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Literature summary extracted from

  • Graham, S.B.; Stephenson, J.T.; Wood, J.M.
    Proline dehydrogenase from Escherichia coli K12. Reconstitution of a functional membrane association (1984), J. Biol. Chem., 259, 2656-2661.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.5.5.2 5-ethylpentyl-barbituric acid membrane-associated enzyme, not soluble enzyme Escherichia coli
1.5.5.2 cyanide only membrane-associated enzyme, not soluble enzyme Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.5.5.2 2 6 L-proline membrane-bound enzyme Escherichia coli
1.5.5.2 45 105 L-proline soluble enzyme Escherichia coli

Localization

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

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.5.5.2 L-proline + acceptor + H2O Escherichia coli
-
 (S)-1-pyrroline-5-carboxylate + reduced acceptor
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.5.5.2 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.5.5.2
-
 Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.5.2 L-proline + acceptor + H2O
-
 Escherichia coli (S)-1-pyrroline-5-carboxylate + reduced acceptor
-
 ?
1.5.5.2 L-proline + acceptor + H2O enzyme exists in soluble and in membrane associated forms differing in catalytic properties Escherichia coli (S)-1-pyrroline-5-carboxylate + reduced acceptor
-
 ?
1.5.5.2 L-proline + acceptor + H2O acceptors: 2,6-dichlorophenolindophenol, phenazine methosulfate, ferricyanide, menadione, cytochrome c Escherichia coli (S)-1-pyrroline-5-carboxylate + reduced acceptor
-
 ?

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.5.2 FAD
-
 Escherichia coli