EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
   1.4.5.1 | 3,4-dehydro-DL-proline + oxidized 2,6-dichloroindophenol |
when membrane fractions from Escherichia coli strain UMM5 (putA1::Tn5 proC24) lacking both L-proline dehydrogenase and L-DELTA1-pyrroline-5-carboxylate reductase are incubated with 3,4-dehydro-DL-proline, pyrrole-2-carboxylate is formed. Oxidation of 3,4-dehydro-DL-proline by membrane fractions from strain UMM5 is induced by growth in minimal medium containing D- or L-alanine. An Escherichia coli strain with no D-alanine dehydrogenase activity due to the dadA237 mutation is unable to oxidize either 3,4-dehydro-D-proline or D-alanine, as are spontaneous Dad- mutants of Escherichia coli strain UMM5. Membrane fractions containing D-alanine dehydrogenase also catalyze the oxidation of D-2-aminobutyrate, D-norvaline, D-norleucine, cis-4-hydroxy-D-proline, and DL-ethionine. D-Alanine dehydrogenase is responsible for the residual 3,4-dehydro-DL-proline oxidation activity in putA proC mutants of Escherichia coli. This enzyme plays a general role in the metabolism of D-amino acids and their analogues |
Escherichia coli |
? |
- |
? |
| 1.4.5.1 | 3,4-dehydro-DL-proline + oxidized 2,6-dichloroindophenol |
when membrane fractions from Escherichia coli strain UMM5 (putA1::Tn5 proC24) lacking both L-proline dehydrogenase and L-DELTA1-pyrroline-5-carboxylate reductase are incubated with 3,4-dehydro-DL-proline, pyrrole-2-carboxylate is formed. Oxidation of 3,4-dehydro-DL-proline by membrane fractions from strain UMM5 is induced by growth in minimal medium containing D- or L-alanine. An Escherichia coli strain with no D-alanine dehydrogenase activity due to the dadA237 mutation is unable to oxidize either 3,4-dehydro-D-proline or D-alanine, as are spontaneous Dad- mutants of Escherichia coli strain UMM5. Membrane fractions containing D-alanine dehydrogenase also catalyze the oxidation of D-2-aminobutyrate, D-norvaline, D-norleucine, cis-4-hydroxy-D-proline, and DL-ethionine. D-Alanine dehydrogenase is responsible for the residual 3,4-dehydro-DL-proline oxidation activity in putA proC mutants of Escherichia coli. This enzyme plays a general role in the metabolism of D-amino acids and their analogues |
Escherichia coli UMM5 (putA1::Tn5 proC24) |
? |
- |
? |
| 1.4.5.1 | beta-chloro-D-alanine + oxidized acceptor + H2O |
assayed in toluenized cells, reaction rate is 20% of the activity with D-alanine |
Escherichia coli K-12 |
? + NH3 + reduced acceptor |
- |
? |
| 1.4.5.1 | D-2-amino-n-butyrate + oxidized 2,6-dichlorophenolindophenol + H2O |
38% of the activity compared to D-alanine |
Escherichia coli |
2-oxobutyrate + NH3 + reduced 2,6-dichloroindophenol |
- |
? |
| 1.4.5.1 | D-2-amino-n-butyrate + oxidized 2,6-dichlorophenolindophenol + H2O |
81% of the activity with D-alanine |
Pseudomonas aeruginosa |
2-oxobutyrate + NH3 + reduced 2,6-dichloroindophenol |
- |
? |
| 1.4.5.1 | D-2-amino-n-butyrate + oxidized 2,6-dichlorophenolindophenol + H2O |
89% of the activity compared to D-alanine |
Escherichia coli B |
2-oxobutyrate + NH3 + reduced 2,6-dichloroindophenol |
- |
? |
| 1.4.5.1 | D-Ala + oxidized coenzyme Q1 + H2O |
specific activity is 37% of that with D-proline |
Helicobacter pylori |
pyruvate + NH3 + reduced coenzyme Q1 |
- |
? |
| 1.4.5.1 | D-alanine + oxidized 2,6-dichloroindophenol + H2O |
- |
Escherichia coli |
pyruvate + NH3 + reduced 2,6-dichloroindophenol |
- |
? |
| 1.4.5.1 | D-alanine + oxidized 2,6-dichloroindophenol + H2O |
- |
Pseudomonas aeruginosa |
pyruvate + NH3 + reduced 2,6-dichloroindophenol |
- |
? |
| 1.4.5.1 | D-alanine + oxidized 2,6-dichloroindophenol + H2O |
- |
Escherichia coli B |
pyruvate + NH3 + reduced 2,6-dichloroindophenol |
- |
? |
