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Information on EC 3.11.1.1 - phosphonoacetaldehyde hydrolase
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3.11.1.1 phosphonoacetaldehyde hydrolaseIUBMB Comments
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.
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Word Map
- 3.11.1.1
- phosphorus
- phosphonates
-
carbon-phosphorus
-
dehalogenase
- phosphonoacetate
- 2-aminoethylphosphonate
-
schiff-base
-
phosphomutase
- phosphonopyruvate
-
organophosphonate
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
2-phosphonoacetaldehyde phosphonohydrolase, 2-phosphonoacetylaldehyde phosphonohydrolase, hydrolase, phosphonoacetylaldehyde, P-Ald hydrolase, phosphonatase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-phosphonoacetylaldehyde phosphonohydrolase
-
-
-
-
hydrolase, phosphonoacetylaldehyde
-
-
-
-
P-Ald hydrolase
-
-
-
-
phosphonatase
phosphonatase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
phosphonoacetaldehyde + H2O = acetaldehyde + phosphate
mechanism involves Schiff base formation with Lys53 followed by phosphoryl transfer to Asp11 and at last hydrolysis at the imine and acyl phosphate phosphorus
-
phosphonoacetaldehyde + H2O = acetaldehyde + phosphate
mechanism involves Schiff base formation with Lys53 followed by phosphoryl transfer to Asp12 and at last hydrolysis at the imine and acyl phosphate phosphorus
-
phosphonoacetaldehyde + H2O = acetaldehyde + phosphate
bicovalent catalytic mechanism in which an active site nucleophile abstracts the phosphoryl group from the Schiff-base intermediate formed from Lys53 and phosphonoacetaldehyde
-
phosphonoacetaldehyde + H2O = acetaldehyde + phosphate
Schiff base formation with catalytic Lys and phosphonoacetaldehyde, PC-bond cleavage in the Schiff base takes place during the second partial reaction and liberation of the acetaldehyde from the resulting enamine occurs during the third partial reaction
-
phosphonoacetaldehyde + H2O = acetaldehyde + phosphate
double displacement mechanism proceeding via protonated Schiff base and phosphoenzyme intermediates. The mechanism involves P-C bond cleavage in a protonated Schiff base intermediate by in-line displacement by an enzyme nucleophile. Subsequent hydrolysis of the resultant acetaldehyde enamine and phosphoenzyme groups then yield acetaldehyde and phosphate
-
phosphonoacetaldehyde + H2O = acetaldehyde + phosphate
Schiff base mechanism
-
phosphonoacetaldehyde + H2O = acetaldehyde + phosphate
imine formation between the enzyme and its substrate
-
phosphonoacetaldehyde + H2O = acetaldehyde + phosphate
active site structure
phosphonoacetaldehyde + H2O = acetaldehyde + phosphate
mechanism, active site conformation during catalysis, Lys53 is involved
phosphonoacetaldehyde + H2O = acetaldehyde + phosphate
mechanism, reaction pathway, Schiff base formation between an amine and a ketone in aqueous solution, active site model
phosphonoacetaldehyde + H2O = acetaldehyde + phosphate
quantum chemical study of the imine formation reaction, which precedes P-C bond cleavage. The barrier of this reaction can be significantly lowered if the reaction is assisted by a water molecule and the substrate is protonated
-
phosphonoacetaldehyde + H2O = acetaldehyde + phosphate
alternative catalytic mechanism, involving proton transfer that triggers P-C bond cleavage, transition states, TSd1, TSm1, TSd2, TSm2, and theoretical QM/MM study using crystal structure of an inhibitor-bound enzyme, overview. The bond breaking process is facilitated by proton transfer from catalytic lysine residue to the substrate. The common catalytic mechanism involves formation of a Schiff base, overview
-
phosphonoacetaldehyde + H2O = acetaldehyde + phosphate
Schiff base formation with catalytic Lys and phosphonoacetaldehyde, PC-bond cleavage in the Schiff base takes place during the second partial reaction and liberation of the acetaldehyde from the resulting enamine occurs during the third partial reaction
-
-
phosphonoacetaldehyde + H2O = acetaldehyde + phosphate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of carbon-phosphorus bond
-
-
-
-
P-C bond cleavage
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PATHWAY SOURCE
PATHWAYS
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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.
