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Literature summary for 1.5.5.2 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
Search for more literature for 1.5.5.2

Inhibitors

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

KM Value [mM]

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

Localization

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-proline + acceptor + H2O
-
 Escherichia coli (S)-1-pyrroline-5-carboxylate + reduced acceptor
-
 ?
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
-
 ?
L-proline + acceptor + H2O acceptors: 2,6-dichlorophenolindophenol, phenazine methosulfate, ferricyanide, menadione, cytochrome c Escherichia coli (S)-1-pyrroline-5-carboxylate + reduced acceptor
-
 ?

Cofactor

Cofactor Comment Organism Structure
FAD
-
 Escherichia coli