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Literature summary for 1.2.1.70 extracted from

  • Rieble, S.; Beale, S.I.
    Purification of glutamyl-tRNA reductase from Synechocystis sp. PCC 6803 (1991), J. Biol. Chem., 266, 9740-9745.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
heme 0.05 mM, 50% inhibition Synechocystis sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
39000
-
x * 39000, SDS-PAGE Synechocystis sp.
350000
-
glycerol density gradient centrifugation Synechocystis sp.

Organism

Organism UniProt Comment Textmining
Synechocystis sp.
-
PCC 6803
-

Purification (Commentary)

Purification (Comment) Organism
-
Synechocystis sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-glutamyl-tRNAGlu + NADH + H+ much higher activity occurs with NADPH than with NADH Synechocystis sp. L-glutamate 1-semialdehyde + NAD+ + tRNAGlu
-
?
L-glutamyl-tRNAGlu + NADPH + H+
-
Synechocystis sp. L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
?

Subunits

Subunits Comment Organism
? x * 39000, SDS-PAGE Synechocystis sp.

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
additional information
-
Synechocystis sp.

Cofactor

Cofactor Comment Organism Structure
NADH much higher activity occurs with NADPH than with NADH Synechocystis sp.
NADPH half-maximal rate at 0.005 mM, saturation is not reached even at 10 mM NADH Synechocystis sp.