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Information on EC 2.6.1.37 - 2-aminoethylphosphonate-pyruvate transaminase
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2.6.1.37 2-aminoethylphosphonate-pyruvate transaminaseIUBMB Comments
A pyridoxal-phosphate protein. 2-Aminoethylarsonate can replace 2-aminoethylphosphonate as a substrate.
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The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
2-aminoethylphosphonate:pyruvate aminotransferase, 2-aminoethylphosphonate aminotransferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(2-aminoethyl)phosphonate aminotransferase
-
-
-
-
(2-aminoethyl)phosphonate transaminase
-
-
-
-
(2-aminoethyl)phosphonic acid aminotransferase
-
-
-
-
2-aminoethylphosphonate aminotransferase
-
-
-
-
2-aminoethylphosphonate-pyruvate aminotransferase
-
-
-
-
2-aminoethylphosphonate:pyruvate aminotransferase
aminotransferase, (2-aminoethyl)phosphonate
-
-
-
-
PA1310
phnW
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(2-aminoethyl)phosphonate + pyruvate = 2-phosphonoacetaldehyde + L-alanine
bi-bi ping-pong mechanism
-
(2-aminoethyl)phosphonate + pyruvate = 2-phosphonoacetaldehyde + L-alanine
ping-pong bi-bi mechanism
-
(2-aminoethyl)phosphonate + pyruvate = 2-phosphonoacetaldehyde + L-alanine
stereochemistry, 2-aminoethylphosphonate-pyruvate transaminase catalyses the abstraction of the pro-S hydrogen atom at the prochiral C2 carbon of 2-aminoethylphosphonate
-
(2-aminoethyl)phosphonate + pyruvate = 2-phosphonoacetaldehyde + L-alanine
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amino group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
-
, ,
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SYSTEMATIC NAME
IUBMB Comments
(2-aminoethyl)phosphonate:pyruvate aminotransferase
A pyridoxal-phosphate protein. 2-Aminoethylarsonate can replace 2-aminoethylphosphonate as a substrate.
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CAS REGISTRY NUMBER
COMMENTARY
37277-91-1
-
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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
2-aminoethylarsonic acid + pyruvate
alanine + 2-arsonoacetaldehyde
-
-
-
?
2-phosphonoacetaldehyde + D-alanine
(2-aminoethyl)phosphonate + pyruvate
-
L-alanine is preferred but not absolutely required
-
?
alpha-ketoglutarate + L-alanine
L-glutamate + pyruvate
-
0.25% of the kcat observed with 2-phosphonoacetaldehyde
-
?
(2-aminoethyl)phosphonate + pyruvate
2-phosphonoacetaldehyde + L-alanine
-
-
-
?
(2-aminoethyl)phosphonate + pyruvate
2-phosphonoacetaldehyde + L-alanine
-
-
-
?
(2-aminoethyl)phosphonate + pyruvate
2-phosphonoacetaldehyde + L-alanine
-
-
-
?
(2-aminoethyl)phosphonate + pyruvate
2-phosphonoacetaldehyde + L-alanine
-
highly specific for pyruvate and (2-aminoethyl)phosphonate, no activity with D-penicillamine, N-ethylmaleimide, iodoacetamide, 3-aminopropylphosphonate and taurine
-
?
(2-aminoethyl)phosphonate + pyruvate
2-phosphonoacetaldehyde + L-alanine
-
trivial name ciliatine
-
?
(2-aminoethyl)phosphonate + pyruvate
2-phosphonoacetaldehyde + L-alanine
-
-
-
?
(2-aminoethyl)phosphonate + pyruvate
2-phosphonoacetaldehyde + L-alanine
-
-
-
?
(2-aminoethyl)phosphonate + pyruvate
2-phosphonoacetaldehyde + L-alanine
-
-
-
?
(2-aminoethyl)phosphonate + pyruvate
2-phosphonoacetaldehyde + L-alanine
-
-
-
?
