity between enolase and phosphoglycerate mutase confirmed by interaction energies and conformation changes, 10 A resolution and three orientations positioning enolase towards to phosphoglycerate mutase tested in presence of 150 mM NaCl
additional information
Q96VP4
biological activity shown, enzyme activity comparable to those of Candida
additional information
P0A6P9
additional and independent function beyond glycolytic enzyme function, association of enolase to the RNA degrasome, role in RNA metabolism predicted
additional information
Q8MU59
functional activity of recombinant protein shown, immunogenicity determined by ELISA and Western Blot using different sera, natural infection of humans by Anisakis simplex larvae lacks sufficient antigenic stimuli
additional information
-
purified recombinant enolase has plasminogen binding activity, analyzed by flow cytometry
additional information
-
recombinant enolase has plasminogen binding activity, similarities to nine amino-acid internal plasminogen-binding motif of Streptococcus pneumoniae, enolase as one of the plasminogen receptors in the parasite predicted
additional information
-
Vmax at 37C and pH 6.8: 0.506 micromol/min/mg for the recombinant protein
additional information
-
31.2 nmol 2-PGA converted/min/36nM enolase
additional information
-
enolase shows the same specific activity (110 U/mg) in Tris-acetate or Tris-HCl buffers, whereas the specific activity is diminished (70 U/mg) in phosphate buffer
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5
Q27727
pH-induced dissociation of enolases, half-dissociation point
6
-
formation of 2-phosphoglycerate, plastidic isoenzyme
6.5 - 7
Q5DDV5
-
6.5
-
muscle enolase, formation of 2-phosphoglycerate
6.6
-
formation of 2-phosphoglycerate
6.8
-
-
6.8
-
imidazole buffer, Tris buffer
6.8
-
brain enolase I, brain enolase III; muscle enolase
6.8
-
muscle enolase, formation of phosphoenolpyruvate
6.8
Q1ET73
optimum determined by activity assay
6.8
-
at 37C, recombinant protein
6.8
-
assay at
6.9
-
formation of phosphoenolpyruvate
7
-
in the direction of 2-phospho-D-glycerate formation
7.1
-
phosphate buffer
7.1
-
formation of 2-phosphoglycerate
7.1
-
formation of phosphoenolpyruvate
7.1
-
activity assay at
7.2
-
-
7.3
-
formation of phosphoenolpyruvate
7.4 - 7.6
-
R-NSE, Y-NSE, Y-NSE.H6
7.4 - 7.6
-
irrespective of substrate
7.4
-
liver enzyme, both directions
7.4
-
assay at
7.5
-
formation of phosphoenolpyruvate
7.5
Q5KVE7
assay at
7.5
P17182, P21550
enzyme activity assay at; enzyme activity assay at
7.5
-
activity assay at
7.5
-
activity assay at
7.8 - 8
-
-
7.8
-
formation of 2-phosphoglycerate, cytosolic isoenzyme
8
-
in the direction of phosphoenolpyruvate formation
8.5
Q2YPV0
recombinant enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 10
Q2YPV0
activity range, recombinant enzyme
5 - 5.5
Q27727
pH-dependent dissociation reveals that protonation of groups at the intersubunit interface is responsible for dissociation
6 - 8.3
Q1ET73
catalytic activity above and below pH 6.8 remains constant at 30% of maximal activity
6 - 9
-
pH 6.0: about 35% of maximal activity, pH 9.0: about 30% of maximal activity
6.5 - 7
-
steep decrease in activity below pH 6.5, 50% of the maximal activity retained above pH 7.0
6.8 - 8
-
about 55% of maximal activity at pH 6.8 and at pH 8.0
7.3 - 8
-
activity decreases steadily, 60% of the activity remains at pH 7.0 and pH 8.4
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20
Q5DDV5
assay at
22
-
assay at room temperature
25
-
activity assay at
25
-
activity assay at
30
Q1ET73
activity assay at
37
P17182, P21550
enzyme activity assay at; enzyme activity assay at
37
-
at pH 6.8, recombinant protein
37
-
assay at
37
Q2YPV0
recombinant enzyme
90
Q9UWJ5
above
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 45
-
at pH 6.8, recombinant protein
25 - 80
-
25-50C: maximal activity, 60C, 89% of maximal activity, 70C: 57% of maximal activity; 80C: 27% of maximal activity
40 - 90
Q9UWJ5
no activity at 25C, activity increases from 40C to 90C, the highest assay temperature used
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.6
-
isoelectric focusing
4.7
Q45RT9
isoelectric focusing
4.8
O69174
chromatofocusing
5.3
-
calculated from amino acid sequence
5.4
-
calculated from amino acid sequence
5.54
D7NHW9
sequence calculation
5.6 - 5.9
Q9LEJ0
calculated from amino acid sequence
5.6
A5JQI1
isoelectric focusing
5.6
B8Q027
calculated from amino acid sequence
5.87
-
isoelectric focusing
5.9
-
isoelectric focusing
6
-
isoelectric focusing
6.2
Q27655
2D-gel electrophoresis
6.37
-
sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Q8IJN7
human serum samples collected from residents living in areas of Eastern India, where Plasmodium falciparum is endemic, 96% reactivity of the recombinant enolase r-Pfren determined
Manually annotated by BRENDA team
Q7RA60
mice hosts, for SDS-PAGE and immunoblot analysis
Manually annotated by BRENDA team
Plasmodium yoelii 17XL
-
mice hosts, for SDS-PAGE and immunoblot analysis
-
Manually annotated by BRENDA team
-
enolase 1 is only expressed in bradyzoites
Manually annotated by BRENDA team
-
the brain alpha,gamma and gamma,gamma forms are not detectable in the early embryonic stage and increase gradually during the development of the brain, whereas the alpha,alpha form exists at an almost constant level during development, enolase I (alpha,alpha-enolase), enolase II (alpha,gamma-enolase), enolase III (gamma,gamma-enolase)
Manually annotated by BRENDA team
-
enolase I (alpha,alpha-enolase), enolase II (alpha,gamma-enolase), enolase III (gamma,gamma-enolase)
Manually annotated by BRENDA team
-
ENOA is upregulated
Manually annotated by BRENDA team
-
cell surface ENOA is enhanced
Manually annotated by BRENDA team
-
ENOA is upregulated
Manually annotated by BRENDA team
-
ENOA is upregulated
Manually annotated by BRENDA team
Leuconostoc mesenteroides B-512FMCM
-
strain B-512FMCM
-
Manually annotated by BRENDA team
Steinernema glaseri NC
-
-
-
Manually annotated by BRENDA team
-
ENOA is upregulated
Manually annotated by BRENDA team
-
ENOA is upregulated
Manually annotated by BRENDA team
-
enolase I and III
Manually annotated by BRENDA team
-
back and hind legs
Manually annotated by BRENDA team
Steinernema glaseri NC
-
-
-
Manually annotated by BRENDA team
A1J8J9
of infected hosts Mesocricetus auratus and Rattus norvegicus, excretory and secretory products after infection analyzed
Manually annotated by BRENDA team
-
ENOA is upregulated
Manually annotated by BRENDA team
Q8MU59
L3 state
Manually annotated by BRENDA team
D7NHW9
constitutive expression of gene LOS2
Manually annotated by BRENDA team
-
ENOA is upregulated
Manually annotated by BRENDA team
-
ENOA is upregulated
Manually annotated by BRENDA team
-
ENOA is upregulated
Manually annotated by BRENDA team
-
hindlimb muscle
Manually annotated by BRENDA team
-
contains only enolase III
Manually annotated by BRENDA team
Trichinella spiralis ISS413
-
-
-
Manually annotated by BRENDA team
-
ENOA is upregulated
Manually annotated by BRENDA team
-
ENOA complexes with annexin A2, cytokeratin 8 and tissue-type plasminogen activator in raft membrane fractions of pancreatic cancer cells
Manually annotated by BRENDA team
-
for in vivo binding studies to human plasminogen
Manually annotated by BRENDA team
Leishmania mexicana AZV
-
for in vivo binding studies to human plasminogen
-
Manually annotated by BRENDA team
-
ENOA is upregulated
Manually annotated by BRENDA team
D7NHW9
constitutive expression of gene LOS2
Manually annotated by BRENDA team
Q967Y8
