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Information on EC 4.2.1.11 - phosphopyruvate hydratase and Organism(s) Brucella abortus and UniProt Accession Q2YPV0

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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:
Brucella abortus
UNIPROT: Q2YPV0
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The taxonomic range for the selected organisms is: Brucella abortus
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 + H2O
show the reaction diagram
-
-
-
?
NATURAL SUBSTRATE
NATURAL 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 + H2O
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Al3+
can partially substitute for Mg2+ or Zn2+ at 10 mM showing 68.8% of the maximal activity with 10 mM Mg2+
Mg2+
activates, optimally at 10 mM
Mn2+
can partially substitute for Mg2+ or Zn2+ at 10 mM showing 90.4% of the maximal activity with 10 mM Mg2+
Ni2+
can partially substitute for Mg2+ or Zn2+ at 10 mM showing 90.5% of the maximal activity with 10 mM Mg2+
Zn2+
activates, optimally at 10 mM, best activating metal ion
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cr2+
leads to complete inhibition at 10 mM
Cu2+
leads to complete inhibition at 10 mM
Hg2+
leads to complete inhibition at 10 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2
2-phospho-D-glycerate
pH 8.5, 25°C, recombinant enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10050
purifed recombinant enzyme, pH 8.5, 37°C, 10 mM Zn2+
3909
purifed recombinant enzyme, pH 8.5, 37°C, no metal ion added
9091
purifed recombinant enzyme, pH 8.5, 37°C, 10 mM Mg2+
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5
recombinant enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 10
activity range, recombinant enzyme
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
recombinant enzyme
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain 2308, 100% sequence identity with strain A19
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
49000
x * 49000, recombinant His-tagged enolase, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 49000, recombinant His-tagged enolase, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 62
maximally stable at 37°C, the purified recombinant enolase is thermally stable at 25°C, 37°C, 50°C, and 62°C, but is completely inhibited by a preincubation of the enzyme at 75°C after 1 h
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enolase from Escherichia coli strain BL21 by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of His-tagged enolase in Escherichia coli strain BL21
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Han, X.; Ding, C.; Chen, H.; Hu, Q.; Yu, S.
Enzymatic and biological characteristics of enolase in Brucella abortus A19
Mol. Biol. Rep.
39
2705-2711
2012
Brucella abortus (Q2YPV0), Brucella abortus, Brucella abortus A19 (Q2YPV0)
Manually annotated by BRENDA team