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CAS REGISTRY NUMBER
COMMENTARY
37289-42-2
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
p-nitrophenylphosphate + H2O
p-nitrophenol + phosphate
-
hydrolyzed at considerable lower rate than phosphonoacetaldehyde
-
-
?
phosphonoacetaldehyde + H2O
acetaldehyde + phosphate
i.e. Pald
-
?
phosphonoacetaldehyde + H2O
acetaldehyde + phosphate
i.e. Pald, cleavage via Schiff base intermediate formed with Lys53, bound substrate stabilizes the closed conformation of the active site, thus facilitating catalysis
-
?
phosphonoacetaldehyde + H2O
acetaldehyde + phosphate
-
catalysis within the core domain of phosphonatase requires the participation of loop 5 of the corresponding cap domain. Gly is an indispensable component
-
-
?
phosphonoacetaldehyde + H2O
acetaldehyde + phosphate
-
-
-
?
phosphonoacetaldehyde + H2O
acetaldehyde + phosphate
-
-
-
?
phosphonoacetaldehyde + H2O
acetaldehyde + phosphate
-
-
-
?
phosphonoacetylaldehyde + H2O
acetaldehyde + phosphate
-
2-phosphonoacetaldehyde
-
?
phosphonoacetylaldehyde + H2O
acetaldehyde + phosphate
-
second step in the pathway by which Bacillus cereus metabolizes 2-aminoethylphosphonic acid
-
?
phosphonoacetylaldehyde + H2O
acetaldehyde + phosphate
-
second step in the pathway by which Bacillus cereus metabolizes 2-aminoethylphosphonic acid
-
?
phosphonoacetylaldehyde + H2O
acetaldehyde + phosphate
-
second step in the pathway by which Bacillus cereus metabolizes 2-aminoethylphosphonic acid
-
?
phosphonoacetylaldehyde + H2O
acetaldehyde + phosphate
-
-
-
?
phosphonoacetylaldehyde + H2O
acetaldehyde + phosphate
-
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
phosphonoacetaldehyde + H2O
acetaldehyde + phosphate
-
-
-
?
phosphonoacetaldehyde + H2O
acetaldehyde + phosphate
-
-
-
?
phosphonoacetaldehyde + H2O
acetaldehyde + phosphate
-
-
-
?
phosphonoacetylaldehyde + H2O
acetaldehyde + phosphate
-
second step in the pathway by which Bacillus cereus metabolizes 2-aminoethylphosphonic acid
-
?
phosphonoacetylaldehyde + H2O
acetaldehyde + phosphate
-
second step in the pathway by which Bacillus cereus metabolizes 2-aminoethylphosphonic acid
-
?
phosphonoacetylaldehyde + H2O
acetaldehyde + phosphate
-
second step in the pathway by which Bacillus cereus metabolizes 2-aminoethylphosphonic acid
-
?