(2-aminoethyl)phosphonate + pyruvate
2-phosphonoacetaldehyde + L-alanine
-
-
-
?
(2-aminoethyl)phosphonate + pyruvate
2-phosphonoacetaldehyde + L-alanine
-
-
-
?
(2-aminoethyl)phosphonate + pyruvate
2-phosphonoacetaldehyde + L-alanine
-
-
-
?
(2-aminoethyl)phosphonate + pyruvate
2-phosphonoacetaldehyde + L-alanine
-
highly specific for (2-aminoethyl)phosphonate, no activity with oxaloacetate as NH3 donor
-
r
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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
(2-aminoethyl)phosphonate + pyruvate
2-phosphonoacetaldehyde + L-alanine
-
-
-
-
?
(2-aminoethyl)phosphonate + pyruvate
2-phosphonoacetaldehyde + L-alanine
-
-
-
?
(2-aminoethyl)phosphonate + pyruvate
2-phosphonoacetaldehyde + L-alanine
-
-
-
?
(2-aminoethyl)phosphonate + pyruvate
2-phosphonoacetaldehyde + L-alanine
-
-
-
?
(2-aminoethyl)phosphonate + pyruvate
2-phosphonoacetaldehyde + L-alanine
-
-
-
?
(2-aminoethyl)phosphonate + pyruvate
2-phosphonoacetaldehyde + L-alanine
-
-
-
?
(2-aminoethyl)phosphonate + pyruvate
2-phosphonoacetaldehyde + L-alanine
-
-
-
?
(2-aminoethyl)phosphonate + pyruvate
2-phosphonoacetaldehyde + L-alanine
-
-
-
?
(2-aminoethyl)phosphonate + pyruvate
2-phosphonoacetaldehyde + L-alanine
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
a pyridoxal phosphate protein, 4 mol of pyridoxal phosphate per mol of enzyme
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Aminomethylphosphonate
-
inhibitor/substrate ratio = 3, 50% inhibition
DL-1-Aminobutylphosphonate
-
inhibitor/substrate ratio = 3, 22% inhibition
DL-1-Aminopentylphosphonate
-
inhibitor/substrate ratio = 3, 22% inhibition
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.11
(2-aminoethyl)phosphonate
-
pH 8.5, 25°C, synthesis of 2-phosphonoacetaldehyde
0.009
2-phosphonoacetaldehyde
-
pH 8.5, 25°C, synthesis of (2-aminoethyl)phosphonate
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.02
(2-aminoethyl)phosphonate
-
pH 8.5, 25°C, synthesis of 2-phosphonoacetaldehyde, R340K and R340A mutant enzymes
7.4
(2-aminoethyl)phosphonate
-
pH 8.5, 25°C, synthesis of 2-phosphonoacetaldehyde
0.02
2-phosphonoacetaldehyde
-
pH 8.5, 25°C, synthesis of (2-aminoethyl)phosphonate, R340A mutant enzyme
0.6
2-phosphonoacetaldehyde
-
pH 8.5, 25°C, synthesis of (2-aminoethyl)phosphonate, R340K mutant enzyme
9.3
2-phosphonoacetaldehyde
-
pH 8.5, 25°C, synthesis of (2-aminoethyl)phosphonate
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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
7.3 - 10.8
-
approx. 20% of maximal activity at pH 7.3, approx. 60% of maximal activity at pH 10.8, no activity above pH 11.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 65
-
approx. 70% of maximal activity at 30°C, approx. 35% of maximal activity at 65°C
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
gene phnW, encoding 2-aminoethylphosphonate:pyruvate aminotransferase, exhibits reduced expression in the oxyR mutant compared to wild-type bacteria. A phnW mutant is more susceptible to tert-butyl-hydroperoxide (t-BOOH) treatment than wild-type bacteria. This may be due to a reduced efficiency for this strain to degrade t-BOOH relative to wild-type organisms because of modulation of AHP gene transcription in the phnW mutant. Provision of the phnW gene in trans can also protect a strain lacking AhpC and Ohr proteins (ohr ahpC mutant), that have previously been shown to be highly susceptible to organic hydroperoxides including t-BOOH. The phnW mutant degrades only 55% of the t-BOOH compared to the 80% degradation observed in wild-type bacteria at the end of assay
malfunction
-
