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Literature summary extracted from

  • Moser, J.; Schubert, W.D.; Heinz, D.W.; Jahn, D.
    Structure and function of glutamyl-tRNA reductase involved in 5-aminolaevulinic acid formation (2002), Biochem. Soc. Trans., 30, 579-584.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.2.1.70 overexpression in Escherichia coli Methanopyrus kandleri

Protein Variants

EC Number Protein Variants Comment Organism
1.2.1.70 C48S complete loss of activity Methanopyrus kandleri

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.2.1.70 5,5'-dithiobis-(2-nitrobenzoic acid)
-
 Methanopyrus kandleri
1.2.1.70 glutamycin competitive Methanopyrus kandleri

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.2.1.70 additional information no significant stimulation by high salt concentrations Methanopyrus kandleri

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.2.1.70 L-glutamyl-tRNAGlu + NADPH + H+ Methanopyrus kandleri the enzyme is involved in the C5 pathway L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.70 Methanopyrus kandleri
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.70 L-glutamyl-tRNAGlu + NADPH + H+
-
 Methanopyrus kandleri L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
 ?
1.2.1.70 L-glutamyl-tRNAGlu + NADPH + H+ the enzyme is involved in the C5 pathway Methanopyrus kandleri L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.2.1.70 90
-
-
 Methanopyrus kandleri

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.70 NADPH
-
 Methanopyrus kandleri