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Literature summary for 1.2.1.70 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)

Cloned (Comment) Organism
overexpression in Escherichia coli Methanopyrus kandleri

Protein Variants

Protein Variants Comment Organism
C48S complete loss of activity Methanopyrus kandleri

Inhibitors

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

Metals/Ions

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Methanopyrus kandleri
-
-
-

Substrates and Products (Substrate)

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

Temperature Optimum [°C]

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

Cofactor

Cofactor Comment Organism Structure
NADPH
-
Methanopyrus kandleri