Information on EC 3.11.1.2 - phosphonoacetate hydrolase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
3.11.1.2
-
RECOMMENDED NAME
GeneOntology No.
phosphonoacetate hydrolase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Phosphonoacetate + H2O = acetate + phosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C-P bond cleavage
hydrolysis of carbon-phosphorus bond
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Microbial metabolism in diverse environments
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-
Phosphonate and phosphinate metabolism
-
-
phosphonoacetate degradation
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SYSTEMATIC NAME
IUBMB Comments
phosphonoacetate phosphonohydrolase
A zinc-dependent enzyme. Belongs to the alkaline phosphatase superfamily of zinc-dependent hydrolases.
CAS REGISTRY NUMBER
COMMENTARY hide
153570-68-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain Vs2, induction of enzyme by grwoth on phosphonoacetate or 2-aminoethyl phosphonate as the sole phosphorus source and a pyruvate carbon source. Model of carbon catabolite repression
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-
Manually annotated by BRENDA team
strain Vs2, induction of enzyme by grwoth on phosphonoacetate or 2-aminoethyl phosphonate as the sole phosphorus source and a pyruvate carbon source. Model of carbon catabolite repression
-
-
Manually annotated by BRENDA team
strain AMMD, gene phnA
UniProt
Manually annotated by BRENDA team
strain AMMD, gene phnA
UniProt
Manually annotated by BRENDA team
strain Ellin6076, gene phnA
UniProt
Manually annotated by BRENDA team
strain Ellin6076, gene phnA
UniProt
Manually annotated by BRENDA team
strain H16, gene phnA
UniProt
Manually annotated by BRENDA team
strain H16, gene phnA
UniProt
Manually annotated by BRENDA team
strain PA1, substrate-inducible enzyme, expression is independent of the phosphate status of the cell
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-
Manually annotated by BRENDA team
strain PA1, substrate-inducible enzyme, expression is independent of the phosphate status of the cell
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-
Manually annotated by BRENDA team
a coccolithophore from coastal mesocosm in a fjord close to Bergen, Norway, gene phnA
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-
Manually annotated by BRENDA team
a dinoflagellate from coastal mesocosm in a fjord close to Bergen, Norway, gene phnA
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-
Manually annotated by BRENDA team
no activity in Vibrio shiloi
strains LMG197032 and LMG197033
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-
Manually annotated by BRENDA team
strain LB400, gene phnA
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-
Manually annotated by BRENDA team
strain CC006, gene phnA
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-
Manually annotated by BRENDA team
strain CC006, gene phnA
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-
Manually annotated by BRENDA team
strain PA2, substrate-inducible enzyme, expression is independent of the phosphate status of the cell
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-
Manually annotated by BRENDA team
strain PA2, substrate-inducible enzyme, expression is independent of the phosphate status of the cell
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-
Manually annotated by BRENDA team
strain CGA009, gene phnA
UniProt
Manually annotated by BRENDA team
strain CGA009, gene phnA
UniProt
Manually annotated by BRENDA team
DSM 15170
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-
Manually annotated by BRENDA team
strain WSM419, gene phnA on a megaplasmid
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-
Manually annotated by BRENDA team
strain WSM419, gene phnA on a megaplasmid
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-
Manually annotated by BRENDA team
gene phnA
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-
Manually annotated by BRENDA team
strain EF01-2, gene phnA
UniProt
Manually annotated by BRENDA team
strain EF01-2, gene phnA
UniProt
Manually annotated by BRENDA team
strain CC028, gene phnA
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-
Manually annotated by BRENDA team
strain CC028, gene phnA
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-
Manually annotated by BRENDA team
strains CC040 and CC004, gene phnA
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
additional information
C-P bond hydrolysis by phosphonoacetate hydrolase, structure and mechanism, overview. Structure analysis of bound substrate, product, inhibitor, and a covalently bound transition state mimic provide insight into active site features that may facilitate cleavage of the C-P bond
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
phosphonoacetate + H2O
?
show the reaction diagram
-
inducible only in the presence of its sole substrate, does not require phosphate starvation
-
-
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Phosphonoacetate + H2O
acetate + phosphate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
phosphonoacetate + H2O
?
