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Literature summary for 1.2.1.70 extracted from

  • Zhang, J.; Weng, H.; Ding, W.; Kang, Z.
    N-terminal engineering of glutamyl-tRNA reductase with positive charge arginine to increase 5-aminolevulinic acid biosynthesis (2017), Bioengineered, 8, 424-427 .
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
synthesis the recombinant engineered GluTR variant R1 can be used for improvement of the C5 pathway to enhance 5-aminolevulinic acid and other products Escherichia coli

Protein Variants

Protein Variants Comment Organism
additional information N-terminal engineering of glutamyl-tRNA reductase with positive charge arginine to increase 5-aminolevulinic acid biosynthesis. Insertion of lysine or arginine residues (especially one arginine residue) behind Thr2 of GluTR significantly increased the stability of GluTR. By co-expression of this GluTR variant R1 and the glutamate-1-semialdehyde aminotransferase, 5-aminolevulinic acid production is improved 1.76fold to 1220 mg/L Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
heme feedback inhibition Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu Escherichia coli
-
L-glutamyl-tRNAGlu + NADPH + H+
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
Escherichia coli L-glutamyl-tRNAGlu + NADPH + H+
-
?

Synonyms

Synonyms Comment Organism
GluTR
-
Escherichia coli

Cofactor

Cofactor Comment Organism Structure
NADP+
-
Escherichia coli
NADPH
-
Escherichia coli

General Information

General Information Comment Organism
physiological function glutamyl-tRNA reductase (GluTR) is the first key enzyme of C5 pathway, it is feedback regulated by heme, and its N-terminus plays a critical role on its stability control Escherichia coli