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Literature summary extracted from

  • Baich, A.
    The biosynthesis of proline in Escherichia coli: phosphate-dependent glutamate-semialdehyde dehydrogenase (NADP), the second enzyme in the pathway (1971), Biochim. Biophys. Acta, 244, 129-134.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2.1.41 0.18
-
 NADP+
-
 Escherichia coli
1.2.1.41 2.2
-
 glutamic gamma-semialdehyde
-
 Escherichia coli
1.2.1.41 11
-
 phosphate
-
 Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.41 Escherichia coli
-
-
-
1.2.1.41 Escherichia coli 55-I
-
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.2.1.41 0.0072
-
 crude extract Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.41 L-glutamate 5-semialdehyde + phosphate + NADP+ arsenate can replace phosphate Escherichia coli L-5-glutamyl phosphate + NADPH
-
 r
1.2.1.41 L-glutamate 5-semialdehyde + phosphate + NADP+ arsenate can replace phosphate Escherichia coli 55-I L-5-glutamyl phosphate + NADPH
-
 r

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.2.1.41 7
-
-
 Escherichia coli

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.2.1.41 6.3 7.8 about 30% of activity maximum at pH 7.3, about 20% of activity maximum at pH 7.8 Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.41 NADPH
-
 Escherichia coli