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
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chlorophyl
- ala
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5-aminolevulinic
- heme
- glutamate-1-semialdehyde
- protochlorophyllide
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delta-aminolevulinic
- 1-semialdehyde
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de-etiolation
- chelatase
- mg-protoporphyrin
- glu-trna
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trna-dependent
- kandleri
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pchlide
- gun4
- glu-trnaglu
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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
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Substrates Products
Substrates Products on EC 1.2.1.70 - glutamyl-tRNA reductase
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REACTION DIAGRAM
L-glutamyl-tRNAGlu + NADPH + H+
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L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
L-glutamyl-tRNAGlu + NADPH + H+
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L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
L-glutamyl-tRNAGlu + NADPH + H+
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L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
L-glutamyl-tRNAGlu + NADPH + H+
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L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
L-glutamyl-tRNAGlu + NADPH + H+
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L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
L-glutamyl-tRNAGlu + NADPH + H+
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L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
L-glutamyl-tRNAGlu + NADPH + H+
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L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
L-glutamyl-tRNAGlu + NADPH + H+
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L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
L-glutamyl-tRNAGlu + NADPH + H+
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L-glutamate 1-semialdehyde + NAD+ + tRNAGlu
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Acidithiobacillus ferrooxidans contains three tRNAGlu where only 2 are a substrate for glutamyl-tRNA reductase
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L-glutamyl-tRNAGlu + NADH + H+
L-glutamate 1-semialdehyde + NAD+ + tRNAGlu
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L-glutamyl-tRNAGlu + NADH + H+
L-glutamate 1-semialdehyde + NAD+ + tRNAGlu
the enzyme also exhibits an esterase activity
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L-glutamyl-tRNAGlu + NADH + H+
L-glutamate 1-semialdehyde + NAD+ + tRNAGlu
the enzyme also exhibits an esterase activity
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L-glutamyl-tRNAGlu + NADH + H+
L-glutamate 1-semialdehyde + NAD+ + tRNAGlu
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L-glutamyl-tRNAGlu + NADH + H+
L-glutamate 1-semialdehyde + NAD+ + tRNAGlu
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much higher activity occurs with NADPH than with NADH
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L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
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L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
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L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
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L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
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L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
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the enzyme catalyzes the initial step of tetrapyrrole biosynthesis in plants and prokaryotes
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L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
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L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
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complex formation between glutamyl-tRNA synthetase and glutamyl-tRNA reductase during the tRNA-dependent synthesis of 5-aminolevulinic acid
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L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
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the enzyme is involved in delta-aminolevulinic acid formation during chlorophyll biosynthesis
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L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
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L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
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glutamyl-tRNA reductase is the solely light-regulated enzyme of 5-aminolevulinic acid-synthesis system, and the elevation of glutamate by light may contribute to the stimulation of 5-aminolevulinic acid synthesis
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L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
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stimulation of the synthesis of 5-aminolevulinic acid by benzyladenine is caused by increased levels of glutamyl-tRNA reductase and that the reductase is the regulatory and rate-determining enzyme in the 5-aminolevulinic-synthesis system except in untreated etioplasts, in which the level of glutamyl-tRNA may be rate-determining factor
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L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
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L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
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L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
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the enzyme catalyzes the initial step of tetrapyrrole biosynthesis
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L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
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the enzyme catalyzes the initial step of tetrapyrrole biosynthesis in plants and prokaryotes
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L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
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in presence of NADPH, the end product, glutamate-1-semialdehyde is formed. In the absence of NADPH, Escherichia coli GluTR exhibits substrate esterase activity
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L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
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the enzyme interacts directly with the amino-acylated acceptor stem and the D-stem, whereas the anticodon domain serves as a major recognition element of aminoacyl tRNA synthetases
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L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
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L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
the enzyme catalyzes the initial step of tetrapyrrole biosynthesis
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L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
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the enzyme directs glutamate to chlorophyll biosynthesis
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L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
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A7-U66, U29-A41, A53-U61 and U72 are expected to be required for recognition by the barley chloroplast glutamyl-tRNA(Glu) reductase
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L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
the fusion protein with glutathione S-transferase uses tRNAGlu from Hordeum vulgare chloroplast preferentially to Escherichia coli tRNAGlu
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L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
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L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
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L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
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the enzyme catalyzes the initial step of tetrapyrrole biosynthesis
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L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
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the enzyme is involved in the C5 pathway
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L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
in absence of NADPH, an esterase activity of GluTR hydrolyzes the highly reactive thioester of tRNAGlu to release glutamate
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L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
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L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
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L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
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L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
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formation of 5-aminolevulinic acid in 5-week-old AtHEMA1-expressing tobacco plants grown in continuous light could be shown to be significantly altered but does not result in significant changes of the amounts of tetrapyrrole intermediates, chlorophyll or heme
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additional information
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identification of a GluTR binding protein, GluTRBP, that is localized in chloroplasts and is part of a 300000 Da protein complex in the thylakoid membrane, protein does not modulate activity of ALA synthesis, but the knockout of GluTRBP is lethal in Arabidopsis thaliana, whereas mutants expressing reduced levels of GluTRBP contain less heme
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additional information
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up to 7fold increased GluTR content in adult transgenic Arabidopsis plants two days after ethanol application but there is no significant increase in 5-aminolevulinic acid synthesis rates in comparison to ethanol-treated wild-type plants
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additional information
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GluTR employs hydride transfer from NADPH to the thioester-bound glutamate to produce glutamate-1-semialdehyde. The close contact between the nicotinamide ring of NADPH and the nucleophile Cys144 allows the transfer of hydride from NADPH to the thioester-bound glutamate. Tunnel formation in the GluTR-GluBP complex for release of product L-glutamate 1-semialdehyde
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additional information
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GluTR employs hydride transfer from NADPH to the thioester-bound glutamate to produce glutamate-1-semialdehyde. The close contact between the nicotinamide ring of NADPH and the nucleophile Cys144 allows the transfer of hydride from NADPH to the thioester-bound glutamate. Tunnel formation in the GluTR-GluBP complex for release of product L-glutamate 1-semialdehyde
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additional information
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binding of heme to the GluTR-binding protein (GBP) inhibits interaction of GBP with the N-terminal regulatory domain of isoform GluTR1, thus making it accessible to the Clp protease
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additional information
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hemA with Lys insertion overexpressing Escherichia coli strain shows an increased 5-aminolevulinic acid accumulation indicating that the reduction of glutamyl-tRNA to glutamate-1-semialdehyde is a rate-limiting step
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