show the reaction diagram
-
inducible only in the presence of its sole substrate, does not require phosphate starvation
-
-
-
Phosphonoacetate + H2O
acetate + phosphate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
slightly activates 1.1fold at 1 mM
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
2-mercaptoethanol
2-phosphonopropionic acid
3-phosphonopropionate
-
-
3-phosphonopropionic acid
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about 30% inhibition at 10 mM
Arsonoacetate
-
weak
dithiothreitol
iminodiacetate
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-
iminodiacetic acid
malonate
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weak
Mg2+
-
slight inhibition of 17% at 1 mM
Phosphonoacetate
-
substrate inhibition at 25 mM and above
Phosphonoformate
Phosphonoformic acid
phosphonoproprionate
-
competitive inhibitor
Phosphonopyruvate
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competitive inhibitor
Sulfonoacetate
-
weak
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Phosphonoacetate
-
substrate activation, mechanism, overview
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0078 - 1.9
Phosphonoacetate
additional information
additional information
-
steady-state kinetics analysis
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.9 - 3
Phosphonoacetate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4100
Phosphonoacetate
Sinorhizobium meliloti
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pH 7.5, 30°C, recombinant enzyme
2756
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.049 - 0.19
Phosphonoformate
1.2
phosphonoproprionate
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pH 7.0, 30°C
1.2
Phosphonopyruvate
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pH 7.0, 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
665
-
pH 8.0, 35°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 8
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assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9.6
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pH 7.0: about 65% of maximal activity, pH 9.6: about 75% of maximal activity
7.5 - 8.6
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more than 90% of maximum activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 30
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assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 45
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20°C: about 40% of maximal activity, 45°C: about 50% of maximal activity
40 - 75
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.1
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isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
the organism is capable of utilizing phosphonoacetate as sole C and P source
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38000
-
2 * 38000, SDS-PAGE
42600
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gel filtration
43200
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1 * 43200, SDS-PAGE
44237
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2 * 44237, calculation from nucleotide sequence
44239
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2 * 44239, sequence calculation and gel filtration
48400
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x * 48400, recombinant His6-tagged PhnA, SDS-PAGE
80000
-
gel filtration
93000
-
gel filtration, recombinant enzyme
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 48400, recombinant His6-tagged PhnA, SDS-PAGE
homodimer
monomer
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1 * 43200, SDS-PAGE
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme in in the presence of Zn2+, Mg2+, phosphonoformate and tartrate, from 30 mM K+BICINE, pH 8.5, and 1 mM ZnCl2, mixed with 10% poly(ethylene glycol) 8000, 100 mM Mg-acetate, and 5 mM phosphonoformate buffered at pH 7.0 with 100 mM MOPSO, X-ray diffraction structure determination and analysis at 2.8 A resolution, multiple isomorphous replacement with two heavy-atom derivatives
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selenomethionine-labeled enzyme, on-chip technology using a 24-well hybrid array chip, X-ray diffraction structure determination and analysis at 2.11 A resolution, crystallization screening and optimization, and usage of a microfluidic approach for the crystallization and de novo X-ray structure determination of novel targets via on-chip anomalous X-ray diffraction analysis, method validation
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X-ray diffraction structure determination and analysis at 1.35 A resolution, cocrystal structures with phosphonoacetate substrate, acetate, phosphonoformate inhibitor, and a covalently bound transition state mimic
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.2
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above pH 6.2 stable for at least 10 min
684053
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
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30 min, rapid loss of activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 35% loss of activity after 31 days, 45% loss of activity after 34 days
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli strain JM105 by ammonium sulfate fractionation, and anion exchange, hydrophobic interaction, and hydroxylapatite chromatography, followed by gel filtration
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recombinant N-terminally His6-tagged PhnA from Escherichia coli by nickel affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli and Pseudomonas putida
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gene phnA, DNA and amino acid sequence determination and analysis, phylogenetic analysis of marine phytoplankton organisms, sequence comparisons and taxonomic identifications, detailed overview
gene phnA, DNA and amino acid sequence determination and analysis, phylogenetic analysis of marine phytoplankton organisms, sequence comparisons and taxonomic identifications, detailed overview; gene phnA, DNA and amino acid sequence determination and analysis, phylogenetic analysis of marine phytoplankton organisms, sequence comparisons and taxonomic identifications, detailed overview
gene phnA, expression of N-terminally His6-tagged PhnA in Escherichia coli
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gene phnA, the gene is encoded within an operon whose expression is regulated by a phosphonoacetate-responsive LTTR
recombinant expression in Escherichia coli strain JM105
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
construction of a phnA deletion mutant
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
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