gene phnW, encoding 2-aminoethylphosphonate:pyruvate aminotransferase, exhibits reduced expression in the oxyR mutant compared to wild-type bacteria. A phnW mutant is more susceptible to tert-butyl-hydroperoxide (t-BOOH) treatment than wild-type bacteria. This may be due to a reduced efficiency for this strain to degrade t-BOOH relative to wild-type organisms because of modulation of AHP gene transcription in the phnW mutant. Provision of the phnW gene in trans can also protect a strain lacking AhpC and Ohr proteins (ohr ahpC mutant), that have previously been shown to be highly susceptible to organic hydroperoxides including t-BOOH. The phnW mutant degrades only 55% of the t-BOOH compared to the 80% degradation observed in wild-type bacteria at the end of assay
-
malfunction
-
gene phnW, encoding 2-aminoethylphosphonate:pyruvate aminotransferase, exhibits reduced expression in the oxyR mutant compared to wild-type bacteria. A phnW mutant is more susceptible to tert-butyl-hydroperoxide (t-BOOH) treatment than wild-type bacteria. This may be due to a reduced efficiency for this strain to degrade t-BOOH relative to wild-type organisms because of modulation of AHP gene transcription in the phnW mutant. Provision of the phnW gene in trans can also protect a strain lacking AhpC and Ohr proteins (ohr ahpC mutant), that have previously been shown to be highly susceptible to organic hydroperoxides including t-BOOH. The phnW mutant degrades only 55% of the t-BOOH compared to the 80% degradation observed in wild-type bacteria at the end of assay
-
malfunction
-
gene phnW, encoding 2-aminoethylphosphonate:pyruvate aminotransferase, exhibits reduced expression in the oxyR mutant compared to wild-type bacteria. A phnW mutant is more susceptible to tert-butyl-hydroperoxide (t-BOOH) treatment than wild-type bacteria. This may be due to a reduced efficiency for this strain to degrade t-BOOH relative to wild-type organisms because of modulation of AHP gene transcription in the phnW mutant. Provision of the phnW gene in trans can also protect a strain lacking AhpC and Ohr proteins (ohr ahpC mutant), that have previously been shown to be highly susceptible to organic hydroperoxides including t-BOOH. The phnW mutant degrades only 55% of the t-BOOH compared to the 80% degradation observed in wild-type bacteria at the end of assay
-
malfunction
-
gene phnW, encoding 2-aminoethylphosphonate:pyruvate aminotransferase, exhibits reduced expression in the oxyR mutant compared to wild-type bacteria. A phnW mutant is more susceptible to tert-butyl-hydroperoxide (t-BOOH) treatment than wild-type bacteria. This may be due to a reduced efficiency for this strain to degrade t-BOOH relative to wild-type organisms because of modulation of AHP gene transcription in the phnW mutant. Provision of the phnW gene in trans can also protect a strain lacking AhpC and Ohr proteins (ohr ahpC mutant), that have previously been shown to be highly susceptible to organic hydroperoxides including t-BOOH. The phnW mutant degrades only 55% of the t-BOOH compared to the 80% degradation observed in wild-type bacteria at the end of assay
-
malfunction
-
gene phnW, encoding 2-aminoethylphosphonate:pyruvate aminotransferase, exhibits reduced expression in the oxyR mutant compared to wild-type bacteria. A phnW mutant is more susceptible to tert-butyl-hydroperoxide (t-BOOH) treatment than wild-type bacteria. This may be due to a reduced efficiency for this strain to degrade t-BOOH relative to wild-type organisms because of modulation of AHP gene transcription in the phnW mutant. Provision of the phnW gene in trans can also protect a strain lacking AhpC and Ohr proteins (ohr ahpC mutant), that have previously been shown to be highly susceptible to organic hydroperoxides including t-BOOH. The phnW mutant degrades only 55% of the t-BOOH compared to the 80% degradation observed in wild-type bacteria at the end of assay
-
malfunction
-
