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Information on EC 3.11.1.3 - phosphonopyruvate hydrolase and Organism(s) Variovorax sp. and UniProt Accession Q84G06

for references in articles please use BRENDA:EC3.11.1.3
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This record set is specific for:
Variovorax sp.
UNIPROT: Q84G06 not found.
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The taxonomic range for the selected organisms is: Variovorax sp.
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
phosphonopyruvate hydrolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PATHWAY SOURCE
PATHWAYS
CAS REGISTRY NUMBER
COMMENTARY hide
266360-38-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-phosphonopyruvate + H2O
pyruvate + phosphate
show the reaction diagram
phosphoenolpyruvate + H2O
pyruvate + phosphate
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
3-phosphonopyruvate + H2O
pyruvate + phosphate
show the reaction diagram
the enzyme is likely to be of considerable significance in global phosphorous cycling, because phosphonopyruvate is known to be a key intermediate in the formation of all naturally occuring compounds that cotain the carbon-phosphorus bond
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
activates, 0.00073 mM
Ni2+
5 mM, 1.54fold activation
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-phosphonopropionic acid
5 mM, 17% loss of activity
Ca2+
competitive
Cu2+
5 mM, 41% loss of activity
hydroxymethylphosphonic acid
5 mM, 25% loss of activity
Mn2+
5 mM, 41% loss of activity
oxalate
competitive
phosphoenolpyruvate
competitive
Phosphonoformic acid
5 mM, 76% loss of activity
sulfopyruvate
competitive
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
phosphonopyruvate and phosphonoalanine induce the enzyme in strain Pal2
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.005 - 0.53
3-phosphonopyruvate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
105 - 121
3-phosphonopyruvate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.032
Ca2+
25°C, pH 7.5
2
oxalate
25°C, pH 7.5
0.21
phosphoenolpyruvate
25°C, pH 7.5
0.017
sulfopyruvate
25°C, pH 7.5
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.35
isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
the enzyme is expressed even in the presence of high levels of phosphate, thus permitting phosphonopyruvate to be used as the sole carbon and energy source
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
110000
gel filtrration
31000
4 * 31000, SDS-PAGE
31187
2 * 31187, mass spectrometry
63000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 31187, mass spectrometry
tetramer
4 * 31000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method, enzyme in unbound state and in complex with Mg2+ and the inhibitor oxalate
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R188A
1.15fold increase in turnover number
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
10 min, loss of activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 25% glycerol, 6 months, about 20% loss of activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene palA, DNA and amino acid sequence determination and analysis, the palA gene is organized with four other structural genes, genes palA, palB, palC, palD and palE, in the 2-amino-3-phosphonopropionic acid (phosphonoalanine)-degradative operon, overview. Expression of GFP-tagged PalA, with or without coexpression of the other genes of the operon, in Pseudomonas putida strain KT2440
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chen, C.C.; Han, Y.; Niu, W.; Kulakova, A.N.; Howard, A.; Quinn, J.P.; Dunaway-Mariano, D.; Herzberg, O.
Structure and kinetics of phosphonopyruvate hydrolase from Variovorax sp. Pal2: new insight into the divergence of catalysis within the PEP mutase/isocitrate lyase superfamily
Biochemistry
45
11491-11504
2006
Variovorax sp. (Q84G06), Variovorax sp. Pal2 (Q84G06)
Manually annotated by BRENDA team
Kulakova, A.N.; Wisdom, G.B.; Kulakov, L.A.; Quinn, J.P.
The purification and characterization of phosphonopyruvate hydrolase, a novel carbon-phosphorus bond cleavage enzyme from Variovorax sp Pal2
J. Biol. Chem.
278
23426-23431
2003
Variovorax sp. (Q84G06), Variovorax sp. Pal2 (Q84G06)
Manually annotated by BRENDA team
Kulakova, A.N.; Kulakov, L.A.; Villarreal-Chiu, J.F.; Gilbert, J.A.; McGrath, J.W.; Quinn, J.P.
Expression of the phosphonoalanine-degradative gene cluster from Variovorax sp. Pal2 is induced by growth on phosphonoalanine and phosphonopyruvate
FEMS Microbiol. Lett.
292
100-106
2009
Variovorax sp., Variovorax sp. Pal2
Manually annotated by BRENDA team