isolated after infection of 2-week-old White Leghorn PA12 chickens for 68 h, protein but not cDNA detected in the sporozoite stage, expression enhanced during the first schizogony
Manually annotated by BRENDA team
Eimeria tenella PaPt36
-
isolated after infection of 2-week-old White Leghorn PA12 chickens for 68 h, protein but not cDNA detected in the sporozoite stage, expression enhanced during the first schizogony
-
Manually annotated by BRENDA team
-
contains a single enzyme form, beta,beta-enolase, complete switching from alpha,alpha enolase to beta,beta enolase during the period around hatching
Manually annotated by BRENDA team
P17182, P21550
alpha,beta heterodimer and beta,beta homodimer in striated muscle, interaction with tubulin during differentiation of muscle satellite cells but not in undifferentiated myoblasts, immobilized beta,beta-enolase interacts with tubulin in vitro
Manually annotated by BRENDA team
P17182, P21550
satellite cell differentiation, alpha,alpha-enolase highly expressed during early ontogenesis, concentration of alpha,alpha-enolase in skeletal muscle varies from 0.1 mM to 0.01 mM until differentiation, binding affinity to tubulin is about 0.2 microM, alpha,beta heteroassociation with tubulin in muscle under physiological conditions
Manually annotated by BRENDA team
-
muscle-specific enolase
Manually annotated by BRENDA team
-
ENOA is upregulated
Manually annotated by BRENDA team
-
testicular, epididymal and ejaculated
Manually annotated by BRENDA team
D7NHW9
constitutive expression of gene LOS2
Manually annotated by BRENDA team
Steinernema glaseri NC
-
-
-
Manually annotated by BRENDA team
-
enolase 2 is only expressed in tachyzoites
Manually annotated by BRENDA team
C9YSH7
present in the teratocytes and released in the host haemocoel
Manually annotated by BRENDA team
-
recovered from liver, the enzyme expression in reduced in trophozoites continuously cultured in axenical conditions, semi-qiantitative RT-PCR expression analysis
Manually annotated by BRENDA team
Entamoeba histolytica HM-1-IMSS
-
recovered from liver, the enzyme expression in reduced in trophozoites continuously cultured in axenical conditions, semi-qiantitative RT-PCR expression analysis
-
Manually annotated by BRENDA team
Entamoeba invadens IP-1
-
-
-
Manually annotated by BRENDA team
additional information
-
5 isoenzymes, one isoenzyme form is present in all tissues tested, two additional forms are expressed in oocytes, embryos, adult liver and adult brain, two further forms are restricted to larval and adult muscle
Manually annotated by BRENDA team
additional information
-
present in all human organs but at levels less than 3% of those found in human brain, with especially low levels in liver, kidney, and skeletal muscle, and with the highest level in adrenal and large intestine
Manually annotated by BRENDA team
additional information
-
the embryonic alpha,alpha isoform remains distributed in many adult cell types, wheras a transition towards beta,beta-isoform and gamma,gamma-isoform occurs in striated muscle cells and neurons respectively
Manually annotated by BRENDA team
additional information
-
ENO1 is expressed in most heterotrophic tissues but not in the mesophyll of leaves
Manually annotated by BRENDA team
additional information
-
enolase 1 is a glycolytic enzyme expressed in most tissues
Manually annotated by BRENDA team
additional information
-
enolase expression analysis in adult worm, metacercaria, cercaria and egg. Csenolase is transcribed at the four life stages of Clonorchis sinensis while showing a significant higher expression level at the stage of adult worm
Manually annotated by BRENDA team
additional information
-
from mature cysts obtained from human stools
Manually annotated by BRENDA team
additional information
D7NHW9
PtrLOS2 expression in roots and stems is much higher than that in leaves under normal conditions, however, the expression of PtrLOS2 is upregulated in leaves, but downregulated in roots after cold treatments. The PtrLOS2 expression in stems is firstly up-regulated and then down-regulated after cold treatments
Manually annotated by BRENDA team
additional information
Q5DDV5
the enolase gene is highly expressed at 18-28 days of the life cycle, RT-PCR expression analysis
Manually annotated by BRENDA team
additional information
-
tissue-specific expression of isozymes: ENOA is present in almost all adult tissues, beta-enolase is expressed in muscle tissues, and gamma-enolase is found in neurons and neuroendocrine tissues
Manually annotated by BRENDA team
additional information
Entamoeba histolytica HM-1-IMSS
-
from mature cysts obtained from human stools
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
putative ENOA translocation mechanism, overview
Manually annotated by BRENDA team
-
secreted enzyme associated to the external surface of the parasite
Manually annotated by BRENDA team
Bifidobacterium animalis subsp. lactis BI07, Bifidobacterium bifidum S16, Paracoccidioides brasiliensis ATCC MYA-826, Bifidobacterium breve BBSF, Bifidobacterium longum S123, Streptococcus suis 05ZYH33
-
-
-
Manually annotated by BRENDA team
Streptococcus pneumoniae R36A
-
-
-
Manually annotated by BRENDA team
-
low amounts of surface-exposed enolase, determined on viable pneumococci, monoclonal and polyconal antibodies used
Manually annotated by BRENDA team
Q967Y8
partly localized inside the nucleus of sporozoites and schizonts, partly secreted, apex of the first generation of merozoites, relocalization inside sporozoites observed
Manually annotated by BRENDA team
Q8IJN7
surface-localization on merozoites determined by indirect immunofluorescence assay
Manually annotated by BRENDA team
Q7RA60
surface-localization on merozoites determined by indirect immunofluorescence assay
Manually annotated by BRENDA team
Streptococcus pneumoniae R36A, Bifidobacterium animalis subsp. lactis BI07
-
-
-
Manually annotated by BRENDA team
Eimeria tenella PaPt36
-
partly localized inside the nucleus of sporozoites and schizonts, partly secreted, apex of the first generation of merozoites, relocalization inside sporozoites observed
-
Manually annotated by BRENDA team
Bifidobacterium bifidum S16, Bifidobacterium breve BBSF, Borrelia burgdorferi B31-MI-16, Vibrio parahaemolyticus ATCC33847, Entamoeba invadens IP-1, Bifidobacterium longum S123
-
-
-
Manually annotated by BRENDA team
Plasmodium yoelii 17XL
-
surface-localization on merozoites determined by indirect immunofluorescence assay
-
Manually annotated by BRENDA team
-
as part of the degradosome complex
Manually annotated by BRENDA team
P17182, P21550
cytosolic fractions of myoblasts and myotubes, microtubule-association of alpha,alpha-enolase in undifferentiated myoblasts and in myotubes, also nuclear localization in myoblasts but not in myotubes determined, role of enolases in cytoskeletal dynamics during myoblast differentiation assumed
Manually annotated by BRENDA team
-
enzyme activity only in cytosolic fraction, inactive form detected in the microsomal fraction, membrane-association and localization at the external face of the plasma membrane determined by digitonin treatment and immunofluorescence studies
Manually annotated by BRENDA team
-
microsomal fraction analyzed
Manually annotated by BRENDA team
P17182, P21550
nuclear localization in myoblasts not detected, direct interaction with microtubules and tubulin during myoblast differentiation identified, role in cytoskeletal dynamics during myoblast differentiation assumed
Manually annotated by BRENDA team
-
small portion of enolase bound to vacuoles, in vitro stimulation of vacuole fusion determined
Manually annotated by BRENDA team
-
isozyme enolase 2
