Inhibitors | Comment | Organism | Structure |
---|---|---|---|
D-alanine | oxidation of 3,4-dehydro-DL-proline by membrane fractions from strain UMM5 is competitively inhibited by D-alanine | Escherichia coli |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | - |
Escherichia coli | 16020 | - |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
3,4-dehydro-DL-proline + oxidized 2,6-dichloroindophenol | Escherichia coli | 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 | ? | - |
? | |
3,4-dehydro-DL-proline + oxidized 2,6-dichloroindophenol | Escherichia coli UMM5 (putA1::Tn5 proC24) | 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 | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Escherichia coli UMM5 (putA1::Tn5 proC24) | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
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 | ? | - |
? | |
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) | ? | - |
? |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
9 | - |
oxidation of 3,4-dehydro-DL-proline by membrane fractions from strain UMM5 has a pH optimum of 9 | Escherichia coli |