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Literature summary 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]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.2.1.88 137000
-
 2 * 137000, bifunctional enzyme: proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase, SDS-PAGE Escherichia coli
1.2.1.88 293000
-
 gel filtration, bifunctional enzyme: proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase, sucrose density centrifugation Escherichia coli
1.5.5.2 137000
-
 2 * 137000, bifunctional enzyme: proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase, SDS-PAGE Escherichia coli
1.5.5.2 293000
-
 gel filtration, bifunctional enzyme: proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase, sucrose density centrifugation Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.2.1.88 L-glutamate 5-semialdehyde + NAD+ + H2O 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+ L-glutamate + NADH + H+
-
 ?
1.5.5.2 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

EC Number Organism UniProt Comment Textmining
1.2.1.88 Escherichia coli P09546
-
-
1.5.5.2 Escherichia coli P09546
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.1.88
-
 Escherichia coli
1.5.5.2
-
 Escherichia coli

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.2.1.88 0.13
-
 25°C, pH 7.5, pH 7.5, L-glutamate gamma-semialdehyde dehydrogenase activity proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase Escherichia coli
1.5.5.2 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)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.88 L-glutamate 5-semialdehyde + NAD+ + H2O 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 L-glutamate + NADH + H+
-
 ?
1.5.5.2 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

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

Synonyms

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.2.1.88 25
-
 assay at Escherichia coli
1.5.5.2 25
-
 assay at Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.2.1.88 7.5
-
 assay at Escherichia coli
1.5.5.2 7.5
-
 assay at Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.88 FAD flavin cofactor, 1.2fold stimulated by exogenous FAD Escherichia coli
1.5.5.2 FAD flavin cofactor, 1.2fold stimulated by exogenous FAD Escherichia coli