Manually annotated by BRENDA team
Paracoccidioides brasiliensis ATCC MYA-826
-
-
-
Manually annotated by BRENDA team
Leishmania mexicana AZV
-
enzyme activity only in cytosolic fraction, inactive form detected in the microsomal fraction, membrane-association and localization at the external face of the plasma membrane determined by digitonin treatment and immunofluorescence studies, microsomal fraction analyzed
-
Manually annotated by BRENDA team
-
secreted enzyme associated to the external surface of the parasite
-
Manually annotated by BRENDA team
Leptospira interrogans 56601, Paracoccidioides brasiliensis ATCC MYA-826, Vibrio parahaemolyticus ATCC33847
-
-
-
-
Manually annotated by BRENDA team
-
caudal flagellum
-
Manually annotated by BRENDA team
-
association of enolase with the food vacuole
Manually annotated by BRENDA team
-
in some human cancer cell lines
Manually annotated by BRENDA team
Vibrio parahaemolyticus ATCC33847
-
-
-
Manually annotated by BRENDA team
Borrelia burgdorferi B31-MI-16
-
-
-
-
Manually annotated by BRENDA team
-
enolase does not contain a detectable secretion signal or membrane anchor region that can explain its membrane localization
Manually annotated by BRENDA team
-
synaptic plasma membrane
Manually annotated by BRENDA team
-
outer membrane vesicle
Manually annotated by BRENDA team
-
outer membrane vesicle
-
Manually annotated by BRENDA team
P00925
up to 7% of enolase activity associated with mitochondria, targeting towards the mitochondrial outer membrane, affinity to the mitochondrial surface more than 10fold higher for Eno2p than for Eno1p
Manually annotated by BRENDA team
additional information
-
alpha-enolase is not detected in the nucleus
-
Manually annotated by BRENDA team
additional information
-
in asexual stages, enolase is predominantly present in soluble fraction, while in sexual stages it is mostly associated with particulate fraction
-
Manually annotated by BRENDA team
additional information
-
enolase as both an excretory/secretory product and a tegumental component of Clonorchis sinensis, immunohistochemical analysis
-
Manually annotated by BRENDA team
additional information
-
enolase is found both in the secretome and in association with the surface
-
Manually annotated by BRENDA team
additional information
-
enolase is found both in the secretome and in association with the surface of Leishmania spp.
-
Manually annotated by BRENDA team
additional information
-
enolase is found both in the secretome and in association with the surface of Leishmania spp., no activity in microsomes. Enolase does not contain a detectable secretion signal or membrane anchor region that can explain its membrane localization
-
Manually annotated by BRENDA team
additional information
-
enolase is specifically located inside vesicles containing densely packed fibrilar material
-
Manually annotated by BRENDA team
additional information
-
in breast, lung and pancreatic neoplasia, ENOA is localized on the surface of cancer cells, whereas in melanoma and nonsmall cell lung carcinoma cells it can also be secreted by exosomes
-
Manually annotated by BRENDA team
additional information
-
the enzyme is not exposed on the cell surface
-
Manually annotated by BRENDA team
additional information
Entamoeba histolytica HM-1-IMSS
-
enolase is specifically located inside vesicles containing densely packed fibrilar material
-
-
Manually annotated by BRENDA team
additional information
-
the enzyme is not exposed on the cell surface
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Bacillus subtilis (strain 168)
Campylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168)
Coxiella burnetii (strain RSA 493 / Nine Mile phase I)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Lactobacillus gasseri (strain ATCC 33323 / DSM 20243 / JCM 1131 / NCIMB 11718 / AM63)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394)
Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394)
Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394)
Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Trypanosoma cruzi (strain CL Brener)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22000
-
monomeric enzyme form, gel filtration, nondenaturing PAGE
33630
25710
-
MALDI-TOF, double charged monomer
664835
45000
-
SDS-PAGE
664971
46000
-
recombinant enzyme, Western blotting
666529
46000
A1J8J9
gel filtration, induced expression of the recombinant protein in Escherichia coli
679701
46220
Q8GR70
calculated from amino-acid sequence
651805
46620
Q8GR70
determined by mass spectrometry
651805
46940
P25704
mass spectrometry
650385
47000
-
SDS-PAGE
696424
47000
Q4KVK5
immunoblot analysis
697812
47000
Q2THT8
immunoblot analysis
697812
47000
Q4KYL2
immunoblot analysis
697812
47000
Q4KYL6
immunoblot analysis
697812
47000
-
calculated from amino acid sequence
701517
47000
P04764
-
703811
47000
-
SDS-PAGE
706464
47000
-
SDS-PAGE
706933
47550
Q1ET73
deduced from sequence
679893
48000
Q96VP4
SDS-PAGE
681072
48000
-
SDS-PAGE
703596
48000
-
alpha-enolase
705257
48000
-
SDS-PAGE
705532
48000
-
enolase 2 and enolase 1, SDS-PAGE
705542
48000
-
SDS-PAGE
705745
48060
-
MALDI-TOF mass spectrometry
705532
49000
-
dimeric enzyme form, gel filtration, native PAGE
33630
49000
Q8KNX9
SDS-PAGE
666254
49000
P00925
gel electrophoresis
680008
50000
-
SDS-PAGE
664835
50000
Q967Y8
gel electrophoresis
674072
50000
-
SDS-PAGE
679699
50000
-
gel filtration
701517
50000
Q45RT9
SDS-PAGE
705569
51000
-
His-tagged enzyme, SDS-PAGE
701517
51380
-
MALDI-TOF, single charged monomer
664835
51400
-
MALDI-TOF
664835
51400
Q1ET73
SDS-PAGE
679893
51500
-
calculated from amino acid sequence
703731
52000
O69174
2D-PAGE
666252
52000
-
-
700041
54000
A5JQI1
SDS-PAGE
705077
61200
-
estimated from SDS-PAGE
703731
62000
-
gel filtration
33611
63700
-
calculation from sedimentation and diffusion data
33599
77000
-
gel filtration
33617
82000
-
low speed sedimentation without reaching equilibrium
33601
84970
-
muscle enolase, calculation from amino acid composition
33639
85000
-
sucrose density gradient ultracentrifugation
33638
85000
-
muscle enzyme, equilibrium sedimentation
33639
85500
-
gel filtration
33633
88000
-
sedimentation velocity measurement
33602
89020
-
liver enolase, calculation from amino acid composition
33639
90000
-
sedimentation velocity and sedimentation equilibrium experiments
33600
90000
P00924
far-UV CD spectroscopy after size-exclusion chromatography
696102
91000
-
liver enzyme, gel filtration
33604
92000
-
gel filtration
33622
92000
-
gel filtration
33631
92000
-
liver enzyme, equilibrium sedimentation
33639
93000
-
muscle enzyme, gel filtration
33604
93000
-
gel filtration
33619
93000
-
gel filtration
33626
93000
-
gel filtration
33631
93000
E9NJD0
gel filtration
730374
94000
-
gel filtration
33631
94000
-
native enzyme, gel filtration
701579
95500
-
gel filtration
33631
96000
-
gel filtration, mutant N207A enzyme; gel filtration, wild type enzyme
653043
98000
C9YSH7
gel filtration
704025
100000
-
sucrose density gradient centrifugation
33611
100000
-
gel filtration
33614
100000
-
gel filtration
664835
102800
-
MALDI-TOF, double charged dimer
664835
110000
-
gel filtration
33602
155000
-
gel filtration
701914
300000
-
non-denaturing PAGE
33627
335000
-
gel filtration
33609
338000
-
gel filtration
33627
345000
-
gel filtration, high-speed equilibrium sedimentation
33637
350000
-
equilibrium sedimentation
33632
370000
-
gel filtration
666033
370000
K7N5M7
sedimentation velocity analysis
730857
440000
C6GGT7
gel filtration
704963
452000
-
calculated molecular mass
706454
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 47000, SDS-PAGE
?
