1.2.1.70: glutamyl-tRNA reductase
This is an abbreviated version!
For detailed information about glutamyl-tRNA reductase, go to the full flat file.
Word Map on EC 1.2.1.70
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1.2.1.70
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tetrapyrrole
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chlorophyl
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ala
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5-aminolevulinic
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heme
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glutamate-1-semialdehyde
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protochlorophyllide
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delta-aminolevulinic
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1-semialdehyde
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de-etiolation
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chelatase
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mg-protoporphyrin
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glu-trna
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trna-dependent
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kandleri
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pchlide
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gun4
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glu-trnaglu
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trna-bound
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2,1-aminomutase
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biotechnology
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synthesis
- 1.2.1.70
- tetrapyrrole
-
chlorophyl
- ala
-
5-aminolevulinic
- heme
- glutamate-1-semialdehyde
- protochlorophyllide
-
delta-aminolevulinic
- 1-semialdehyde
-
de-etiolation
- chelatase
- mg-protoporphyrin
- glu-trna
-
trna-dependent
- kandleri
-
pchlide
- gun4
- glu-trnaglu
-
trna-bound
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2,1-aminomutase
- biotechnology
- synthesis
Reaction
Synonyms
AtHEMA1, EC 2.7.2.13, GluRS, glutamate tRNA reductase, glutamate-specific tRNA reductase, glutamyl transfer RNA reductase, glutamyl-tRNA reductase, GluTR, GluTR1, GTR, GtrR, hemA, HEMA1, HEMA2, reductase, glutamyl-transfer ribonucleate, ZjGluTR
ECTree
1.2.1.70 glutamyl-tRNA reductaseAdvanced search results
results (
results (Engineering
Engineering on EC 1.2.1.70 - glutamyl-tRNA reductase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C170S
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mutant enzyme with esterase activity 95% of the wild-type activity and reductase activity with 90% of the wild-type activity
C50S
C74S
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mutant enzyme with esterase activity 110% of the wild-type activity and reductase activity with 120% of the wild-type activity
G191D
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mutant enzyme reveals esterase, 105% of the wild-type activity, but no reductase activity
Q116L
lacks reductase activity whereas 30% esterase activity is retained
C393S
95% of the GluTR reductase activity compared to wild-type enzyme, 100% of the GluTR esterase activity compared to wild-type enzyme
C48S
C6S
130% of the GluTR reductase activity compared to wild-type enzyme, 120% of the GluTR esterase activity compared to wild-type enzyme
C90S
85% of the GluTR reductase activity compared to wild-type enzyme, 105% of the GluTR esterase activity compared to wild-type enzyme
H84A
no GluTR reductase activity, 5% of the GluTR esterase activity compared to wild-type enzyme
H84N
30% of the GluTR reductase activity compared to wild-type enzyme, 15% of the GluTR esterase activity compared to wild-type enzyme
additional information
C48S
90% of the GluTR reductase activity compared to wild-type enzyme, 95% of the GluTR esterase activity compared to wild-type enzyme
additional information
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insertional knockout mutants show heme contents of the roots about half of that of the wild-type and reduction of the ozone-induced increase in heme content
additional information
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as excessive accumulation of GluTR in transgenic plants does not correlate with increased 5-aminolevulinic acid formation, it is hypothesized that 5-aminolevulinic acid synthesis is additionally limited by other effectors that balance the allocation of 5-aminolevulinic acid with the activity of enzymes of chlorophyll and heme biosynthesis
additional information
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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
additional information
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a 30 amino acid N-terminal deletion has no detrimental effect on the catalytic activity of the enzyme
additional information
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the knockout mutant is absolutely dependent on supplementation with 5-aminolevulinic acid
additional information
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the knockout mutant is absolutely dependent on supplementation with 5-aminolevulinic acid
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additional information
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the knockout mutant is absolutely dependent on supplementation with 5-aminolevulinic acid
