BRENDA - Enzyme Database

Structure and function of glutamyl-tRNA reductase involved in 5-aminolaevulinic acid formation

Moser, J.; Schubert, W.D.; Heinz, D.W.; Jahn, D.; Biochem. Soc. Trans. 30, 579-584 (2002)

Data extracted from this reference:

Cloned(Commentary)
EC Number
Commentary
Organism
1.2.1.70
overexpression in Escherichia coli
Methanopyrus kandleri
Engineering
EC Number
Amino acid exchange
Commentary
Organism
1.2.1.70
C48S
complete loss of activity
Methanopyrus kandleri
Inhibitors
EC Number
Inhibitors
Commentary
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
Commentary
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
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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
Primary Accession No. (UniProt)
Commentary
Textmining
1.2.1.70
Methanopyrus kandleri
-
-
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.2.1.70
L-glutamyl-tRNAGlu + NADPH + H+
-
654558
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
654558
Methanopyrus kandleri
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
-
-
?
Temperature Optimum [°C]
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
1.2.1.70
90
-
-
Methanopyrus kandleri
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
1.2.1.70
NADPH
-
Methanopyrus kandleri
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
1.2.1.70
overexpression in Escherichia coli
Methanopyrus kandleri
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
1.2.1.70
NADPH
-
Methanopyrus kandleri
Engineering (protein specific)
EC Number
Amino acid exchange
Commentary
Organism
1.2.1.70
C48S
complete loss of activity
Methanopyrus kandleri
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
1.2.1.70
5,5'-dithiobis-(2-nitrobenzoic acid)
-
Methanopyrus kandleri
1.2.1.70
glutamycin
competitive
Methanopyrus kandleri
Metals/Ions (protein specific)
EC Number
Metals/Ions
Commentary
Organism
Structure
1.2.1.70
additional information
no significant stimulation by high salt concentrations
Methanopyrus kandleri
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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
-
-
?
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.2.1.70
L-glutamyl-tRNAGlu + NADPH + H+
-
654558
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
654558
Methanopyrus kandleri
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
-
-
?
Temperature Optimum [°C] (protein specific)
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
1.2.1.70
90
-
-
Methanopyrus kandleri