-
x * 47000, SDS-PAGE
?
Q27655
x * 47000, SDS-PAGE
?
B8Q027
x * 47000, SDS-PAGE
?
-
x * 48000, SDS-PAGE
?
-
x * 48000, SDS-PAGE
?
-
x * 50000, SDS-PAGE
?
-
x * 50000, SDS-PAGE
?
Q97QS2
x * 45000, SDS-PAGE
?
-
x * 56000, SDS-PAGE
?
-
x * 46000, SDS-PAGE
?
-
x * 46000, enzyme R-NSE, enzyme Y-NSE, SDS-PAGE
?
-
x * 46914, calculation from nucleotide sequence
?
-
x * 47000, Y-NSE.H6, SDS-PAGE
?
-
x * 49000, SDS-PAGE
?
-
x * 46461, calculated from amino-acid sequence
?
-
x * 46500, SDS-PAGE, H159A and H159G mutants, x * 46500, SDS-PAGE, wild type
?
Q9LEJ0
x * 47600, calculated from amino acid sequence
?
P04764
x * 47000 about, 2D-gel electrophoresis
?
-
x * 45000-66200, recombinant solubilized enzyme, SDS-PAGE
?
-
x * 47450, sequence calculation and mass spectrometry
?
D7NHW9
x * 47790, sequence calculation
?
Q2YPV0
x * 49000, recombinant His-tagged enolase, SDS-PAGE
?
Q5DDV5
x * 50000, recombinant His-tagged enolase, SDS-PAGE
?
B8Q027
x * 47200, calculated from amino acid sequence
?
-
x * 163000, SDS-PAGE
?
-
x * 46672, isoform Eno1p, calculated from amino acid sequence, x * 46673, isoform Eno1p, electrospray ionization mass spectrometry
?
-
x * 47000, calculated from amino acid sequence
?
-
x * 47074, calculated from amino acid sequence
?
-
x * 47181, isoform Err3p, calculated from amino acid sequence, x * 47184, isoform Err3p, electrospray ionization mass spectrometry, x * 47196, isoform Err2p, calculated from amino acid sequence, x * 47198, isoform Err2p, electrospray ionization mass spectrometry
?
W6ABG9
x * 48000, calculated from amino acid sequence
?
-
x * 48000, MALDI-TOF mass spectrometry
?
W6ABG9
x * 52000, His6-tagged enzyme, SDS-PAGE
?
-
x * 46672, isoform Eno1p, calculated from amino acid sequence, x * 46673, isoform Eno1p, electrospray ionization mass spectrometry, x * 47181, isoform Err3p, calculated from amino acid sequence, x * 47184, isoform Err3p, electrospray ionization mass spectrometry, x * 47196, isoform Err2p, calculated from amino acid sequence
-
?
Streptococcus pneumoniae R36A
-
x * 45000, SDS-PAGE
-
?
Entamoeba histolytica HM-1-IMSS
-
x * 48000, SDS-PAGE
-
?
Borrelia burgdorferi B31-MI-16
-
x * 50000, SDS-PAGE
-
?
Vibrio parahaemolyticus ATCC33847
-
x * 48000, calculated from amino acid sequence, x * 52000, His6-tagged enzyme, SDS-PAGE
-
?
Steinernema glaseri NC
-
x * 47000, SDS-PAGE, x * 47200, calculated from amino acid sequence
-
?
Brucella abortus A19
-
x * 49000, recombinant His-tagged enolase, SDS-PAGE
-
?
Peptoclostridium difficile MC201
-
x * 163000, SDS-PAGE
-
?
-
x * 47000, calculated from amino acid sequence
-
?
Lactobacillus plantarum LM3
-
x * 48000, MALDI-TOF mass spectrometry
-
dimer
-
2 * 45000, SDS-PAGE
dimer
-
2 * 45000, SDS-PAGE
dimer
-
2 * 50000, SDS-PAGE
dimer
-
2 * 50000, SDS-PAGE
dimer
-
2 * 50000, SDS-PAGE
dimer
-
2 * 47000, SDS-PAGE
dimer
-
SDS-PAGE
dimer
-
2 * 51000, SDS-PAGE
dimer
-
2 * 48000, SDS-PAGE
dimer
-
2 * 52000, SDS-PAGE
dimer
-
2 * 52000, SDS-PAGE
dimer
-
2 * 46000, SDS-PAGE
dimer
-
alpha,gamma, 1 * 51000 + 1 * 52000, brain enolase II, SDS-PAGE, gamma,gamma, 2 * 52000, brain enolase III, SDS-PAGE, alpha,alpha, 2 * 51000, brain enolase I, SDS-PAGE
dimer
-
2 * 53000, liver enzyme, SDS-PAGE
dimer
-
2 * 48000, recombinant alpha-enolase
dimer
-
beta,beta, 2 * 51500, muscle enolase, SDS-PAGE
dimer
-
2 * 49000, enolase I, SDS-PAGE
dimer
-
2 * 49000, muscle enzyme, SDS-PAGE
dimer
-
1 * 46000 + 1 * 49000, enolase II, SDS-PAGE
dimer
-
2 * 44000, muscle enzyme, SDS-PAGE
dimer
-
2 * 46000, enolase III, SDS-PAGE
dimer
-
2 * 46000, gama,gamma-enolase, SDS-PAGE
dimer
-
2 * 46000, liver enzyme, SDS-PAGE
dimer
P00924
2 * 46000
dimer
-
2 * 45545, mass spectrometry and X-ray crystallography
dimer
-
native enzyme
dimer
C9YSH7
2 * 49000, gel filtration, the recombinant protein produced in bacteria under native conditions is a dimer
dimer
C4LXE8
in the crystal structure of 2-phospho-D-glycerate-complexed enzyme, ENO forms an asymmetric dimer with one active site in the open conformation and the other active site in the closed conformation, overview
dimer
-
the dimeric structure of Pfeno is required for the optimal vacuolar functions
heterodimer
-
alpha-gamma-heterodimer
heterodimer
-
engineered type
homodimer
-
-
homodimer
-
2 * 45000, SDS-PAGE
homodimer
-
2 * 47000, SDS-PAGE
homodimer
E9NJD0
2 * 48000, SDS-PAGE
homodimer
-
gel filtration
homodimer
Q9UWJ5
2 * 46000
homodimer
-
2 * 50000, gel filtration
homodimer
-
N80D/N126D
homodimer
-
2 * 50000, gel filtration
-
homooctamer
K7N5M7
-
octamer
C6GGT7
-
octamer
-
8 * 45000, SDS-PAGE
octamer
-
8 * 42000, SDS-PAGE
octamer
-
8 * 48000, a tetramer of dimers, SDS-PAGE
octamer
-
sedimentation velocity analysis
monomer
-
1 * 50000, gel filtration
additional information
Q5KVE7
composed of a N-terminal alpha,beta domain and a C-terminal domain consisting of eight alpha,alpha barrels, polypeptides packed as tight dimers
additional information
Q27727
dissociation studies of homodimeric enolases into their active monomeric forms, analysis of intersubunit interactions and influence on catalytic and structural stability, properties of monomeric enolase determined
additional information
-
epitope for plasminogen-binding localized in a surface-exposed loop in each of the monomers of the octameric enolase
additional information
Q1ET73
extracellular enolase predicted as octamer, with two of its subunits defining the asymmetric unit of the crystal
additional information
-
subunit dissociation of wild-type and G157D enolases by incubation with NaClO4 at 15C for 24 h, spectrometrically measured
additional information
-
the monomer of ENOA consists of a smaller N-terminal domain, residues 1-133, and a larger C-terminal domain, residues 141-431
additional information
-
the protein contains a potential nuclear localization sequence aa190-199 and several linear B cell epitopes and CTL T cell epitopes, of which the outside epitope aa49-57 and inside epitope aa228-236 are facultative T cell and B cell epitope, and the linear B cell epitope aa206-213 contains the active center site Glu210, suggesting the putative protein is a potential membrane with strong immunogenicity
additional information
Leuconostoc mesenteroides B-512FMCM
-
extracellular enolase predicted as octamer, with two of its subunits defining the asymmetric unit of the crystal
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
acetylation
-
-
phosphoprotein
-
-
alkylation
-
methylation
additional information
-
ENOA in tumor cells is subjected to more acetylation, methylation and phoshorylation than in normal tissues
side-chain modification
-
acetylation, methylation
additional information
P00924
in vivo- and in vitro-glycation induce a considerable irreversible activity loss
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant EhENO with two 2-phospho-D-glycerate substrate molecules bound at the two active sites, the protein solution contains 7.5 mg/ml protein in 100 mM Tris-HCl pH 7.5, 100 mM NaCl, 5 mM MgCl2, sitting-drop vapour-diffusion, 20C, mixing of equal volumes of precipitant solution, contraining 100 mM Bis-Tris, pH 5.5, 25% w/v PEG 3350, 200 mM ammonium sulfate, and protein solution, X-ray diffractrion structure determination and analysis at 1.9 A resolution, molecular replacement
C4LXE8
using the hanging drop method followed by recrystallization under the same conditions, X-ray structure solved by molecular replacement
Q8GR70
1.6 A resolution, co-crystallization of enolase with a synthetic peptide corresponding to residues 833 to 850 from RNase E determined, asymmetric binding of a single molecule of RNase E to a conserved cleft at the interface of the enolase dimer
P0A6P9
using the sitting drop method, co-crystallized with Mg2+
-
hanging drop method, 17 A resolution, X-ray coordinates and structure factors determined, complexes with phosphate, with Mg2+, with Mg2+ and HCO3-, with Mg2+ and the alternate substrate 2,3-diketohexane 1-phosphate identified, activated enolase carboxylated on Lys173, conserved Lys98 in the N-terminal domain determined for C1 proton abstraction
