Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Deutch, C.E.
    Oxidation of 3,4-dehydro-D-proline and other D-amino acid analogues by D-alanine dehydrogenase from Escherichia coli (2004), FEMS Microbiol. Lett., 238, 383-389.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.4.5.1 D-alanine oxidation of 3,4-dehydro-DL-proline by membrane fractions from strain UMM5 is competitively inhibited by D-alanine Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.4.5.1 membrane
-
Escherichia coli 16020
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.4.5.1 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 ?
-
?
1.4.5.1 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

EC Number Organism UniProt Comment Textmining
1.4.5.1 Escherichia coli
-
-
-
1.4.5.1 Escherichia coli UMM5 (putA1::Tn5 proC24)
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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) ?
-
?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.4.5.1 9
-
oxidation of 3,4-dehydro-DL-proline by membrane fractions from strain UMM5 has a pH optimum of 9 Escherichia coli