phosphonoacetylaldehyde + H2O
acetaldehyde + phosphate
-
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mg2+
activates, required for catalysis, serves as a cofactor, binds via ligation to the loop 1 Asp12 carboxylate and Thr 14 backbone carbonyl and to the loop 4 Asp186carboxylate, the loop 4 Asp190 forms a hydrogen bond to the Mg(II) water ligand, Asp186 is essential while Asp190 simply enhances cofactor binding
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,4-Dinitrophenylacetate
loss of activity due to acetylation of Ls53 with the inert compound, pH profile of inactivation
n-butylphosphonic acid
-
activates at low concentrations, inhibits at high concentrations. Allosteric model involving two different classes of sites for n-butylphosphonic acid
NaBH4
-
in presence of phosphonoacetaldehyde or acetaldehyde; no effect in absence of substrate or product
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
n-butylphosphonic acid
-
activates at low concentrations, inhibits at high concentrations. Allosteric model involving two different classes of sites for n-butylphosphonic acid
2-Aminoethylphosphonic acid
-
both 2-aminoethylphosphonic acid:pyruvate aminotransferase and phosphonoacetaldehyde hydrolase activities are inducible by the presence of 2-aminoethylphosphonic acid in the culture medium
2-Aminoethylphosphonic acid
-
both 2-aminoethylphosphonic acid:pyruvate aminotransferase and phosphonoacetaldehyde hydrolase activities are inducible by the presence of 2-aminoethylphosphonic acid in the culture medium
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Starvation
In vitro characterization of a phosphate starvation-independent carbon-phosphorus bond cleavage activity in Pseudomonas fluorescens 23F.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.033
phosphonoacetaldehyde
wild-type enzyme, mutant C22S, and mutant Y128F/C22S, pH 7.5, 25°C
0.056
phosphonoacetaldehyde
triple mutant K121R/K146R/K192R, pH 7.5, 25°C
additional information
additional information
kinetics, activity of mutant D186A is too low to measure Km accurately
-
additional information
additional information
-
kinetics, activity of mutant D186A is too low to measure Km accurately
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.28
phosphonoacetaldehyde
triple mutant K121R/K146R/K192R, pH 7.5, 25°C
6.08
phosphonoacetaldehyde
triple mutant K121R/K146R/K192R, pH 7.5, 25°C
15
phosphonoacetaldehyde
wild-type enzyme and mutant M49L, pH 7.5, 25°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 10
-
pH 6.5: about 35% of maximal activity, pH 10.0: about 30% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 55
-
30°C: about 50% of maximal activity, 55°C: about 45% of maximal activity
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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
-
-
brenda
i.e. Geomyces pannorum strain P11, a psychrophilic fungal strain
UniProt
brenda
i.e. Geomyces pannorum strain P11, a psychrophilic fungal strain
UniProt
brenda
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
-
-
brenda
strain NG2 can utilize 2-aminoethylphosphonic acid as sole carbon and energy, nitrogen and phosphorus source. Both 2-aminoethylphosphonic acid:pyruvate aminotransferase and phosphonoacetaldehyde hydrolase activities are inducible by the presence of 2-aminoethylphosphonic acid in the culture medium
-
-
brenda
strain NG2 can utilize 2-aminoethylphosphonic acid as sole carbon and energy, nitrogen and phosphorus source. Both 2-aminoethylphosphonic acid:pyruvate aminotransferase and phosphonoacetaldehyde hydrolase activities are inducible by the presence of 2-aminoethylphosphonic acid in the culture medium
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
-
the organism is not capable of utilizing 2-aminoethyl phosphonate as sole carbon and energy source
brenda
additional information
the organism is able to mineralize 2-aminoethyl phosphonate as sole C, N, and P source
brenda
additional information
the organism is able to mineralize 2-aminoethyl phosphonate as sole C, N, and P source
brenda
additional information
-
the organism is able to mineralize 2-aminoethyl phosphonate as sole C, N, and P source
-
brenda
additional information
the organism is not capable of utilizing 2-aminoethyl phosphonate as sole carbon and energy source
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
additional information
evolution
-
the enzyme is a member of the halo acid dehalogenase superfamily. Distribution of phnX homologs within sequenced bacterial genomes, overview
evolution
the enzyme is a member of the halo acid dehalogenase superfamily. Distribution of phnX homologs within sequenced bacterial genomes, overview
evolution
the enzyme is a member of the halo acid dehalogenase superfamily. Distribution of phnX homologs within sequenced bacterial genomes, overview