Q5KVE7
1.7 A resolution by multiwavelength anomalous diffraction and molecular replacement techniques
-
asymmetric complex NSE*Mg2SO4/NSE*MgCl, pH 7.0, large orthorhombic plates, structure by molecular replacement
-
at room temperature using the hanging-drop vapour-diffusion method for structure analysis by X-ray diffraction
-
enolase fluoride/phosphate inhibitory complex and enolase phosphate inhibitory complex
P09104
hanging drop vapor diffusion method, using 0.1 M ammonium acetate, 0.1 M bis-tris pH 5.5, 20% (w/v) polyethylene glycol monomethyl ether 2000
-
hanging drop vapor diffusion method, using 20% (w/v) PEG 550, 100 mM bicine pH 9.0, 100 mM sodium chloride
Q042F4
hanging drop method, from preparations of purified dextransucrase
Q1ET73
co-crystallization of the S39A mutant with Mg2+ and phosphonoacetohydroxamate, the active-site flap is opened
-
crystal structure of asymmetric dimer enolase-2-phospho-D-glycerate/enolase-phosphoenolpyruvate at 2.0 A resolution
-
engineered K345A/N80D/N126D heterodimer in complex with substrate/product, 1.85A resolution, batch method
-
mutant E211Q complexed with Mg2+ and phosphoenolpyruvate, mutant E168Q complexed with Mg2+ and 2-phospho-D-glycerate
-
structure of enolase-Zn2+/Mn2+ complex formation with phosphonoacetohydroxamate solved to 1.54 A resolution by X-ray crystallography, replacement of native Mg2+ ions with Mn2+/Zn2+ introduces only minor atom displacements in the binding site, crystallographic data refined, simulations reveal a model of the enolase active site chosen for the study indicating sites MI and MII either occupied with Mn2+ at site MI and Zn2+ at site MII or vice versa, stereo view of the coordination of the two metal ions in the enolase-inhibitor-complex and of key active site residues presented, rotation patterns shown
-
2.0 A resolution, molecular replacement, hanging-drop vapor-diffusion
-
hanging drop vapor diffusion method, using 0.1 M MES (pH 6.5) and 10% (w/v) PEG 20000
K7N5M7
hanging drop method
-
hanging drop method, six novel crystal structures with various ligation states and conformations identified, high structural diversity of loops near the catalytic site determined, novel metal-binding site within the catalytic site identified
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8
-
remains stable between pH 6.0 and 8.0
730926
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4
P25704
both the wild-type and the E414L mutant are stable as suspensions in ammonium sulfate
650385
25 - 62
Q2YPV0
maximally stable at 37C, the purified recombinant enolase is thermally stable at 25C, 37C, 50C, and 62C, but is completely inhibited by a preincubation of the enzyme at 75C after 1 h
716180
44.7
-
dimeric recombinant enolase shows two transitions which corresponds to dissociation of dimer in to monomer (Tm of 44.7C)
701914
50
-
heat shock protein, 50% of the activity retained after 1 h of incubation, 30% of the activity retained after 2 h of incubation
650872
55
-
60 min, in presence of Mg2+, enolase II retains more than 40% of its activity, brain enolase I and II lose 80% of their activities. In absence of Mg2+ all enolases quickly lose activity
33614
55.5
-
the melting temperature of isoform Eno1p, Err2, and Err3p are 55.5C, 60.5C, and 60C, respectively
731032
58.1
-
dimeric recombinant enolase shows two transitions which corresponds to unfolding of monomer (Tm of 58.1C)
701914
80
-
sensitive to moist heat at 80C
678997
88
Q9UWJ5
t1/2: 300 min
721409
100
Q9UWJ5
40 min, 50% inactivation. The half-life declines by a factor of about three in the presence of 700 mM KCl
721409
additional information
-
thermal stability is increased by divalent metal ions and binding to substrate, enzyme dissociates before denaturation
651535
additional information
Q27727
thermal stability different in monomeric and dimeric forms, the dimeric form is stable at 37C and shows 20-25% inactivation at 50C, the monomeric form is to 80% inactivated at 37C after 2h and completely inactivated at 50C
679767
additional information
-
thermal stability lower in mutant forms of enolase, wild-type enolase has Tm of 55.4C, whereas G367E and G157D reveals a Tm of 51.2C and 49.9C, respectively, addition of 50 microM phosphonoacetohydroxamate increases thermal stabilization of wildtype and G157D enolases, but not of G367E
679807
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme maintains only 5% of the initial catalytic activity upon glycation for the first 90 min
-
Mg2+, 20% sucrose or glycerol stabilize enzyme in dilute solutions
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
in the frozen state, stable for 6 months
-
4C, 70% saturated ammonium sulfate solution, stable for several months
-
-74C, pH 7.0, stable for up to 10 months, provided that multiple freezing and thawing steps are avoided
-
-20C, 10 mM Tris-HCL, pH 7.5, stable
-
4C, stable for several months
-
4C, 15% ethylene glycol, stable for at least 3 months
-
4C, 1 mg/ml or more, 0.1 M imidazole HCl, pH 7.0 and 2 mM MgCl2, stable for at least 2 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
glutathione-Sepharose-4B chromatography
Q8MU59
Ni-NTA-agarose column chromatography, gel filtration
C9YSH7
Ni-NTA column chromatography, gel filtration
-
recombinant protein, gel filtration
P37869
Ni2+-charged HiTrap chelating column
Q8KNX9
Ni-NTA resin column chromatography
Q45RT9
His-Trap column chromatography
-
MagneHis nickel-conjugated magnetic bead column chromatography, and gel filtration
-
Ni-NTA column chromatography, gel filtration
-
recombinant His-tagged enolase from Escherichia coli strain BL21 by nickel affinity chromatography
Q2YPV0
to homogeneity, using ammonium sulfate precipitation and DEAE-Sephadex column chromatography
-
using anion- and cation exchange chromatography
-
recombinant protein amounts are 10-15% of the total protein, purification from inclusion bodies yields 0.5 mg per liter, allergenic activity of the recombinant protein tested by ELIZA
Q96VP4
recombinant protein
A1J8J9
recombinant protein, pET22/14-X vector, His-tag purification, SDS-PAGE
Q967Y8
recombinant GST-tagged ENO from Escherichia coli BL21 (DE3) by glutathione affinity chromatography, cleavage of the GST tag, and gel filtration
C4LXE8
partial, using ammonium sulfate fractionation and gel filtration chromatography
Q8GR70
using gel filtration chromatography
-
recombinant protein, gel filtration
Q5KVE7
Ni-NTA column chromatography
-
using affinity chromatography to isolate a his-tagged recombinant enzyme, purification from latex using ammonium sulfate precipitation and gel filtration chromatography
Q9LEJ0
alpha,alpha-enolase and gamma,gamma-enolase
-
ammonium sulfate precipitation, DEAE-Sephadex A-50 gel filtration, CM-Sephadex gel filtration, and QAE-Sephadex gel filtration
-
DEAE and carboxymethyl columns, oligonucleotide affinity column
-
glutathione-Sepharose 4B bead chromatography, gel filtration
-
HiTrap Ni2+-chelating column chromatography and Superdex 75 gel filtration
-
isoforms S1, S2, S3
-
native enzyme from muscle by ammonium sulfate fractionation and ion exchange chromatography
-
Ni-NTA Sepharose, ion-exchange chromatography, ammonium sulfate precipitation
-
Ni2+-affinity column chromatography
-
ammonium sulfate precipitation, DEAE Sephadex A-50 gel filtration, Sephadex G-100 gel filtration
-
preparative electrophoresis
-
nickel affinity column chromatography
Q042F4
recombinant protein
-
recombinant protein and natural enolase
-
extracellular enolase identified from isolates of extracellular dextransucrase from cultures of Leuconostoc mesenteroides, accumulation as small crystals
Q1ET73
beta,beta-enolase
-
for localization studies, immunochemistry and confocal microscopy; gel filtration, for localization studies and tubulin-binding kinetics
P17182, P21550
