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Literature summary for 2.7.2.8 extracted from

  • McKay, G.; Shargool, P.D.
    Purification and characterization of N-acetylglutamate 5-phosphotransferase from pea (Pisum sativum) cotyledons (1981), Biochem. J., 195, 71-81.
    View publication on PubMedView publication on EuropePMC
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KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.7
-
 ATP pH 7.5, 30°C Pisum sativum
1.9
-
 N-acetyl-L-glutamate two Km-values: 1.9 and 6.2, pH 7.5, 30°C Pisum sativum
6.2
-
 N-acetyl-L-glutamate 2 Km-values: 1.9 and 6.2, pH 7.5, 30°C Pisum sativum

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
43000
-
 dimer or tetramer, 1 or 2 * 43000 + 1 or 2 * 53000, SDS-PAGE Pisum sativum
53000
-
 dimer or tetramer, 1 or 2 * 43000 + 1 or 2 * 53000, SDS-PAGE Pisum sativum
93000
-
 gel filtration Pisum sativum
190000
-
 gel filtration in presence of N-acetylglutamate Pisum sativum

Organism

Organism UniProt Comment Textmining
Pisum sativum
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Pisum sativum

Reaction

Reaction Comment Organism Reaction ID
ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate random bi-bi mechanism Pisum sativum
a

Source Tissue

Source Tissue Comment Organism Textmining
cotyledon
-
 Pisum sativum
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + N-acetyl-L-glutamate
-
 Pisum sativum ADP + N-acetyl-L-glutamyl 5-phosphate
-
 ?

Subunits

Subunits Comment Organism
? dimer or tetramer, 1 or 2 * 43000 + 1 or 2 * 53000, SDS-PAGE Pisum sativum