BRENDA - Enzyme Database

Purification of glutamyl-tRNA reductase from Synechocystis sp. PCC 6803

Rieble, S.; Beale, S.I.; J. Biol. Chem. 266, 9740-9745 (1991)

Data extracted from this reference:

Inhibitors
EC Number
Inhibitors
Commentary
Organism
Structure
1.2.1.70
heme
0.05 mM, 50% inhibition
Synechocystis sp.
Molecular Weight [Da]
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
1.2.1.70
39000
-
x * 39000, SDS-PAGE
Synechocystis sp.
1.2.1.70
350000
-
glycerol density gradient centrifugation
Synechocystis sp.
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
1.2.1.70
Synechocystis sp.
-
PCC 6803
-
Purification (Commentary)
EC Number
Commentary
Organism
1.2.1.70
-
Synechocystis sp.
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 + NADH + H+
much higher activity occurs with NADPH than with NADH
655964
Synechocystis sp.
L-glutamate 1-semialdehyde + NAD+ + tRNAGlu
-
-
-
?
1.2.1.70
L-glutamyl-tRNAGlu + NADPH + H+
-
655964
Synechocystis sp.
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
-
-
?
Subunits
EC Number
Subunits
Commentary
Organism
1.2.1.70
?
x * 39000, SDS-PAGE
Synechocystis sp.
Turnover Number [1/s]
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1.2.1.70
additional information
-
additional information
-
Synechocystis sp.
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
1.2.1.70
NADH
much higher activity occurs with NADPH than with NADH
Synechocystis sp.
1.2.1.70
NADPH
half-maximal rate at 0.005 mM, saturation is not reached even at 10 mM NADH
Synechocystis sp.
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
1.2.1.70
NADH
much higher activity occurs with NADPH than with NADH
Synechocystis sp.
1.2.1.70
NADPH
half-maximal rate at 0.005 mM, saturation is not reached even at 10 mM NADH
Synechocystis sp.
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
1.2.1.70
heme
0.05 mM, 50% inhibition
Synechocystis sp.
Molecular Weight [Da] (protein specific)
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
1.2.1.70
39000
-
x * 39000, SDS-PAGE
Synechocystis sp.
1.2.1.70
350000
-
glycerol density gradient centrifugation
Synechocystis sp.
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
1.2.1.70
-
Synechocystis sp.
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 + NADH + H+
much higher activity occurs with NADPH than with NADH
655964
Synechocystis sp.
L-glutamate 1-semialdehyde + NAD+ + tRNAGlu
-
-
-
?
1.2.1.70
L-glutamyl-tRNAGlu + NADPH + H+
-
655964
Synechocystis sp.
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
-
-
?
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
1.2.1.70
?
x * 39000, SDS-PAGE
Synechocystis sp.
Turnover Number [1/s] (protein specific)
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1.2.1.70
additional information
-
additional information
-
Synechocystis sp.