purification of the wild-type and a mutant enzyme cloned in Escherichia coli using ammonium sulfate precipitation and Sephadex chromatography
P25704
gelatin-agarose affinity column chromatography
A5JQI1
using anion- and cation exchange chromatography
-
gel filtration, recombinant enolase of Plasmodium falciparum for vaccination studies in mice
Q8IJN7
gel-filtration
Q27727
glutathione-Sepharose beads chromatography, gel filtration
-
native enzyme partially by preparation of food vacuoles
-
Ni-nitrilotriacetic acid affinity chromatography, eluted with imidazole
-
gel filtration
Q7RA60
enolase 1, enolase II, enolase III
-
liver enzyme; muscle enzyme
-
ammonium sulfate precipitation and gel filtration
-
gel filtration of recombinant protein; gel filtration of recombinant protein
P00925
gel filtration, for in vitro import assays into mitochondria and three-hybrid analysis
P00925
Q-Sepharose column chromatography
-
recombinant proteins, SDS-PAGE
-
wild type and several mutant recombinant enzymes using chromatography on Sepharose
-
recombinant soluble His-tagged enzyme from Escherichia coli by nickel affinity chromatography
Q5DDV5
GSTrap FF column chromatography and Superdex 200 gel filtration
B8Q027
by ion-exchange chromatography and gel filtration
Q97QS2
ion exchange chromatography and gel filtration
-
recombinant protein, for epitope mapping and identification of plasminogen-binding motifs
-
Ni-NTA column chromatography
-
His-Trap column chromatography
C6GGT7
Ni-NTA column chromatography, gel filtration
-
nickel-affinity column chromatography and Superdex 200 gel filtration
K7N5M7
gamma,gamma-enolase
-
native enzyme from muscle by ammonium sulfate fractionation and ion exchange chromatography
-
Ni-NTA agarose column chromatography
E9NJD0
muscle-stage larvae isolated by pepsin-HCl digestion from mice, recombinant enzyme by His Trap chelating column
-
recombinant protein
-
using affinity chromatography to isolate a his-tagged recombinant enzyme followed by cleavage of the tag
-
His-Bind column chromatography
W6ABG9
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cDNA inserted in PGEX-4T-3 expressed in Escherichia coli, glutathione S-transferase fusion protein, protein with 436 amino acid residues, 70-80% sequence similarity to enolases from other organisms, including helminth parasites
Q8MU59
expressed in Escherichia coli Rosettagami (DE3) cells
C9YSH7
expressed in Escherichia coli BL21 cells
-
expressed in Escherichia coli
-
expressed in Escherichia coli, PCR-amplified genomic DNA from Bacillus subtilis strain 168 ligated into pET15b encoding an N-terminal six-His tag vector
P37869
expression in Escherichia coli strain BL21 AI with an N-terminal 10His-tag
Q8KNX9
expressed in Escherichia coli BL21 Star(DE3) cells
Q45RT9
expressed in Escherichia coli Rosetta (DE3) cells
-
expressed in Escherichia coli Rosetta (DE3)pLysS cells
-
expressed in Escherichia coli Rosetta cells
-
expression of His-tagged enolase in Escherichia coli strain BL21
Q2YPV0
gene LOS, DNA and amino acid sequence determination and analysis, semi-quantitative RT-PCR expression analysis, overview
D7NHW9
isolated from cDNA library, expressed in Escherichia coli BL21, expression vector pET22b, 60% sequence similarities to human non-neuronal alpha enolase, conserved residues determined
Q96VP4
expressed in Escherichia coli BL21 cells
-
clone Eg_PSGRS_13B09, cloning from cDNA library, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain BL21(DE3) in inclusion bodies
-
expressed in Escherichia coli strains M15 and SG13009 using expression vector pQE30, protein of 431 amino acids identified, homologies to other trematode enolases estimated
A1J8J9
identified from cDNA library, expression in Escherichia coli
Q967Y8
expression of GST-tagged ENO in Escherichia coli BL21 (DE3)
C4LXE8
gamma-enolase
-
expressed in Escherichia coli BL21, pET17b expression vector
Q5KVE7
expressed in Escherichia coli BL21(DE3) cells
-
expression in Escherichia coli of a his-tagged recombinant enzyme
Q9LEJ0
expressed in Escherichia coli
-
expressed in Escherichia coli BL21 cells
-
expressed in Escherichia coli BL21(DE3) cells
-
expression in Escherichia coli
-
expression in Escherichia coli strain JM109 with C-terminal His-tag
-
expression in Escherichia coli; neuron specific enolase and modified neuron-specific enolases: Y-NSE with one Tyr residue added at the N-terminal of the recombinant neuron-specific enolase
-
subcloned in Escherichia coli
-
the three genes, ENO1, ENO2 and ENO3, encoding for three isoforms of the enzyme, alpha-enolase, gamma-enolase, and beta-enolase, respectively, show high sequence identity
-
expressed in Escherichia coli
Q042F4
expressed in Escherichia coli BL21 cells
-
isolated from a genomic library, over-expressed in Escherichia coli, expression vector pET28a
-
expressed in Escherichia coli BL21(DE3)pLysS using the pRSETA expression vector, recombinant His-tagged protein
Q1ET73
co-expression of enolase 1 in bone marrow-derived mast cells with calreticulin
-
expression of recombinant wild-type and mutant enzymes in Escherichia coli
P25704
expression of GST-tagged enolase in Escherichia coli
A5JQI1
ability of Pfeno to complement a mutant Saccharomyces cervisiae strain R11258 deficient in enolase activity. In this strain Tetr-Eno2, the enolase 1 gene is deleted and expression of the enolase 2 gene is under the control of a tetracycline repressible promoter. Pfeno is able to restore all three phenotypic effects fully or partially, i.e. growth retardation, vacuolar fragmentation and altered expression of certain vacuolar proteins, overview
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli, expression vector pQE30, His-tagged fusion protein
Q8IJN7
expressed in Escherichia coli, His-tagged recombinant protein
Q27727
expression in Escherichia coli strain XL1Blue as an N-terminal His6-tagged protein
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expressed in Escherichia coli, expression vector pQE30, His-tagged fusion protein
Q7RA60
expression of His-tagged alpha-enolase in Escherichia coli strain BL21(DE3)
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli, His-tagging and GST-tagging of recombinant enolase protein; expressed in Escherichia coli, His-tagging and GST-tagging of recombinant enolase protein
P00925
expression in Escherichia coli
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expression of the mutants E211Q and E168Q in Escherichia coli
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expression of the recombinant H159A and H159G mutants in Escherichia coli
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expression of wild-type and mutant genes in Escherichia coli
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inserted into pET-3a, expressed in Escherichia coli BL21-DE3, site-directed mutagenesis performed
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over-expression in Escherichia coli strain BL21, expression vector pET3a, His-tagged recombinant protein
P00925
DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression of His-tagged enzyme in Escherichia coli
Q5DDV5
expressed in Escherichia coli BL21(DE3) cells
B8Q027
expressed in Escherichia coli host strain M15-pREP4, His-tagged protein
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expression in Escherichia coli
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expressed in Escherichia coli BL21(DE3) cells
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expression in Escherichia coli strain XL1-Blue and BL-21 with N-terminal His-tag
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expressed in Escherichia coli BL21 (DE3) cells
C6GGT7
expressed in Escherichia coli BL21(DE3) cells
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subcloned in Escherichia coli
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expressed in Escherichia coli BL21(DE3) cells
E9NJD0
expression in Escherichia coli strain DH5alpha with His-tag, recombinant enzyme without enolase activity, gaines activity after cutting off the signal peptide from the full-length protein
