Information on EC 3.11.1.1 - phosphonoacetaldehyde hydrolase

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

EC NUMBER
COMMENTARY hide
3.11.1.1
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RECOMMENDED NAME
GeneOntology No.
phosphonoacetaldehyde hydrolase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
phosphonoacetaldehyde + H2O = acetaldehyde + phosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of carbon-phosphorus bond
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
2-aminoethylphosphonate degradation I
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Metabolic pathways
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Microbial metabolism in diverse environments
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Phosphonate and phosphinate metabolism
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SYSTEMATIC NAME
IUBMB Comments
2-oxoethylphosphonate phosphonohydrolase
This enzyme destabilizes the C-P bond, by forming an imine between one of its lysine residues and the carbonyl group of the substrate, thus allowing this, normally stable, bond to be broken. The mechanism is similar to that used by EC 4.1.2.13, fructose-bisphosphate aldolase, to break a C-C bond. Belongs to the haloacetate dehalogenase family.
CAS REGISTRY NUMBER
COMMENTARY hide
37289-42-2
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
AI-2
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Manually annotated by BRENDA team
strain IFO 12010. 2-aminoethylphosphonic acid:pyruvate aminotransferase and phosphonoacetaldehyde hydrolase activities are induced when cells are both phosphate limited and supplied with 2-aminoethylphosphonic acid as sole source of phosphorus in the culture medium. Neither enzyme is induced in phosphate-replete medium, or in medium where both 2-aminoethylphosphoonic acid and phosphate are supplied
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Manually annotated by BRENDA team
i.e. Geomyces pannorum strain P11, a psychrophilic fungal strain
UniProt
Manually annotated by BRENDA team
i.e. Geomyces pannorum strain P11, a psychrophilic fungal strain
UniProt
Manually annotated by BRENDA team
DSM 15170
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetonyl phosphonate + H2O
?
show the reaction diagram
p-nitrophenylphosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
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hydrolyzed at considerable lower rate than phosphonoacetaldehyde
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?
phosphonoacetaldehyde + H2O
acetaldehyde + phosphate
show the reaction diagram
phosphonoacetylaldehyde + H2O
acetaldehyde + phosphate
show the reaction diagram
thiophosphonoacetaldehyde + H2O
thiophosphate + acetaldehyde
show the reaction diagram
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
phosphonoacetaldehyde + H2O
acetaldehyde + phosphate
show the reaction diagram
phosphonoacetylaldehyde + H2O
acetaldehyde + phosphate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
copper
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contains 0.3 gatom per molecular weight of 75000 Da
Iron
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contains trace amounts of iron
Zinc
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contains 0.4 gatom per molecular weight of 75000 Da
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,4-Dinitrophenylacetate
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loss of activity due to acetylation of Ls53 with the inert compound, pH profile of inactivation
acetonylphosphonate
fluorophosphate
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competitive inhibitor
Malonic semialdehyde
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competitive inhibitor
n-butylphosphonic acid
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activates at low concentrations, inhibits at high concentrations. Allosteric model involving two different classes of sites for n-butylphosphonic acid
phosphite
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phosphonoacetaldehyde
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competitive inhibitor
phosphonoethanol
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competitive inhibitor
Trypsin
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degradation
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vinyl sulfonate
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competitive, inhibition mechanism
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-Aminoethylphosphonic acid
n-butylphosphonic acid
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activates at low concentrations, inhibits at high concentrations. Allosteric model involving two different classes of sites for n-butylphosphonic acid
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.033 - 11
phosphonoacetaldehyde
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
16.7
2-phosphonoacetaldehyde
Bacillus cereus
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0.000084 - 15
phosphonoacetaldehyde
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.79
vinyl sulfonate
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pH 7.5, 25C
additional information
additional information
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inhibition kinetics
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 10
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pH 6.5: about 35% of maximal activity, pH 10.0: about 30% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 55
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30C: about 50% of maximal activity, 55C: about 45% of maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
68000
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nondenaturing PAGE
83000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 33000-37000, similar subunits, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
10 mg/ml purified recombinant wild-type and mutant enzymes, complexed with Mg2+ only or with Mg2+ and inhibitor vinyl sulfonate, in 1 mM HEPES, 10 mM MgCl2, 0.1 mM DTT, pH 7.5, 4C, hanging drop vapour diffusion method, equal volume of protein and reservoir solution, the latter containing 30% PEG 4000, 100 mM Tris-HCl, pH 7.4, 100 mM MgCl2, 1 week, against the reservoir well solution additionally with 20% glycerol before data collection, X-ray diffraction structure determination and analysis at 2.4-2.8 A resolution
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10 mg/ml wild-type and mutant D12A enzymes complexed with Mg2+ only or with Mg2+ and substrate, in 1 mM HEPES, 10 mM MgCl2, 0.1 mM DTT, pH 7.5, 4C, hanging drop vapour diffusion method, equal volume of protein and reservoir solution, the latter containing 30% PEG 4000, 100 mM Tris-HCl, pH 7.4, 100 mM MgCl2, 1 week, against the reservoir well solution additionally with 20% glycerol before data collection, X-ray diffraction structure determination and analysis at 2.3-2.55 A
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crystal structure of the homodimeric enzyme complexed with the phosphate analogue tungstate and Mg2+
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mutant enzymes
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
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protonation of the active site Lys is the cause for loss of activity
246535
8
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deprotonation of the active site Cys may be the cause for the loss of enzyme activity
246535
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
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rapid loss loss of activity in absence of Mg2+
45
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heat-labile, even in presence of 5 mM Mg2+
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
inactivation in absence of Mg2+ is aggravated at higher pH or when either EDTA or Ca2+ is added
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repeated freezing and thawing causes rapid loss of activity
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, stable for several months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant enzymes from Escherichia coli
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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expression of wild-type and mutant enzymes in Escherichia coli
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expression of wild-type and mutant enzymes in Escherichia coli JM109
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gene phnX, the gene is encoded within a degradative operon for the mineralization of 2-aminoethylphosphonic acid (2-AEP, ciliatine)
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C22A
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site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
C22S
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site-directed mutagenesis, reduced activity compared to the wild-type enzyme
D12A
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site-directed mutagenesis, catalytically inactive mutant
D186A
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site-directed mutagenesis, highly reduced activity
D186A/D190A
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site-directed mutagenesis, inactive mutant
D186E
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site-directed mutagenesis, very highly reduced activity
D190A
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site-directed mutagenesis, reduced activity
G185D/D190G
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site-directed mutagenesis, reduced activity
G50A
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kcat/Km is 12820fold lower than wild-type value
G50P
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inactive mutant protein
G50V
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inactive mutant protein
H56A
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site-directed mutagenesis, very highly reduced activity compared to the wild-type enzyme
H56Q
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kcat/Km is 238fold lower than wild-type value
K121R/K146R/K192R
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site-directed mutagenesis, reduced activity compared to the wild-type enzyme
K183A
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site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme, Lys183 is probably important in maintaining the active site environment
K183L
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site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme, Lys183 is probably important in maintaining the active site environment
K53A
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inactive mutant protein
K53R
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inactive mutant protein
Y128A
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site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
Y128F
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site-directed mutagenesis, reduced activity compared to the wild-type enzyme
Y128F/C22S
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site-directed mutagenesis, reduced activity compared to the wild-type enzyme
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression of mutant enzymes in escherichia coli
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