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phosphonoacetaldehyde + H2O = acetaldehyde + phosphate
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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acetonyl phosphonate + H2O
?
p-nitrophenylphosphate + H2O
p-nitrophenol + phosphate
-
hydrolyzed at considerable lower rate than phosphonoacetaldehyde
-
-
?
phosphonoacetaldehyde + H2O
acetaldehyde + phosphate
phosphonoacetylaldehyde + H2O
acetaldehyde + phosphate
thiophosphonoacetaldehyde + H2O
thiophosphate + acetaldehyde
acetonyl phosphonate + H2O
?
-
-
-
-
?
acetonyl phosphonate + H2O
?
-
-
-
-
?
phosphonoacetaldehyde + H2O
acetaldehyde + phosphate
-
-
-
-
?
phosphonoacetaldehyde + H2O
acetaldehyde + phosphate
-
-
ir
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
-
-
-
?
phosphonoacetaldehyde + H2O
acetaldehyde + phosphate
-
-
-
?
phosphonoacetaldehyde + H2O
acetaldehyde + phosphate
-
-
-
?
phosphonoacetaldehyde + H2O
acetaldehyde + phosphate
-
-
-
?
phosphonoacetaldehyde + H2O
acetaldehyde + phosphate
-
-
-
-
?
phosphonoacetaldehyde + H2O
acetaldehyde + phosphate
-
-
-
?
phosphonoacetylaldehyde + H2O
acetaldehyde + phosphate
-
-
-
?
phosphonoacetylaldehyde + H2O
acetaldehyde + phosphate
-
-
-
?
phosphonoacetylaldehyde + H2O
acetaldehyde + phosphate
-
-
-
?
phosphonoacetylaldehyde + H2O
acetaldehyde + phosphate
-
-
-
?
phosphonoacetylaldehyde + H2O
acetaldehyde + phosphate
-
-
-
?
phosphonoacetylaldehyde + 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
-
-
-
?
phosphonoacetylaldehyde + H2O
acetaldehyde + phosphate
-
-
-
?
phosphonoacetylaldehyde + H2O
acetaldehyde + phosphate
-
-
-
?
thiophosphonoacetaldehyde + H2O
thiophosphate + acetaldehyde
-
-
-
-
?
thiophosphonoacetaldehyde + H2O
thiophosphate + acetaldehyde
-
-
-
-
?
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0.033 - 11
phosphonoacetaldehyde
additional information
additional information
-
0.033
phosphonoacetaldehyde
wild-type enzyme, pH 7.5, 25°C
0.033
phosphonoacetaldehyde
-
wild-type enzyme, pH 7.5, 25°C
0.033
phosphonoacetaldehyde
-
25°C, pH 7.5, wild-type enzyme
0.033
phosphonoacetaldehyde
wild-type enzyme, mutant C22S, and mutant Y128F/C22S, pH 7.5, 25°C
0.035
phosphonoacetaldehyde
mutant Y128A, pH 7.5, 25°C
0.04
phosphonoacetaldehyde
-
-
0.045
phosphonoacetaldehyde
mutant Y128F, pH 7.5, 25°C
0.054
phosphonoacetaldehyde
mutant G185D/D190G, pH 7.5, 25°C
0.056
phosphonoacetaldehyde
triple mutant K121R/K146R/K192R, pH 7.5, 25°C
0.072
phosphonoacetaldehyde
mutant D12E, pH 7.5, 25°C
0.145
phosphonoacetaldehyde
mutant H56A, pH 7.5, 25°C
0.175
phosphonoacetaldehyde
-
25°C, pH 7.5, mutant enzyme H56Q
0.193
phosphonoacetaldehyde
mutant K183A, pH 7.5, 25°C
0.52
phosphonoacetaldehyde
mutant D190A, pH 7.5, 25°C
0.53
phosphonoacetaldehyde
mutant C22A, pH 7.5, 25°C
0.77
phosphonoacetaldehyde
mutant K183L, pH 7.5, 25°C
5.1
phosphonoacetaldehyde
mutant M49L, pH 7.5, 25°C
5.1
phosphonoacetaldehyde
-
25°C, pH 7.5, mutant enzyme m49L
11
phosphonoacetaldehyde
-
25°C, pH 7.5, mutant enzyme G50A
additional information
additional information
kinetics
-
additional information
additional information
-
kinetics
-
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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16.7
2-phosphonoacetaldehyde
-
-
0.000084 - 15
phosphonoacetaldehyde
0.000084
phosphonoacetaldehyde
mutant D186A, pH 7.5, 25°C
0.0012
phosphonoacetaldehyde
mutant D12E, pH 7.5, 25°C
0.00247
phosphonoacetaldehyde
-
25°C, pH 7.5, mutant enzyme m49L
0.006
phosphonoacetaldehyde
-
25°C, pH 7.5, mutant enzyme H56Q
0.0071
phosphonoacetaldehyde
-
25°C, pH 7.5, mutant enzyme G50A
0.012
phosphonoacetaldehyde
