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Information on EC 4.2.1.11 - phosphopyruvate hydratase and Organism(s) Enterococcus hirae and UniProt Accession Q8GR70

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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:
Enterococcus hirae
UNIPROT: Q8GR70
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Word Map
The taxonomic range for the selected organisms is: Enterococcus hirae
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, eno-1, 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
-
-
-
-
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 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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
two magnesium ions per subunit are required for catalytic activity
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
124
pH 7.5, 22ºC
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gram-positive bacteria, ATCC9790
SwissProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ENO_ENTHR
432
0
46411
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
46220
calculated from amino-acid sequence
46620
determined by mass spectrometry
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
using the hanging drop method followed by recrystallization under the same conditions, X-ray structure solved by molecular replacement
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partial, using ammonium sulfate fractionation and gel filtration chromatography
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hosaka, T.; Meguro, T.; Yamato, I.; Shirakihara, Y.
Crystal structure of Enterococcus hirae enolase at 2.8 A resolution
J. Biochem.
133
817-823
2003
Enterococcus hirae (Q8GR70), Enterococcus hirae
Manually annotated by BRENDA team