gene phnW, encoding 2-aminoethylphosphonate:pyruvate aminotransferase, exhibits reduced expression in the oxyR mutant compared to wild-type bacteria. A phnW mutant is more susceptible to tert-butyl-hydroperoxide (t-BOOH) treatment than wild-type bacteria. This may be due to a reduced efficiency for this strain to degrade t-BOOH relative to wild-type organisms because of modulation of AHP gene transcription in the phnW mutant. Provision of the phnW gene in trans can also protect a strain lacking AhpC and Ohr proteins (ohr ahpC mutant), that have previously been shown to be highly susceptible to organic hydroperoxides including t-BOOH. The phnW mutant degrades only 55% of the t-BOOH compared to the 80% degradation observed in wild-type bacteria at the end of assay
-
malfunction
-
gene phnW, encoding 2-aminoethylphosphonate:pyruvate aminotransferase, exhibits reduced expression in the oxyR mutant compared to wild-type bacteria. A phnW mutant is more susceptible to tert-butyl-hydroperoxide (t-BOOH) treatment than wild-type bacteria. This may be due to a reduced efficiency for this strain to degrade t-BOOH relative to wild-type organisms because of modulation of AHP gene transcription in the phnW mutant. Provision of the phnW gene in trans can also protect a strain lacking AhpC and Ohr proteins (ohr ahpC mutant), that have previously been shown to be highly susceptible to organic hydroperoxides including t-BOOH. The phnW mutant degrades only 55% of the t-BOOH compared to the 80% degradation observed in wild-type bacteria at the end of assay
-
physiological function
the OxyR-regulated phnW gene encoding enzyme 2-aminoethylphosphonate:pyruvate aminotransferase helps protect Pseudomonas aeruginosa from tert-butyl hydroperoxide. The LysR member of bacterial transactivators, OxyR, governs transcription of genes involved in the response to H2O2 and organic (alkyl) hydroperoxides (AHP) in the Gram-negative pathogen, Pseudomonas aeruginosa. Analysis of binding of OxyR to the phnW promoter, binding sequence determination, overview. The enzyme PhnW influences the degradation of tert-butyl-hydroperoxide (t-BOOH), but purified does not show a direct ability to degrade t-BOOH in vitro. Tert-butyl-hydroperoxide can cause apoptosis
physiological function
-
the OxyR-regulated phnW gene encoding enzyme 2-aminoethylphosphonate:pyruvate aminotransferase helps protect Pseudomonas aeruginosa from tert-butyl hydroperoxide. The LysR member of bacterial transactivators, OxyR, governs transcription of genes involved in the response to H2O2 and organic (alkyl) hydroperoxides (AHP) in the Gram-negative pathogen, Pseudomonas aeruginosa. Analysis of binding of OxyR to the phnW promoter, binding sequence determination, overview. The enzyme PhnW influences the degradation of tert-butyl-hydroperoxide (t-BOOH), but purified does not show a direct ability to degrade t-BOOH in vitro. Tert-butyl-hydroperoxide can cause apoptosis
-
physiological function
-
the OxyR-regulated phnW gene encoding enzyme 2-aminoethylphosphonate:pyruvate aminotransferase helps protect Pseudomonas aeruginosa from tert-butyl hydroperoxide. The LysR member of bacterial transactivators, OxyR, governs transcription of genes involved in the response to H2O2 and organic (alkyl) hydroperoxides (AHP) in the Gram-negative pathogen, Pseudomonas aeruginosa. Analysis of binding of OxyR to the phnW promoter, binding sequence determination, overview. The enzyme PhnW influences the degradation of tert-butyl-hydroperoxide (t-BOOH), but purified does not show a direct ability to degrade t-BOOH in vitro. Tert-butyl-hydroperoxide can cause apoptosis
-
physiological function
-
the OxyR-regulated phnW gene encoding enzyme 2-aminoethylphosphonate:pyruvate aminotransferase helps protect Pseudomonas aeruginosa from tert-butyl hydroperoxide. The LysR member of bacterial transactivators, OxyR, governs transcription of genes involved in the response to H2O2 and organic (alkyl) hydroperoxides (AHP) in the Gram-negative pathogen, Pseudomonas aeruginosa. Analysis of binding of OxyR to the phnW promoter, binding sequence determination, overview. The enzyme PhnW influences the degradation of tert-butyl-hydroperoxide (t-BOOH), but purified does not show a direct ability to degrade t-BOOH in vitro. Tert-butyl-hydroperoxide can cause apoptosis