mutant K183A, pH 7.5, 25°C
0.022
phosphonoacetaldehyde
mutant D190A, pH 7.5, 25°C
0.046
phosphonoacetaldehyde
mutant K183L, pH 7.5, 25°C
0.075
phosphonoacetaldehyde
mutant H56A, pH 7.5, 25°C
0.077
phosphonoacetaldehyde
mutant Y128A, pH 7.5, 25°C
0.25
phosphonoacetaldehyde
-
25°C, pH 7.5, wild-type enzyme
1.28
phosphonoacetaldehyde
triple mutant K121R/K146R/K192R, pH 7.5, 25°C
1.7
phosphonoacetaldehyde
mutant G185D/D190G, pH 7.5, 25°C
1.95
phosphonoacetaldehyde
mutant C22A, pH 7.5, 25°C
2.11
phosphonoacetaldehyde
mutant Y128F/C22S, pH 7.5, 25°C
2.21
phosphonoacetaldehyde
mutant Y128F, pH 7.5, 25°C
2.26
phosphonoacetaldehyde
mutant C22S, pH 7.5, 25°C
2.94
phosphonoacetaldehyde
mutant C22S, pH 7.5, 25°C
2.94
phosphonoacetaldehyde
mutant Y128F, pH 7.5, 25°C
2.94
phosphonoacetaldehyde
mutant Y128F/C22S, pH 7.5, 25°C
6.08
phosphonoacetaldehyde
triple mutant K121R/K146R/K192R, pH 7.5, 25°C
15
phosphonoacetaldehyde
wild-type enzyme, pH 7.5, 25°C
15
phosphonoacetaldehyde
-
wild-type enzyme, pH 7.5, 25°C
15
phosphonoacetaldehyde
wild-type enzyme and mutant M49L, pH 7.5, 25°C
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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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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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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
D12A
site-directed mutagenesis, catalytically inactive mutant
D186A
site-directed mutagenesis, highly reduced activity
D186A/D190A
site-directed mutagenesis, inactive mutant
D186E
site-directed mutagenesis, very highly reduced activity
D190A
site-directed mutagenesis, reduced activity
G185D/D190G
site-directed mutagenesis, reduced activity
G50A
-
kcat/Km is 12820fold lower than wild-type value
G50P
-
inactive mutant protein
G50V
-
inactive mutant protein
H56A
site-directed mutagenesis, very highly reduced activity compared to the wild-type enzyme
H56Q
-
kcat/Km is 238fold lower than wild-type value
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
K53A
-
inactive mutant protein
K53R
-
inactive mutant protein
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
M49L
-
kcat/Km is 17241fold lower than wild-type value
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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
Arch. Biochem. Biophys.
296
144-151
1992
Bacillus cereus, Bacillus cereus AI-2
brenda
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
brenda
Zhang, G.; Mazurkie, A.S.; Dunaway-Mariano, D.; Allen, K.N.
Kinetic evidence for a substrate-induced fit in phosphonoacetaldehyde hydrolase catalysis
Biochemistry
41
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
brenda
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
9353-9361
2004
Bacillus cereus (O31156)
brenda
Dumora, C.; Lacoste, A.M.; Cassaigne, A.; Mazat, J.P.
Allosteric regulation of phosphonoacetaldehyde hydrolase by n-butylphosphonic acid
Biochem. J.
280
557-559
1991
Pseudomonas aeruginosa, Pseudomonas aeruginosa A237
brenda
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.
21
346-352
1998
Klebsiella aerogenes, Pseudomonas putida, Pseudomonas putida NG2, Klebsiella aerogenes IFO 12010
brenda
Szefczyk, B.; Kedzierski, P.; Sokalski, W.A.; Leszczynski, J.
Theoretical insights into catalysis by phosphonoacetaldehyde hydrolase
Mol. Phys.
104
2203-2211
2006
Bacillus cereus
-
brenda
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
brenda
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
brenda
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)
brenda
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