evolution
the enzyme is a member of the halo acid dehalogenase superfamily. Distribution of phnX homologs within sequenced bacterial genomes, overview
evolution
-
the enzyme is a member of the halo acid dehalogenase superfamily. Distribution of phnX homologs within sequenced bacterial genomes, overview
-
metabolism
-
the enzyme is involved in the phosphonatase pathway of 2-aminoethylphosphonic acid degradation, overview
metabolism
the enzyme is involved in biodegradation pathway of ciliatine or 2-aminoethylphosphonic acid, a two-step process. The first reaction reported as transamination is carried out by 2-aminoethylphosphonic acid transaminase and leads to the formation of phosphonoacetaldehyde and corresponding amino acid. The next step includes hydrolytic cleavage of the C-P bond within the phosphonoacetaldehyde molecule and results in formation of inorganic phosphate and acetaldehyde, carried out by the phosphonoacetaldehyde hydrolase. The phophonoacetaldehyde hydrolase hydrolyzes
metabolism
the enzyme is involved in the phosphonatase pathway of 2-aminoethyl phosphonate degradation also including a 2-AEP:pyruvate aminotransferase (EC 2.6.1.37), encoded by gene phnW, whose products are phosphonoacetaldehyde and alanine. Expression of the operon is substrate-inducible, mediated by the product of an adjacent gene that encodes a LysR-like transcriptional activator, LTTR
metabolism
the enzyme is involved in the phosphonatase pathway of 2-aminoethyl phosphonate degradation also including a 2-AEP:pyruvate aminotransferase (EC 2.6.1.37), encoded by gene phnW, whose products are phosphonoacetaldehyde and alanine. Expression of the operon is substrate-inducible, mediated by the product of an adjacent gene that encodes a LysR-like transcriptional activator, LTTR
metabolism
-
the enzyme is involved in the phosphonatase pathway of 2-aminoethyl phosphonate degradation also including a 2-AEP:pyruvate aminotransferase (EC 2.6.1.37), encoded by gene phnW, whose products are phosphonoacetaldehyde and alanine. Phosphate-starvation-inducible expression of this pathway as a part of the Pho regulon
metabolism
the enzyme is involved in the phosphonatase pathway of 2-aminoethyl phosphonate degradation also including a 2-AEP:pyruvate aminotransferase (EC 2.6.1.37), encoded by gene phnW, whose products are phosphonoacetaldehyde and alanine. Phosphate-starvation-inducible expression of this pathway as a part of the Pho regulon
metabolism
-
the enzyme is involved in biodegradation pathway of ciliatine or 2-aminoethylphosphonic acid, a two-step process. The first reaction reported as transamination is carried out by 2-aminoethylphosphonic acid transaminase and leads to the formation of phosphonoacetaldehyde and corresponding amino acid. The next step includes hydrolytic cleavage of the C-P bond within the phosphonoacetaldehyde molecule and results in formation of inorganic phosphate and acetaldehyde, carried out by the phosphonoacetaldehyde hydrolase. The phophonoacetaldehyde hydrolase hydrolyzes
-
metabolism
-
the enzyme is involved in the phosphonatase pathway of 2-aminoethyl phosphonate degradation also including a 2-AEP:pyruvate aminotransferase (EC 2.6.1.37), encoded by gene phnW, whose products are phosphonoacetaldehyde and alanine. Expression of the operon is substrate-inducible, mediated by the product of an adjacent gene that encodes a LysR-like transcriptional activator, LTTR
-
physiological function
the enzyme is involved in biodegradation pathway of ciliatine or 2-aminoethylphosphonic acid
physiological function
-
the enzyme is involved in biodegradation pathway of ciliatine or 2-aminoethylphosphonic acid
-
additional information
-
the mechanism of C-P bond cleavage by phosphonatase involves the formation of a Schiff base intermediate between a lysine residue at the active site of the enzyme and the phosphonoacetaldehyde carbonyl group, this activates the phosphonate group for attack by an active site nucleophile
additional information
the mechanism of C-P bond cleavage by phosphonatase involves the formation of a Schiff base intermediate between a lysine residue at the active site of the enzyme and the phosphonoacetaldehyde carbonyl group, this activates the phosphonate group for attack by an active site nucleophile
additional information
the mechanism of C-P bond cleavage by phosphonatase involves the formation of a Schiff base intermediate between a lysine residue at the active site of the enzyme and the phosphonoacetaldehyde carbonyl group, this activates the phosphonate group for attack by an active site nucleophile
additional information