-
physiological function
-
the OxyR-regulated phnW gene encoding enzyme 2-aminoethylphosphonate:pyruvate aminotransferase helps protect Pseudomonas aeruginosa from tert-butyl hydroperoxide. The LysR member of bacterial transactivators, OxyR, governs transcription of genes involved in the response to H2O2 and organic (alkyl) hydroperoxides (AHP) in the Gram-negative pathogen, Pseudomonas aeruginosa. Analysis of binding of OxyR to the phnW promoter, binding sequence determination, overview. The enzyme PhnW influences the degradation of tert-butyl-hydroperoxide (t-BOOH), but purified does not show a direct ability to degrade t-BOOH in vitro. Tert-butyl-hydroperoxide can cause apoptosis
-
physiological function
-
the OxyR-regulated phnW gene encoding enzyme 2-aminoethylphosphonate:pyruvate aminotransferase helps protect Pseudomonas aeruginosa from tert-butyl hydroperoxide. The LysR member of bacterial transactivators, OxyR, governs transcription of genes involved in the response to H2O2 and organic (alkyl) hydroperoxides (AHP) in the Gram-negative pathogen, Pseudomonas aeruginosa. Analysis of binding of OxyR to the phnW promoter, binding sequence determination, overview. The enzyme PhnW influences the degradation of tert-butyl-hydroperoxide (t-BOOH), but purified does not show a direct ability to degrade t-BOOH in vitro. Tert-butyl-hydroperoxide can cause apoptosis
-
physiological function
-
the OxyR-regulated phnW gene encoding enzyme 2-aminoethylphosphonate:pyruvate aminotransferase helps protect Pseudomonas aeruginosa from tert-butyl hydroperoxide. The LysR member of bacterial transactivators, OxyR, governs transcription of genes involved in the response to H2O2 and organic (alkyl) hydroperoxides (AHP) in the Gram-negative pathogen, Pseudomonas aeruginosa. Analysis of binding of OxyR to the phnW promoter, binding sequence determination, overview. The enzyme PhnW influences the degradation of tert-butyl-hydroperoxide (t-BOOH), but purified does not show a direct ability to degrade t-BOOH in vitro. Tert-butyl-hydroperoxide can cause apoptosis
-
physiological function
-
the OxyR-regulated phnW gene encoding enzyme 2-aminoethylphosphonate:pyruvate aminotransferase helps protect Pseudomonas aeruginosa from tert-butyl hydroperoxide. The LysR member of bacterial transactivators, OxyR, governs transcription of genes involved in the response to H2O2 and organic (alkyl) hydroperoxides (AHP) in the Gram-negative pathogen, Pseudomonas aeruginosa. Analysis of binding of OxyR to the phnW promoter, binding sequence determination, overview. The enzyme PhnW influences the degradation of tert-butyl-hydroperoxide (t-BOOH), but purified does not show a direct ability to degrade t-BOOH in vitro. Tert-butyl-hydroperoxide can cause apoptosis
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
16500
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals of Se-Met containing 2-aminoethylphosphonate-pyruvate transaminase, hanging drop vapor diffusion at 4°C, enzyme solution containing 0.45 mM protein, 8 mM phosphate buffer, pH 7.5, 0.8 mM dithiothreitol and 20 mM phosphonacetaldehyde is equilibrated against a reservoir solution containing 200 mM ammonium acetate, 100 mM sodium citrate, pH 5.0, and 10-13% monomethyl polyethylene glycol 5000, yellow crystals appear within 2 weeks
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
poly(ethyleneimine), heat treatment, ammonium sulfate, DEAE-cellulose, hydroxyapatite, Ultrogel AcA
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
La Nauze, J.M.; Rosenberg, H.
