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phosphonoacetate + H2O
?
-
inducible only in the presence of its sole substrate, does not require phosphate starvation
-
-
?
Phosphonoacetate + H2O
acetate + phosphate
additional information
?
-
Phosphonoacetate + H2O
acetate + phosphate
-
route of microbial metabolism of xenobiotic organophosphonates, substrate can serve as the sole source of carbon, energy and phosphate for the organism in the range of 40-100 mM
-
-
?
Phosphonoacetate + H2O
acetate + phosphate
-
absolutely specific for, overview
-
-
?
Phosphonoacetate + H2O
acetate + phosphate
-
route of microbial metabolism of xenobiotic organophosphonates, substrate can serve as the sole source of carbon, energy and phosphate for the organism in the range of 40-100 mM
-
-
?
Phosphonoacetate + H2O
acetate + phosphate
-
absolutely specific for, overview
-
-
?
Phosphonoacetate + H2O
acetate + phosphate
-
-
-
-
?
Phosphonoacetate + H2O
acetate + phosphate
-
-
-
?
Phosphonoacetate + H2O
acetate + phosphate
-
-
-
?
Phosphonoacetate + H2O
acetate + phosphate
-
-
-
?
Phosphonoacetate + H2O
acetate + phosphate
-
-
-
?
Phosphonoacetate + H2O
acetate + phosphate
-
-
-
-
?
Phosphonoacetate + H2O
acetate + phosphate
-
-
-
?
Phosphonoacetate + H2O
acetate + phosphate
metal-assisted hydrolytic cleavage of the C-P bond
-
-
?
Phosphonoacetate + H2O
acetate + phosphate
-
-
-
-
?
Phosphonoacetate + H2O
acetate + phosphate
-
-
-
?
Phosphonoacetate + H2O
acetate + phosphate
-
-
-
?
Phosphonoacetate + H2O
acetate + phosphate
-
route of microbial metabolism of xenobiotic organophosphonates, substrate can serve as the sole source of carbon, energy and phosphate for the organism in the range of 40-100 mM
-
-
?
Phosphonoacetate + H2O
acetate + phosphate
-
absolutely specific for, overview
-
-
?
Phosphonoacetate + H2O
acetate + phosphate
-
route of microbial metabolism of xenobiotic organophosphonates, substrate can serve as the sole source of carbon, energy and phosphate for the organism in the range of 40-100 mM
-
-
?
Phosphonoacetate + H2O
acetate + phosphate
-
absolutely specific for, overview
-
-
?
Phosphonoacetate + H2O
acetate + phosphate
-
-
-
-
?
Phosphonoacetate + H2O
acetate + phosphate
-
-
-
-
?
Phosphonoacetate + H2O
acetate + phosphate
-
-
-
?
additional information
?
-
-
substrate specificity, overview. No activity with fosfomycin or phosphonopyruvate
-
-
?
additional information
?
-
-
substrate specificity, overview. No activity with fosfomycin or phosphonopyruvate
-
-
?
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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
evolution
-
the P-C bond cleaving enzyme phosphonoacetate hydrolase belongs to the alkaline phosphatase superfamily
evolution
the enzyme is a member of the alkaline phosphatase superfamily. Distributionof phnX homologs within sequenced bacterial genomes, overview
evolution
-
the P-C bond cleaving enzyme phosphonoacetate hydrolase belongs to the alkaline phosphatase superfamily
-
metabolism
2-aminoethylphosphonate is catabolized to phosphonoacetate, which is converted to acetate and inorganic phosphate by phosphonoacetate hydrolase, PhnA
metabolism
-
the enzyme catalyzes a step in the 2-aminoethylphosphonate degradation, conversion of 2-aminoethylphosphonate to phosphate and degradation of phosphonate compounds, pathway overview
metabolism
-
the enzyme is involved in the 2-aminoethylphosphonic acid degradation pathway, overview
metabolism
-
the enzyme is involved in the pathway of 2-aminoethylphosphonic acid degradation, overview
metabolism
catabolic C-P-bond metabolism in bacteria, and the pathways for the microbial metabolism of phosphonates, overview. The enzyme is involved in the phosphonoacetate catabolism
metabolism
-
the enzyme is involved in the 2-aminoethylphosphonic acid degradation pathway, overview
-
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expression in Escherichia coli and Pseudomonas putida
-
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
-
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
-
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, 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, 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, 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, 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
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McGrath, J.W.; Wisdom, G.B.; McMullan, G.; Larkin, M.J.; Quinn, J.P.
The purification and properties of phosphonoacetate hydrolase, a novel carbon-phosphorus bond-cleavage enzyme from Pseudomonas fluorescens 23F
Eur. J. Biochem.
234
225-230
1995
Pseudomonas fluorescens, Pseudomonas fluorescens 23F
brenda
McGrath, J.W.; Quinn, J.P.
A plate assay for the detection of organophosphonate mineralization by environmental bacteria, and its modification as an activity stain for identification of the phosphonocacetate hydrolase
Biotechnol. Tech.