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recombinant protein expressed as a glutathione S-transferase GST::tv-ENO1 fusion protein in Escherichia coli, cleaved using thrombin
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expression in Escherichia coli of a his-tagged recombinant enzyme
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recombinant enolase, expressed in Escherichia coli BL21-DE3-pLysS strain harbouring the recombinant pET28a plasmid
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expressed in Escherichia coli BL21 cells
W6ABG9
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enolase is induced by cold stress and cAMP but not by heat stress
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PtrLOS2 expression in roots and stems is much higher than that in leaves under normal conditions, however, the expression of PtrLOS2 is upregulated in leaves, but downregulated in roots after cold treatments. The PtrLOS2 expression in stems is firstly up-regulated and then down-regulated after cold treatments. Abscisic acid treatment leads to upregulation of expression of PtrLOS2in leaves, while in stems and roots it is firstly downregulated and then followed by upregulation
D7NHW9
enolase protein level decreases by more than 50% after 1.5-3 h exposure to hyperosmotic salt stress
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enolase is induced under heat-shock treatment
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levels of enolase mRNA are increased in encysting cells
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levels of enolase mRNA are increased in encysting cells
Entamoeba invadens IP-1
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In human follicular thyroid carcinoma cells, retinoic acid causes a decrease in ENOA levels that coincides with their reduced motility
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alpha-enolase is consistently up-regulated from mild cognitive impairment to Alzheimer's disease
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alpha-enolase is overexpressed at both mRNA and protein levels in pancreatic ductal adenocarcinoma cells
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alpha-enolase is up-regulated in pancreatic ductal adenocarcinoma
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lipopolysaccharide rapidly up-regulates ENO-1 cell-surface expression
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ENOA expression is enhanced in diverse cancer cell types, e.g. cell surface ENOA in breast cancer cells, overview
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tyrosine nitration inactivates enolase
P04764
after 6 weeks of streptozotocin administration, the cardiac proteins from diabetic rats show the levels of alpha-enolase expression and protein tyrosine nitration are clearly increased, whereas the enolase activity and oxidation status are not significantly changed
P04764
the introduction or expression of enolase 2 double stranded RNA successfully silences the expression of enolase 2 at the levels of transcripts and proteins
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K147A
Q5KVE7
requires a 10fold greater concentration of protein for observation of enolization
K173A
Q5KVE7
detectable activity of about 3% of that of wild-type enolase, retains ability to enolize the desthio substrate
D257K
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the mutation has no effect on excystation
K255A
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while the binding activity of the mutated protein is drastically reduced, the residual enzymatic activity is more than 50% of the wild type enzyme
K259A K255A
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while the binding activity of the mutated protein is drastically reduced, the residual enzymatic activity is more than 50% of the wild type enzyme
K259A/K422A K255A
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while the binding activity of the mutated protein is drastically reduced, the residual enzymatic activity is more than 50% of the wild type enzyme
K422A K255A
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while the binding activity of the mutated protein is drastically reduced, the residual enzymatic activity is more than 50% of the wild type enzyme
K255A
Lactobacillus plantarum LM3
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while the binding activity of the mutated protein is drastically reduced, the residual enzymatic activity is more than 50% of the wild type enzyme
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K259A K255A
Lactobacillus plantarum LM3
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while the binding activity of the mutated protein is drastically reduced, the residual enzymatic activity is more than 50% of the wild type enzyme
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K259A/K422A K255A
Lactobacillus plantarum LM3
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while the binding activity of the mutated protein is drastically reduced, the residual enzymatic activity is more than 50% of the wild type enzyme
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E168Q
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the mutant has approximately 0.01% of the activity of native enolase. It binds 3-aminoenolpyruvate-2-phosphate, the 3-amino analogue of the product phosphoenolpyruvate and D-tartronate semialdehyde-2-phosphate, the aldehyde analogue of the substrate 2-phosphoglycerate, the latter two with affinities similar to those of the native enzyme
E168Q
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severely depressed activity, does not catalyze hydrolysis of (Z)-3-chloro-2-phosphoenolpyruvate by addition of OH- and elimination of Cl- at C-3, alters the tautomeric state or catalyzes ionization of bound tartronate semialdehyde phosphate
E168Q
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the Mg2+ binding site is different compared to the wild type enzyme
E211Q
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severely depressed activity, alters the tautomeric state or catalyzes ionization of bound tartronate semialdehyde phosphate. Glu211 participates in the second step of the reaction
E211Q
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can exchange the alpha proton of 2-phospho-D-glycerate, but cannot catalyze the complete dehydration to phosphoenolpyruvate
E211Q
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inactive, but properly folded
G157D
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correctly folded, less stable than wild-type enolase, dissociation into subunit forms accelerated
G376E
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correctly folded, less stable than wild-type enolase, dissociation into subunit forms accelerated
H159A
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less than 1% of the activity compared to the wild type
H159A
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mutation has no effect on conformation or enzyme-ligand complex, but yields an inactive enzyme
H159F
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less than 1% of the activity compared to the wild type
H159G
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inactive form
H159N
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less than 1% of the activity compared to the wild type
K345A
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severely depressed activity, does not catalyze hydrolysis of (Z)-3-chloro-2-phosphoenolpyruvate by addition of OH- and elimination of Cl- at C-3, fails to catalyze the exchange of the C-2 proton of 2-phospho-D-glycerate with deuterium in D2O, inactive in ionization of tartronate semialdehyde phosphate. Lys345 functions as the base in the ionization of 2-phosphoglycerate
K345A
