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0.41
-
in 50 mM HEPES, 200 mM NaCl, pH 7.5, temperature not specified in the publication
1.3
-
in 50 mM HEPES, 200 mM NaCl, pH 7.5, temperature not specified in the publication
0.01
-
mutant enzyme N158A, at pH 7.5 and 30°C
0.01
-
mutant enzyme N158A, with NAD+ in 50 mM HEPES, pH 7.5 supplemented with 10 mM MgSO4 for 5 min at 30°C
0.051
-
mutant enzyme R108A, at pH 7.5 and 30°C
0.051
-
mutant enzyme R108A, with NAD+ in 50 mM HEPES, pH 7.5 supplemented with 10 mM MgSO4 for 5 min at 30°C
0.076
-
mutant enzyme R447A, at pH 7.5 and 30°C
0.076
-
mutant enzyme R447A, with NAD+ in 50 mM HEPES, pH 7.5 supplemented with 10 mM MgSO4 for 5 min at 30°C
0.12
-
mutant enzyme R290A, at pH 7.5 and 30°C
0.12
-
mutant enzyme R290A, with NAD+ in 50 mM HEPES, pH 7.5 supplemented with 10 mM MgSO4 for 5 min at 30°C
0.19
-
mutant enzyme E385A, at pH 7.5 and 30°C
0.19
-
mutant enzyme E385A, with NAD+ in 50 mM HEPES, pH 7.5 supplemented with 10 mM MgSO4 for 5 min at 30°C
2.2
-
wild type enzyme, at pH 7.5 and 30°C
2.2
-
wild type enzyme, with NAD+ in 50 mM HEPES, pH 7.5 supplemented with 10 mM MgSO4 for 5 min at 30°C
0.02
-
pH 8.5, 25°C, synthesis of (2-aminoethyl)phosphonate, R340A mutant enzyme
0.6
-
pH 8.5, 25°C, synthesis of (2-aminoethyl)phosphonate, R340K mutant enzyme
9.3
-
pH 8.5, 25°C, synthesis of (2-aminoethyl)phosphonate
0.000084
-
mutant D186A, pH 7.5, 25°C
0.0012
-
mutant D12E, pH 7.5, 25°C
0.00247
-
25°C, pH 7.5, mutant enzyme m49L
0.006
-
25°C, pH 7.5, mutant enzyme H56Q
0.0071
-
25°C, pH 7.5, mutant enzyme G50A
0.012
-
mutant K183A, pH 7.5, 25°C
0.022
-
mutant D190A, pH 7.5, 25°C
0.046
-
mutant K183L, pH 7.5, 25°C
0.075
-
mutant H56A, pH 7.5, 25°C
0.077
-
mutant Y128A, pH 7.5, 25°C
0.25
-
25°C, pH 7.5, wild-type enzyme
1.28
-
triple mutant K121R/K146R/K192R, pH 7.5, 25°C
1.7
-
mutant G185D/D190G, pH 7.5, 25°C
1.95
-
mutant C22A, pH 7.5, 25°C
2.11
-
mutant Y128F/C22S, pH 7.5, 25°C
2.21
-
mutant Y128F, pH 7.5, 25°C
2.26
-
mutant C22S, pH 7.5, 25°C
2.94
-
mutant C22S, pH 7.5, 25°C
2.94
-
mutant Y128F, pH 7.5, 25°C
2.94
-
mutant Y128F/C22S, pH 7.5, 25°C
6.08
-
triple mutant K121R/K146R/K192R, pH 7.5, 25°C
15
-
wild-type enzyme and mutant M49L, pH 7.5, 25°C
15
-
wild-type enzyme, pH 7.5, 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.185
-
in 50 mM HEPES, 200 mM NaCl, pH 7.5, temperature not specified in the publication
0.031
-
in 50 mM HEPES, 200 mM NaCl, pH 7.5, temperature not specified in the publication
0.0032
-
wild type enzyme, at pH 7.5 and 30°C
0.0032
-
wild type enzyme, with NAD+ in 50 mM HEPES, pH 7.5 supplemented with 10 mM MgSO4 for 5 min at 30°C
0.005
-
mutant enzyme R290A, with NAD+ in 50 mM HEPES, pH 7.5 supplemented with 10 mM MgSO4 for 5 min at 30°C
0.0051
-
mutant enzyme R290A, at pH 7.5 and 30°C
0.009
-
mutant enzyme R108A, with NAD+ in 50 mM HEPES, pH 7.5 supplemented with 10 mM MgSO4 for 5 min at 30°C
0.0097
-
mutant enzyme R108A, at pH 7.5 and 30°C
0.019
-
mutant enzyme E385A, at pH 7.5 and 30°C
0.019
-
mutant enzyme E385A, with NAD+ in 50 mM HEPES, pH 7.5 supplemented with 10 mM MgSO4 for 5 min at 30°C