the mechanism of C-P bond cleavage by phosphonatase involves the formation of a Schiff base intermediate between a lysine residue at the active site of the enzyme and the phosphonoacetaldehyde carbonyl group, this activates the phosphonate group for attack by an active site nucleophile
additional information
-
the mechanism of C-P bond cleavage by phosphonatase involves the formation of a Schiff base intermediate between a lysine residue at the active site of the enzyme and the phosphonoacetaldehyde carbonyl group, this activates the phosphonate group for attack by an active site nucleophile
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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, 4°C, 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
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, 4°C, 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
crystal structure of the homodimeric enzyme complexed with the phosphate analogue tungstate and Mg2+
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C22A
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
C22S
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
H56A
site-directed mutagenesis, very highly reduced activity compared to the wild-type enzyme
K121R/K146R/K192R
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
K183A
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme, Lys183 is probably important in maintaining the active site environment
K183L
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme, Lys183 is probably important in maintaining the active site environment
M49L
Y128A
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
Y128F
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
Y128F/C22S
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
M49L
site-directed mutagenesis, very highly reduced activity compared to the wild-type enzyme
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8
-
deprotonation of the active site Cys may be the cause for the loss of enzyme activity
246535
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of wild-type and mutant enzymes in Escherichia coli
gene phnX, the gene is encoded within a degradative operon for the mineralization of 2-aminoethylphosphonic acid (2-AEP, ciliatine)
gene phnX, the gene is encoded within a degradative operon for the mineralization of 2-aminoethylphosphonic acid (2-AEP, ciliatine)
-
gene phnX, the gene is encoded within a degradative operon for the mineralization of 2-aminoethylphosphonic acid (2-AEP, ciliatine)
gene phnX, the gene is encoded within a degradative operon for the mineralization of 2-aminoethylphosphonic acid (2-AEP, ciliatine)
gene phnX, the gene is encoded within a degradative operon for the mineralization of 2-aminoethylphosphonic acid (2-AEP, ciliatine)
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Olsen, D.B.; Hepburn, T.W.; Moos, M.; Mariano, P.S.; Dunaway-Mariano, D.
Investigation of the Bacillus cereus phosphonoacetaldehyde hydrolase. Evidence for a Schiff base mechanism and sequence analysis of an active-site peptide containing the catalytic lysine residue
Biochemistry
27
2229-2234
1988
Bacillus cereus
brenda
La Nauze, J.M.; Coggins, J.R.; Dixon, H.B.F.
Aldolase-like imine formation in the mechanism of action of phosphonoacetaldehyde hydrolase
Biochem. J.
165
409-411
1977
Bacillus cereus
brenda
La Nauze, J.M.; Rosenberg, H.; Shaw, D.C.
The enzyme cleavage of the carbon-phosphorous bond: purification and properties of phosphonatase
Biochim. Biophys. Acta
212
332-350
1970
Bacillus cereus
brenda
Lee, S.L.; Hepburn, T.W.; Swartz, W.H.; Ammon, H.L.; Mariano, P.S.; Dunaway-Mariano, D.
Stereochemical probe for the mechanism of P-C bond cleavage catalyzed by the Bacillus cereus phosphonoacetaldehyde hydrolase
J. Am. Chem. Soc.
114
7346-7354
1992
Bacillus cereus
-
brenda
Dumora, C.; Marche, M.; Doignon, F.; Aigle, M.; Cassaigne, A.; Crouzet, M.
First characterization of the phosphonoacetaldehyde hydrolase gene of Pseudomonas aeruginosa
Gene
197
405-412
1997
Pseudomonas aeruginosa, Pseudomonas aeruginosa A237
brenda
Baker, A.S.; Ciocci, M.J.; Metcalf, W.W.; Kim, J.; Babbitt, P.C.; Wanner, B.L.; Martin, B.M.; Dunaway-Mariano, D.
Insight into the mechanism of catalysis by the P-C cleaving enzyme phosphonoacetaldehyde hydrolase derived from gene sequence analysis and mutagenesis
Biochemistry
37
9305-9315
1998
Bacillus cereus, Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Olsen, D.B.; Hepburn, T.W.; Lee, S.l.; Martin, B.M.; Mariano, P.S.; Dunaway-Mariano, D.
Investigation of the substrate binding and catalytic groups of the P-C bond cleaving enzyme, phosphonoacetaldehyde hydrolase
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1992
Bacillus cereus, Bacillus cereus AI-2
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Morais, M.C.; Zhang, W.; Baker, A.S.; Zhang, G.; Dunaway-Mariano, D.; Allen, K.N.
