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Literature summary for 2.7.2.11 extracted from

  • Hayzer, D.J.; Moses, V.
    The enzymes of proline biosynthesis in Escherichia coli. Their molecular weights and the problem of enzyme aggregation (1978), Biochem. J., 173, 219-228.
    View publication on PubMedView publication on EuropePMC

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
two glutamyl kinases of MW 125000 Da and of 38000 Da are detected by gel filtration on Sephadex G-150, a single glutamyl kinase of 250000 Da is detected by Bio-gel A1.5M chromatpgraphy Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-glutamate Escherichia coli enzyme is involved in biosynthesis of proline ADP + L-glutamate 5-phosphate
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-glutamate
-
Escherichia coli ADP + L-glutamate 5-phosphate
-
?
ATP + L-glutamate enzyme is involved in biosynthesis of proline Escherichia coli ADP + L-glutamate 5-phosphate
-
?