0.029
-
mutant enzyme N158A, at pH 7.5 and 30°C
0.029
-
mutant enzyme N158A, with NAD+ in 50 mM HEPES, pH 7.5 supplemented with 10 mM MgSO4 for 5 min at 30°C
0.15
-
mutant enzyme R447A, at pH 7.5 and 30°C
0.15
-
mutant enzyme R447A, with NAD+ in 50 mM HEPES, pH 7.5 supplemented with 10 mM MgSO4 for 5 min at 30°C
0.5
-
at pH 7.5 and 30°C
0.009
-
pH 8.5, 25°C, synthesis of (2-aminoethyl)phosphonate
0.19
-
pH 8.5, 25°C, R340A mutant enzyme
2.9
-
pH 8.5, 25°C, R340K mutant enzyme
0.033
-
25°C, pH 7.5, wild-type enzyme
0.033
-
wild-type enzyme, mutant C22S, and mutant Y128F/C22S, pH 7.5, 25°C
0.033
-
wild-type enzyme, pH 7.5, 25°C
0.035
-
mutant Y128A, pH 7.5, 25°C
0.045
-
mutant Y128F, pH 7.5, 25°C
0.054
-
mutant G185D/D190G, pH 7.5, 25°C
0.056
-
triple mutant K121R/K146R/K192R, pH 7.5, 25°C
0.072
-
mutant D12E, pH 7.5, 25°C
0.145
-
mutant H56A, pH 7.5, 25°C
0.175
-
25°C, pH 7.5, mutant enzyme H56Q
0.193
-
mutant K183A, pH 7.5, 25°C
0.52
-
mutant D190A, pH 7.5, 25°C
0.53
-
mutant C22A, pH 7.5, 25°C
0.77
-
mutant K183L, pH 7.5, 25°C
5.1
-
25°C, pH 7.5, mutant enzyme m49L
5.1
-
mutant M49L, pH 7.5, 25°C
11
-
25°C, pH 7.5, mutant enzyme G50A
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
1988
Olsen, D.B.; Hepburn, T.W.; Moos, M.; Mariano, P.S.; Dunaway-Mariano, D.
Biochemistry
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Aldolase-like imine formation in the mechanism of action of phosphonoacetaldehyde hydrolase
1977
La Nauze, J.M.; Coggins, J.R.; Dixon, H.B.F.
Biochem. J.
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The enzyme cleavage of the carbon-phosphorous bond: purification and properties of phosphonatase
1970
La Nauze, J.M.; Rosenberg, H.; Shaw, D.C.
Biochim. Biophys. Acta
212
332-350
-
Stereochemical probe for the mechanism of P-C bond cleavage catalyzed by the Bacillus cereus phosphonoacetaldehyde hydrolase
1992
Lee, S.L.; Hepburn, T.W.; Swartz, W.H.; Ammon, H.L.; Mariano, P.S.; Dunaway-Mariano, D.
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First characterization of the phosphonoacetaldehyde hydrolase gene of Pseudomonas aeruginosa
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Insight into the mechanism of catalysis by the P-C cleaving enzyme phosphonoacetaldehyde hydrolase derived from gene sequence analysis and mutagenesis
1998
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Biochemistry
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9305-9315
Investigation of the substrate binding and catalytic groups of the P-C bond cleaving enzyme, phosphonoacetaldehyde hydrolase
1992
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296
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The crystal structure of Bacillus cereus phosphonoacetaldehyde hydrolase insight into catalysis of phosphorus bond cleavage and catalytic diversification within the HAD enzyme superfamily
2000
Morais, M.C.; Zhang, W.; Baker, A.S.; Zhang, G.; Dunaway-Mariano, D.; Allen, K.N.
Biochemistry
39
10385-10396
Two omega-amino acid transaminases from Bacillus cereus
1977
Nakano, Y.; Tokunaga, H.; Kitaoka, S.
