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Information on EC 4.2.1.11 - phosphopyruvate hydratase and Organism(s) Geobacillus kaustophilus and UniProt Accession Q5KVE7

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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:
Geobacillus kaustophilus
UNIPROT: Q5KVE7
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The taxonomic range for the selected organisms is: Geobacillus kaustophilus
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
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-
-
-
2-phosphoglycerate enolase
-
-
-
-
2-phosphoglyceric dehydratase
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-
-
-
alpha,alpha-enolase
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-
-
-
Alt a XI
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-
-
-
beta,beta-enolase
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-
-
-
Cla h VI
-
-
-
-
enolase
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-
-
-
gamma,gamma-enolase
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-
-
-
gamma-enolase
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-
-
-
HLE1
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-
-
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hydratase, phosphoenolpyruvate
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-
-
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Laminin binding protein
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-
-
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Major allergen Alt a 11
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-
-
-
MSE
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-
-
-
Neural enolase
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-
-
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neuron-specific enolase
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-
-
-
NNE
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-
-
-
Non-neural enolase
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-
-
-
NSE
-
-
-
-
OSE1
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-
-
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phosphoenolpyruvate hydratase
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-
-
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Phosphopyruvate hydratase
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-
-
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R-NSE
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-
-
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Skeletal muscle enolase
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-
-
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Tau-crystallin
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
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-
-
-
addition
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-
-
-
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
2,3-diketo-5-methylthiopentane 1-phosphate
2-hydroxy-3-keto-5-methylthiopent-1-ene 1-phosphate
show the reaction diagram
2,3-diketohexane 1-phosphate
?
show the reaction diagram
alternate substrate, C1 proton abstraction
-
-
?
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
2,3-diketo-5-methylthiopentane 1-phosphate
2-hydroxy-3-keto-5-methylthiopent-1-ene 1-phosphate
show the reaction diagram
methionine salvage pathway
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
activity depends on
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
HCO3-
Km about 50% increased in presence of sodium bicarbonate, crystallized enzyme structure complexed with HCO3- in its activated form
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
composed of a N-terminal alpha,beta domain and a C-terminal domain consisting of eight alpha,alpha barrels, polypeptides packed as tight dimers
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K147A
requires a 10fold greater concentration of protein for observation of enolization
K173A
detectable activity of about 3% of that of wild-type enolase, retains ability to enolize the desthio substrate
K98A
unable to catalyze the enolase reaction
additional information
site-directed mutagenesis of active site residues, spectrophotometric activity assay performed with elevated concentrations of the mutant enzymes
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant protein, gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21, pET17b expression vector
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Imker, H.J.; Fedorov, A.A.; Fedorov, E.V.; Almo, S.C.; Gerlt, J.A.
Mechanistic diversity in the RuBisCO superfamily: the enolase in the methionine salvage pathway in Geobacillus kaustophilus
Biochemistry
46
4077-4089
2007
Bacillus subtilis (P37869), Geobacillus kaustophilus (Q5KVE7), Bacillus subtilis 168 (P37869)
Manually annotated by BRENDA team