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Literature summary for 1.2.1.41 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
Search for more literature for 1.2.1.41

Inhibitors

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

KM Value [mM]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-5-glutamyl phosphate + NADPH second enzyme in pathway of proline biosynthesis Escherichia coli ?
-
 ?
L-glutamate 5-semialdehyde + phosphate + NADP+ divalent anions can substitute for phosphate Escherichia coli L-5-glutamyl phosphate + NADPH
-
 r
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
L-glutamate 5-semialdehyde + phosphate + NADP+
-
 Escherichia coli gamma-glutamyl phosphate + NADPH + H+
-
 r

Cofactor

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

Ki Value [mM]

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