stereochemistry, 2-aminoethylphosphonate-pyruvate transaminase catalyses the abstraction of the pro-S hydrogen atom at the prochiral C2 carbon of 2-aminoethylphosphonate
highly specific for pyruvate and (2-aminoethyl)phosphonate, no activity with D-penicillamine, N-ethylmaleimide, iodoacetamide, 3-aminopropylphosphonate and taurine
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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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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