9
497-502
1995
Pseudomonas fluorescens, Pseudomonas fluorescens 23F
-
brenda
McMullan, G.; Quinn, J.P.
In vitro characterization of a phosphate starvation-independent carbon-phosphorus bond cleavage activity in Pseudomonas fluorescens
J. Bacteriol.
176
320-324
1994
Pseudomonas fluorescens
brenda
Kulakova, A.N.; Kulakov, L.A.; Quinn, J.P.
Cloning of the phosphonoacetate hydrolase gene from Pseudomonas fluorescens 23F encoding a new type of carbon-phosphorus bond cleaving enzyme and its expression in Echerichia coli and Pseudomonas putida
Gene
195
49-53
1997
Pseudomonas fluorescens
brenda
McGrath, J.W.; Kulakova, A.N.; Quinn, J.P.
A comparison of three bacterial phosphonoacetate hydrolases from different environmental sources
J. Appl. Microbiol.
86
834-840
1999
Pseudomonas sp., Curtobacterium sp., Pseudomonas sp. PA2, Curtobacterium sp. PA1
-
brenda
Forlani, G.; Klimek-Ochab, M.; Jaworski, J.; Lejczak, B.; Picco, A.M.
Phosphonoacetic acid utilization by fungal isolates: occurrence and properties of a phosphonoacetate hydrolase in some penicillia
Mycol. Res.
110
1455-1463
2006
Penicillium oxalicum
brenda
O'Loughlin, S.N.; Graham, R.L.; McMullan, G.; Ternan, N.G.
A role for carbon catabolite repression in the metabolism of phosphonoacetate by Agromyces fucosus Vs2
FEMS Microbiol. Lett.
261
133-140
2006
Agromyces fucosus, Agromyces fucosus Vs2
brenda
Klimek-Ochab, M.; Raucci, G.; Lejczak, B.; Forlani, G.
Phosphonoacetate hydrolase from Penicillium oxalicum: Purification and properties, phosphate starvation-independent expression, and partial sequencing
Res. Microbiol.
157
125-135
2006
Penicillium oxalicum
brenda
Gilbert, J.A.; Thomas, S.; Cooley, N.A.; Kulakova, A.; Field, D.; Booth, T.; McGrath, J.W.; Quinn, J.P.; Joint, I.
Potential for phosphonoacetate utilization by marine bacteria in temperate coastal waters
Environ. Microbiol.
11
111-125
2009
Emiliania huxleyi, Sinorhizobium meliloti, Vibrio harveyi, Paraburkholderia xenovorans, Burkholderia multivorans, Burkholderia multivorans (A0A0H3KB87), Sorangium cellulosum, no activity in Vibrio shiloi, Photobacterium rosenbergii, Vibrio campbellii, Karenia mikimotoi, Sinorhizobium medicae, Verminephrobacter eiseniae (A1WGW5), Candidatus Solibacter usitatus (Q01YC7), Burkholderia ambifaria (Q0BAS3), Cupriavidus necator (Q0JZU4), Cupriavidus necator (Q0K2Z6), Rhodopseudomonas palustris (Q6N3F7), Rhodopseudomonas palustris CGA009 (Q6N3F7), Burkholderia ambifaria AMMD (Q0BAS3), Sinorhizobium medicae WSM419, Verminephrobacter eiseniae EF01-2 (A1WGW5), Vibrio campbellii CC028, Candidatus Solibacter usitatus Ellin6076 (Q01YC7), Photobacterium rosenbergii CC006, Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1 (Q0JZU4), Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1 (Q0K2Z6)
brenda
Kim, A.; Benning, M.M.; OkLee, S.; Quinn, J.; Martin, B.M.; Holden, H.M.; Dunaway-Mariano, D.
Divergence of chemical function in the alkaline phosphatase superfamily: structure and mechanism of the P-C bond cleaving enzyme phosphonoacetate hydrolase
Biochemistry
50
3481-3494
2011
Pseudomonas fluorescens, Pseudomonas fluorescens 23F
brenda
Agarwal, V.; Borisova, S.A.; Metcalf, W.W.; van der Donk, W.A.; Nair, S.K.
Structural and mechanistic insights into C-P bond hydrolysis by phosphonoacetate hydrolase
Chem. Biol.
18
1230-1240
2011
Sinorhizobium meliloti (Q92UV8)
brenda
Borisova, S.A.; Christman, H.D.; Metcalf, M.E.; Zulkepli, N.A.; Zhang, J.K.; van der Donk, W.A.; Metcalf, W.W.
Genetic and biochemical characterization of a pathway for the degradation of 2-aminoethylphosphonate in Sinorhizobium meliloti 1021
J. Biol. Chem.
286
22283-22290
2011
Sinorhizobium meliloti
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
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
Pseudomonas fluorescens (Q51782)
brenda
Perry, S.L.; Guha, S.; Pawate, A.S.; Bhaskarla, A.; Agarwal, V.; Nair, S.K.; Kenis, P.J.
A microfluidic approach for protein structure determination at room temperature via on-chip anomalous diffraction
Lab Chip
13
3183-3187
2013
Sinorhizobium meliloti
brenda