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inactive
N207A
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50% of the activity compared to the wild type
N80D/N126D
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mutant with surface mutations to facilitate ion-exchange chromatographic separation
S39A
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mutant of isoenzyme 1, relative maximal velocity of 0.01% and an activation constant for Mg2+ ca. 10fold higher, compared with the native enzyme
S39A
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inactive mutant
deltaK433/K434
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mutant with different oligomerization state
K433L/K434L
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mutant with different oligomerization state
K434L
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mutant with different oligomerization state
DELTA434-435
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mutant with decreased Glu- and Lys-plasminogen-binding activities
F137L/E363G
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the dimer-dimer interface mutant destabilizes the octameric structure, the double mutant is more easily dissociated in the presence of NaClO4 than is the wild type
K434L/K435L
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mutant with decreased Glu- and Lys-plasminogen-binding activities
K98A
Q5KVE7
unable to catalyze the enolase reaction
additional information
Q5KVE7
site-directed mutagenesis of active site residues, spectrophotometric activity assay performed with elevated concentrations of the mutant enzymes
H389Q/R390S
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the mutations significantly inhibit excystation
additional information
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recombinant neuron-specific enolase (R-NSE) has markedly decreased binding affinity to anti-neuron-specific enolase antibodies. Reactivity of modified neuron-specific enolases (Y-NSE with one Tyr residue added at the N-terminal of the recombinant neuron-specific enolase. Y-NSE.H6 with six His residues further added at the C-terminal of recombinant neuron-specific enolase) to the antibody is almost equivalent to that of human brain gamma,gamma-enolase
K422A K255A
Lactobacillus plantarum LM3
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while the binding activity of the mutated protein is drastically reduced, the residual enzymatic activity is more than 50% of the wild type enzyme
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additional information
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enolase 1 gene silencing by siRNA leading to reduced the mRNA and protein expressions of surface receptor Fc-RIalpha, surface molecules, such as c-kit, CD40, CD40 ligand and 373 VCAM-1, and also reduced granular tryptase in the culture periods, as well as expressions of enolase 1 and calreticulin. Enolase 1 or calreticulin siRNA transfected-bone marrow-derived mast cells remarkably reduce [Ca2+]i levels compared to wild-type bone marrow-derived mast cells. Both protein siRNA transfected-bone marrow-derived mast cells reduced [Ca2+]i levels more than by individual protein transfection, but does not show additive effect
E414L
P25704
this mutant has the same activity than the wild-type enzyme
additional information
A5JQI1
immobilization of purified recombinant enolase
additional information
Paracoccidioides brasiliensis ATCC MYA-826
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immobilization of purified recombinant enolase
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E414L
Q27727
replacement of an interface glutamate residue with a leucine does not result into dimer dissociation
additional information
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deletion of a plant like pentapeptide insert 104EWGWS108 in a highly conserved surface loop of the protein results in about 100fold decrease in kcat/Km and causes dissociation of dimeric form into monomers
K345A/N80D/N126D
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heterodimer with one inactive K345A subunit and one active N80D and N126D subunit
additional information
P00925
engineered enolase forms disrupted in catalytic activity retain features to direct mitochondrial import of tRNA
additional information
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folding studies, dissociation experiments, determination of thermal and enzymatic stability
additional information
P00925
impaired catalytic activity of enolase retains in vitro stimulation of fusion of isolated vacuoles, partial inactivity of enolase diminishes vacuole fusion, enolase-deficient vacuoles lacks in vitro stimulation of vacuole fusion, impaired catalytic activity of enolase retains in vitro stimulation of vacuole fusion, partial inactivity of enolase diminishes vacuole fusion, enolase-deficient vacuoles lacks in vitro stimulation of vacuole fusion
K435L
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mutant with decreased Glu- and Lys-plasminogen-binding activities
additional information
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replacement of the C-terminal lysine residues by leucine reduces Glu- and Lys-plasminogen-binding properties
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
solubilization of the recombinant enzyme from Escherichia coli inclusion bodies by 6 M urea
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
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the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
medicine
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the tegumental membrane protein enolase is a vaccine candidate
drug development
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the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
medicine
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alpha-enolase is a pancreatic ductal adenocarcinoma-associated antigen
medicine
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changes in tumor ENO-1 levels are related to clinical 4-hydroxytamoxifen therapeutic outcome, downregulation of ENO-1 can be utilized as a pharmacological approach for overcoming 4-hydroxytamoxifen resistance in breast cancer therapy
medicine
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salivary neuron specific enolase is an indicator for neuronal damage in patients with ischemic stroke and stroke-prone patients
drug development
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the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
medicine
P04764
the up-regulation of alpha-enolase expression can be a protective mechanism to neutralize oxidative and nitrative stress in diabetes
molecular biology
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influence of enolase on membrane fusion of vacuoles and protein trafficking analyzed
molecular biology
P00925
studies on mitochondrial import machinery of Saccharomyces cerevisiae
drug development
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the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
medicine
Q5DDV5
the recombinant enzyme protein is a useful antigen in vaccination against adult worms
molecular biology
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alpha-enolase doubles as a surface-displayed plasminogen-binder supporting virulence
drug development
Streptococcus pyogenes, Streptomyces mutans, Streptomyces pneumoniae, Trichomonas vaginalis
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the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
drug development
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structure and molecular dynamics applied to design irreversible species-specific inhibitors, parasite-specific lysine residue closely to catalytic site identified
drug development
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the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design