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 | 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 | Comment | Organism | Structure |
---|---|---|---|
heme | feedback inhibition | Escherichia coli |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu | - |
Escherichia coli | L-glutamyl-tRNAGlu + NADPH + H+ | - |
? |
Synonyms | Comment | Organism |
---|---|---|
GluTR | - |
Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADP+ | - |
Escherichia coli | |
NADPH | - |
Escherichia coli |
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 |