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Literature summary for 1.5.5.2 extracted from

  • Brown, E.D.; Wood, J.M.
    Redesigned purification yields a fully functional PutA protein dimer from Escherichia coli (1992), J. Biol. Chem., 267, 13086-13092.
    View publication on PubMed

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
137000
-
2 * 137000, bifunctional enzyme: proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase, SDS-PAGE Escherichia coli
293000
-
gel filtration, bifunctional enzyme: proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase, sucrose density centrifugation Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-proline + acceptor Escherichia coli the bifunctional enzyme catalyzes the oxidation of proline in two steps. (S)-1-Pyrroline-5-carboxylate, the product of the first reaction is in spontaneous equilibrium with its tautomer L-glutamate gamma-semialdehyde: (1) L-proline + acceptor = (S)-1-pyrroline-5-carboxylate + reduced acceptor, (2) L-glutamate 5-semialdehyde + NAD+ + H2O = L-glutamate + NADH + H+ (S)-1-pyrroline-5-carboxylate + reduced acceptor
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli P09546
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.24
-
25°C, pH 7.5, proline oxidase activity of the bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-proline + acceptor the bifunctional enzyme catalyzes the oxidation of proline in two steps. (S)-1-Pyrroline-5-carboxylate, the product of the first reaction is in spontaneous equilibrium with its tautomer L-glutamate gamma-semialdehyde: (1) L-proline + acceptor = (S)-1-pyrroline-5-carboxylate + reduced acceptor, (2) L-glutamate 5-semialdehyde + NAD+ + H2O = L-glutamate + NADH + H+ Escherichia coli (S)-1-pyrroline-5-carboxylate + reduced acceptor
-
?

Subunits

Subunits Comment Organism
dimer 2 * 137000, bifunctional enzyme: proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase, SDS-PAGE Escherichia coli

Synonyms

Synonyms Comment Organism
proline/P5C dehydrogenase bifunctional enzyme: proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase Escherichia coli
PutA bifunctional enzyme: proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Escherichia coli

Cofactor

Cofactor Comment Organism Structure
FAD flavin cofactor, 1.2fold stimulated by exogenous FAD Escherichia coli