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Information on EC 4.2.1.11 - phosphopyruvate hydratase and Organism(s) Oryctolagus cuniculus and UniProt Accession P25704

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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.1 Hydro-lyases
                4.2.1.11 phosphopyruvate hydratase
IUBMB Comments
Also acts on 3-phospho-D-erythronate.
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This record set is specific for:
Oryctolagus cuniculus
UNIPROT: P25704
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The taxonomic range for the selected organisms is: Oryctolagus cuniculus
The enzyme appears in selected viruses and cellular organisms
Synonyms
neuron-specific enolase, enolase, neuron specific enolase, alpha-enolase, gamma-enolase, enolase 1, beta-enolase, yeast enolase, enolase 2, laminin binding protein, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
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
enolase-beta
-
-
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
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2-phospho-D-glycerate = phosphoenolpyruvate + H2O
show the reaction diagram
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
-
-
-
-
addition
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
2-phospho-D-glycerate hydro-lyase (phosphoenolpyruvate-forming)
Also acts on 3-phospho-D-erythronate.
CAS REGISTRY NUMBER
COMMENTARY hide
9014-08-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
phosphoenolpyruvate
2-phospho-D-glycerate
show the reaction diagram
-
-
-
r
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
-
can partially replace Mg2+ in activation
Zn2+
-
can partially replace Mg2+ in activation
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NaClO4
E414L mutant is more sensitive to inactivation than the wild-type enzyme
NaClO4
-
inactivation is due to dissociation of the enolase into inactive monomers, 2-phospho-D-glycerate prevents this inactivation
phosphate
-
competitive inhibition at 2-4 mM phosphate with respect to 2-phosphoglycerate becomes noncompetitive in presence of 20-40 mM phosphate
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetylcholinesterase C-terminal peptide 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%
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
43
phosphoenolpyruvate
E414L mutant enzyme, pH 7.1, 25ºC
0.061
2-phospho-D-glycerate
-
-
0.25
phosphoenolpyruvate
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
67
recombinant wild-type enzyme, pH 7.1, 25ºC
77
recombinant E414L mutant, pH 7.1, 25ºC
additional information
-
31.2 nmol 2-PGA converted/min/36nM enolase
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.9
-
formation of phosphoenolpyruvate
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
rabbit
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
back and hind legs
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ENOB_RABIT
434
0
47069
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
46940
mass spectrometry
47000
-
2 * 47000, SDS-PAGE
48000
-
2 * 48000, SDS-PAGE
85500
-
gel filtration
92000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E414L
this mutant has the same activity than the wild-type enzyme
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
both the wild-type and the E414L mutant are stable as suspensions in ammonium sulfate
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purification of the wild-type and a mutant enzyme cloned in Escherichia coli using ammonium sulfate precipitation and Sephadex chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of recombinant wild-type and mutant enzymes in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Scopes, R.K.; Stoter, A.
Purification of all glycolytic enzymes from one muscle extract
Methods Enzymol.
90
479-490
1982
Oryctolagus cuniculus
Manually annotated by BRENDA team
Aoki, T.; Tanaka, T.; Watabe, H.
Purification and characterization of gamma-enolase from various mammals
Chem. Pharm. Bull.
40
1236-1239
1992
Bos taurus, Canis lupus familiaris, Capra hircus, Oryctolagus cuniculus, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Nakagawa, T.; Nagayama, F.
Enzymatic properties of enolase from fish muscle
Comp. Biochem. Physiol. B
98
355-359
1991
Cyprinus carpio, Oryctolagus cuniculus, Pagrus major, Scomber japonicus
-
Manually annotated by BRENDA team
Provost, J.J.; Ray, P.D.; Lambeth, D.O.
Concomitant purification and characterization of malate dehydrogenase, aspartate transaminase, nucleoside diphosphate kinase and enolase from rabbit liver cytosol
Prep. Biochem. Biotechnol.
26
121-133
1996
Oryctolagus cuniculus
Manually annotated by BRENDA team
Kornblatt, M.J.
Mechanism of rabbit muscle enolase: identification of the rate-limiting steps and the site of Li+ inhibition
Arch. Biochem. Biophys.
330
12-18
1996
Oryctolagus cuniculus
Manually annotated by BRENDA team
Lin, T.; Kornblatt, M.J.
The binding of Na(+) to apo-enolase permits the binding of substrate
Biochim. Biophys. Acta
1476
279-286
2000
Oryctolagus cuniculus
Manually annotated by BRENDA team
Kornblatt, M.J.; Zheng, S.X.; Lamande, N.; Lazar, M.
Cloning, expression and mutagenesis of a subunit contact of rabbit muscle-specific (betabeta) enolase
Biochim. Biophys. Acta
1597
311-319
2002
Oryctolagus cuniculus (P25704), Oryctolagus cuniculus
Manually annotated by BRENDA team
Mor, I.; Bruck, T.; Greenberg, D.; Berson, A.; Schreiber, L.; Grisaru, D.; Soreq, H.
Alternate AChE-R variants facilitate cellular metabolic activity and resistance to genotoxic stress through enolase and RACK1 interactions
Chem. Biol. Interact.
175
11-21
2008
Oryctolagus cuniculus
Manually annotated by BRENDA team