Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Hayzer, D.J.; Leisinger, T.
    Proline biosynthesis in Escherichia coli. Kinetic and mechanistic properties of glutamate semialdehyde dehydrogenase (1983), Biochim. Biophys. Acta, 742, 391-398.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.2.1.41 3-(Phosphonoacetylamido)-L-alanine competitive with respect to DL-pyrroline-5-carboxylic acid, non-competitive with respect to NADP+ and phosphate Escherichia coli
1.2.1.41 NADPH competitive with respect to all three substrates Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2.1.41 additional information
-
 additional information Km with various phosphate substitutes Escherichia coli
1.2.1.41 0.05
-
 NADP+
-
 Escherichia coli
1.2.1.41 0.35
-
 phosphate
-
 Escherichia coli
1.2.1.41 2.5
-
 L-glutamate 5-semialdehyde
-
 Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.2.1.41 L-5-glutamyl phosphate + NADPH Escherichia coli second enzyme in pathway of proline biosynthesis ?
-
 ?

Organism

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.41 L-5-glutamyl phosphate + NADPH second enzyme in pathway of proline biosynthesis Escherichia coli ?
-
 ?
1.2.1.41 L-glutamate 5-semialdehyde + phosphate + NADP+ divalent anions can substitute for phosphate Escherichia coli L-5-glutamyl phosphate + NADPH
-
 r
1.2.1.41 L-glutamate 5-semialdehyde + phosphate + NADP+ L-glutamate 5-semialdehyde is in equilibrium with delta'-pyrroline-5-carboxylate Escherichia coli L-5-glutamyl phosphate + NADPH
-
 r
1.2.1.41 L-glutamate 5-semialdehyde + phosphate + NADP+
-
 Escherichia coli gamma-glutamyl phosphate + NADPH + H+
-
 r

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.41 NADH less active than NADPH Escherichia coli
1.2.1.41 NADPH
-
 Escherichia coli

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.2.1.41 0.002
-
 NADPH
-
 Escherichia coli
1.2.1.41 22.5
-
 3-(Phosphonoacetylamido)-L-alanine
-
 Escherichia coli