The crystal structure of Bacillus cereus phosphonoacetaldehyde hydrolase insight into catalysis of phosphorus bond cleavage and catalytic diversification within the HAD enzyme superfamily
Biochemistry
39
10385-10396
2000
Bacillus cereus
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Zhang, G.; Mazurkie, A.S.; Dunaway-Mariano, D.; Allen, K.N.
Kinetic evidence for a substrate-induced fit in phosphonoacetaldehyde hydrolase catalysis
Biochemistry
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13370-13377
2002
Bacillus cereus (O31156), Bacillus cereus
brenda
Zhang, G.; Morais, M.C.; Dai, J.; Zhang, W.; Dunaway-Mariano, D.; Allen, K.N.
Investigation of metal ion binding in phosphonoacetaldehyde hydrolase identifies sequence markers for metal-activated enzymes of the HAD enzyme superfamily
Biochemistry
43
4990-4997
2004
Bacillus cereus (O31156), Bacillus cereus
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Morais, M.C.; Zhang, G.; Zhang, W.; Olsen, D.B.; Dunaway-Mariano, D.; Allen, K.N.
X-ray crystallographic and site-directed mutagenesis analysis of the mechanism of Schiff-base formation in phosphonoacetaldehyde hydrolase catalysis
J. Biol. Chem.
279
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2004
Bacillus cereus (O31156)
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Dumora, C.; Lacoste, A.M.; Cassaigne, A.; Mazat, J.P.
Allosteric regulation of phosphonoacetaldehyde hydrolase by n-butylphosphonic acid
Biochem. J.
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Pseudomonas aeruginosa, Pseudomonas aeruginosa A237
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Lahiri, S.D.; Zhang, G.; Dai, J.; Dunaway-Mariano, D.; Allen, K.N.
Analysis of the substrate specificity loop of the HAD superfamily cap domain
Biochemistry
43
2812-2820
2004
Bacillus cereus
brenda
Ternan, N.G.; Quinn, J.P.
Phosphate starvation-independent 2-aminoethylphosphonic acid biodegradation in a newly isolated strain of Pseudomonas putida, NG2
Syst. Appl. Microbiol.
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346-352
1998
Klebsiella aerogenes, Pseudomonas putida, Pseudomonas putida NG2, Klebsiella aerogenes IFO 12010
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Szefczyk, B.; Kedzierski, P.; Sokalski, W.A.; Leszczynski, J.
Theoretical insights into catalysis by phosphonoacetaldehyde hydrolase
Mol. Phys.
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Bacillus cereus
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Szefczyk, B.
Towards understanding phosphonoacetaldehyde hydrolase: an alternative mechanism involving proton transfer that triggers P-C bond cleavage
Chem. Commun. (Camb. )
2008
4162-4164
2008
Bacillus cereus
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Cooley, N.A.; Kulakova, A.N.; Villarreal-Chiu, J.F.; Gilbert, J.A.; McGrath, J.W.; Quinn, J.P.
Phosphonoacetate biosynthesis: in vitro detection of a novel NADP(+)-dependent phosphonoacetaldehyde-oxidizing activity in cell-extracts of the marine Roseovarius nubinhibens ISM
Microbiology
80
335-340
2011
Roseovarius nubinhibens
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Klimek-Ochab, M.; Mucha, A.; Zymanczyk-Duda, E.
2-Aminoethylphosphonate utilization by the cold-adapted Geomyces pannorum P11 strain
Curr. Microbiol.
68
330-335
2014
Pseudogymnoascus pannorum (A0A093YC30), Pseudogymnoascus pannorum, Pseudogymnoascus pannorum VKM F-3808 (A0A093YC30)
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Villarreal-Chiu, J.F.; Quinn, J.P.; McGrath, J.W.
The genes and enzymes of phosphonate metabolism by bacteria, and their distribution in the marine environment
Front. Microbiol.
3
19
2012
Klebsiella aerogenes, Salmonella enterica subsp. enterica serovar Typhimurium (Q7ZAP3), Pseudomonas putida (Q8RSQ3), Pseudomonas aeruginosa (Q9I433), Pseudomonas putida NG2 (Q8RSQ3)
brenda
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