The identification of 2-phosphonoacetaldehyde as an intermediate in the degradation of 2-aminoethylphosphonate by Bacillus cereus
Biochim. Biophys. Acta
165
438-447
1968
Bacillus cereus
brenda
Dumora, C.; Lacoste, A.M.; Cassaigne, A.
Purification and properties of 2-aminoethylphosphonate:pyruvate aminotransferase from Pseudomonas aeruginosa
Eur. J. Biochem.
133
119-125
1983
Pseudomonas aeruginosa
brenda
Lacoste, A.M.; Dumora, C.; Balas, L.; Hammerschmidt, F.; Vercauteren, J.
Stereochemistry of the reaction catalysed by 2-aminoethylphosphonate aminotransferase. A 1H-NMR study
Eur. J. Biochem.
215
841-844
1993
Pseudomonas aeruginosa
brenda
Lacoste, A.M.; Dumora, C.; Ali, B.R.S.; Neuzil, E.; Dixon, H.B.F.
Utilization of 2-aminoethylarsonic acid in Pseudomonas aeruginosa
J. Gen. Microbiol.
138
1283-1287
1992
Pseudomonas aeruginosa
brenda
Kim, A.D.; Baker, A.S.; Dunaway-Mariano, D.; Metcalf, W.W.; Wanner, B.L.; Martin, B.M.
The 2-aminoethylphosphonate-specific transaminase of the 2-aminoethylphosphonate degradation pathway
J. Bacteriol.
184
4134-4140
2002
Salmonella enterica, Pseudomonas aeruginosa (Q51573)
brenda
Chen, C.C.; Zhang, H.; Kim, A.D.; Howard, A.; Sheldrick, G.M.; Mariano-Dunaway, D.; Herzberg, O.
Degradation pathway of the phosphonate ciliatine: crystal structure of 2-aminoethylphosphonate transaminase
Biochemistry
41
13162-13169
2002
Salmonella enterica
brenda
Panmanee, W.; Charoenlap, N.; Atichartpongkul, S.; Mahavihakanont, A.; Whiteside, M.D.; Winsor, G.; Brinkman, F.S.L.; Mongkolsuk, S.; Hassett, D.J.
The OxyR-regulated phnW gene encoding 2-aminoethylphosphonate pyruvate aminotransferase helps protect Pseudomonas aeruginosa from tert-butyl hydroperoxide
PLoS ONE
12
e0189066
2017
Pseudomonas aeruginosa (Q9I434), Pseudomonas aeruginosa, Pseudomonas aeruginosa ATCC 15692 (Q9I434), Pseudomonas aeruginosa 1C (Q9I434), Pseudomonas aeruginosa PRS 101 (Q9I434), Pseudomonas aeruginosa DSM 22644 (Q9I434), Pseudomonas aeruginosa CIP 104116 (Q9I434), Pseudomonas aeruginosa LMG 12228 (Q9I434), Pseudomonas aeruginosa JCM 14847 (Q9I434)
brenda
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