J. Biochem.
81
1375-1381
The identification of 2-phosphonoacetaldehyde as an intermediate in the degradation of 2-aminoethylphosphonate by Bacillus cereus
1968
La Nauze, J.M.; Rosenberg, H.
Biochim. Biophys. Acta
165
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Purification and properties of 2-aminoethylphosphonate:pyruvate aminotransferase from Pseudomonas aeruginosa
1983
Dumora, C.; Lacoste, A.M.; Cassaigne, A.
Eur. J. Biochem.
133
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Stereochemistry of the reaction catalysed by 2-aminoethylphosphonate aminotransferase. A 1H-NMR study
1993
Lacoste, A.M.; Dumora, C.; Balas, L.; Hammerschmidt, F.; Vercauteren, J.
Eur. J. Biochem.
215
841-844
The 2-aminoethylphosphonate-specific transaminase of the 2-aminoethylphosphonate degradation pathway
2002
Kim, A.D.; Baker, A.S.; Dunaway-Mariano, D.; Metcalf, W.W.; Wanner, B.L.; Martin, B.M.
J. Bacteriol.
184
4134-4140
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2002
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Biochemistry
41
13370-13377
Investigation of metal ion binding in phosphonoacetaldehyde hydrolase identifies sequence markers for metal-activated enzymes of the HAD enzyme superfamily
2004
Zhang, G.; Morais, M.C.; Dai, J.; Zhang, W.; Dunaway-Mariano, D.; Allen, K.N.
Biochemistry
43
4990-4997
X-ray crystallographic and site-directed mutagenesis analysis of the mechanism of Schiff-base formation in phosphonoacetaldehyde hydrolase catalysis
2004
Morais, M.C.; Zhang, G.; Zhang, W.; Olsen, D.B.; Dunaway-Mariano, D.; Allen, K.N.
J. Biol. Chem.
279
9353-9361
Analysis of the substrate specificity loop of the HAD superfamily cap domain
2004
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Biochemistry
43
2812-2820
Towards understanding phosphonoacetaldehyde hydrolase: an alternative mechanism involving proton transfer that triggers P-C bond cleavage
2008
Szefczyk, B.
Chem. Commun. (Camb. )
2008
4162-4164
New insight into the mechanism of methyl transfer during the biosynthesis of fosfomycin
2007
Woodyer, R.D.; Li, G.; Zhao, H.; van der Donk, W.A.
Chem. Commun. (Camb. )
4
359-361
Unusual transformations in the biosynthesis of the antibiotic phosphinothricin tripeptide
2007
Blodgett, J.A.; Thomas, P.M.; Li, G.; Velasquez, J.E.; van der Donk, W.A.; Kelleher, N.L.; Metcalf, W.W.
Nat. Chem. Biol.
3
480-485
Biosynthesis of 2-hydroxyethylphosphonate, an unexpected intermediate common to multiple phosphonate biosynthetic pathways
2008
Shao, Z.; Blodgett, J.A.V.; Circello, B.T.; Eliot, A.C.; Woodyer, R.; Li, G.; van der Donk, W.A.; Metcalf, W.W.; Zhao, H.
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Genetic and biochemical characterization of a pathway for the degradation of 2-aminoethylphosphonate in Sinorhizobium meliloti 1021
2011
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Phosphonoacetate biosynthesis: in vitro detection of a novel NADP(+)-dependent phosphonoacetaldehyde-oxidizing activity in cell-extracts of the marine Roseovarius nubinhibens ISM
2011
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Reaction of HppE with substrate analogues: evidence for carbon-phosphorus bond cleavage by a carbocation rearrangement
2013
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J. Am. Chem. Soc.
135
8153-8156
Structure and function of phosphonoacetaldehyde dehydrogenase: the missing link in phosphonoacetate formation
2014
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Chem. Biol.
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2-Aminoethylphosphonate utilization by the cold-adapted Geomyces pannorum P11 strain
2014
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68
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The genes and enzymes of phosphonate metabolism by bacteria, and their distribution in the marine environment
2012
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Front. Microbiol.
3
19
Crystal structure of PhnZ in complex with substrate reveals a di-iron oxygenase mechanism for catabolism of organophosphonates
2014
van Staalduinen, L.M.; McSorley, F.R.; Schiessl, K.; Seguin, J.; Wyatt, P.B.; Hammerschmidt, F.; Zechel, D.L.; Jia, Z.
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111
5171-5176
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