2.6.1.37: 2-aminoethylphosphonate-pyruvate transaminase
This is an abbreviated version!
For detailed information about 2-aminoethylphosphonate-pyruvate transaminase, go to the full flat file.
Reaction
Synonyms
(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
ECTree
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General Information
General Information on EC 2.6.1.37 - 2-aminoethylphosphonate-pyruvate transaminase
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malfunction
physiological function
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
-
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
-