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Literature summary 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

EC Number Metals/Ions Comment Organism Structure
2.7.2.11 Mg2+ required Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.2.11 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)

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

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.41 Escherichia coli
-
 various strains
-
2.7.2.11 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+
-
 Escherichia coli L-5-glutamyl phosphate + NADPH
-
 r
2.7.2.11 ATP + L-glutamate
-
 Escherichia coli ADP + L-glutamate 5-phosphate
-
 ?
2.7.2.11 ATP + L-glutamate enzyme is involved in biosynthesis of proline Escherichia coli ADP + L-glutamate 5-phosphate
-
 ?

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.41 NADPH
-
 Escherichia coli