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
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General Information
General Information on EC 1.2.1.70 - glutamyl-tRNA reductase
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metabolism
physiological function
additional information
three mechanisms for plant GluTR activity regulation: (i) the end-product feedback inhibition by heme, (ii) repression by a membrane protein FLUORESCENT (FLU), and (iii) formation of complex with a soluble GluTR-binding protein (GBP)
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GluTR is proposed to be the key regulatory enzyme of tetrapyrrole biosynthetic pathway that is tightly controlled at transcriptional and posttranslational levels
metabolism
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GluTR is the first committed enzyme of plant 5-aminolevulinic acid synthesis and 5-aminolevulinic acid synthesis has been shown to be the rate limiting step of tetrapyrrole biosynthesis
metabolism
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GluTR is the first enzyme committed to tetrapyrrole biosynthesis by the C5-pathway
metabolism
glutamyl-tRNA reductase (GluTR) is the key enzyme for heme biosynthesis. The flow of glutamyl-tRNA is diverted from heme biosynthesis towards protein synthesis under oxidative stress conditions. In the C5 pathway, 5-aminolevulinic acid is synthesized from Glu-tRNAGlu in two steps. First, the glutamate moiety of Glu-tRNAGlu is reduced to glutamate semialdehyde (GSA) by glutamyl-tRNA reductase (GluTR), and then GSA is converted to 5-aminolevulinic acid by the glutamate semialdehyde 1-2 aminomutase (GSAM)
metabolism
plants synthesize delta-aminolevulenic acid (ALA), the precursor for all tetrapyrrole molecules, from glutamate via a three-step pathway1 The first step is ligation of glutamate to tRNAGlu catalyzed by glutamyl-tRNA synthetase. Then glutamyl-tRNA reductase (GluTR) reduces the tRNAGlu-bound glutamate to glutamate-1-semialdehyde (GSA) in an NADPH-dependent manner. GSA is subsequently isomerized to ALA by a vitamin B6-dependent enzyme, glutamate-1-semialdehyde aminomutase (GSAM). 5-Aminolevulinic acid synthesis is the key regulatory point for the entire tetrapyrrole biosynthetic pathway, and particularly GluTR is subjected to a tight control at the post-translational level
metabolism
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the enzyme is the first committed enzyme in tetrapyrrole biosynthesis reducing the activated tRNA-bound glutamate to glutamate-1-semialdehyde, which is subsequently transaminated by glutamate-1-semialdehyde aminotransferase (GSAT) to form 5-aminolevulinic acid. 5-Aminolevulinic acid formation is the rate limiting step of tetrapyrrole biosynthesis and temporally controlled by GluTR expression
metabolism
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the enzyme is the first unique enzyme in the tetrapyrrole biosynhetic pathway in plants
metabolism
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enzyme abundance as a critical regulator of Staphylococcus aureus heme synthesis. HemX controls enzyme abundance in heme-proficient cells to regulate heme synthesis
metabolism
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the enzyme catalyzes the rate-limiting step of 5-aminolevulinic acid synthesis
metabolism
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enzyme abundance as a critical regulator of Staphylococcus aureus heme synthesis. HemX controls enzyme abundance in heme-proficient cells to regulate heme synthesis
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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
physiological function
GluTR-catalyzed reaction is the rate-limiting step of tetrapyrrole biosynthesis, and GluTR is the target of multiple posttranslational regulations, such as heme feedback inhibition, for the tetrapyrrole biosynthetic pathway. GluBP stimulates GluTR activity and regulates glutamate 1-semialdehyde release
physiological function
in chemolithoautotrophic bacteria like Acidithiobacillus ferrooxidans that use the C5 pathway to synthesize tetrapyrroles, high demand for Glu-tRNAGlu for heme biosynthesis is expected, due to the high cytochrome content required for respiration using poor electron donors, such as ferrous ions. This bacterium has a complex system of glutamyl-tRNA formation composed of two non-discriminating glutamyl-tRNA synthetases (GluRS1 and GluRS2) and up to four tRNAGlu isoacceptors, with GluRS1 serving as the main enzyme for Glu-tRNAGlu formation. Three out of four glutamyl-tRNAs can act as donors for both heme and protein synthesis, while the fourth is not a substrate of GluTR and likely acts exclusively in protein synthesis
physiological function
protein FLU negatively regulates glutamyl-tRNA reductase (GluTR) during chlorophyll biosynthesis. It directly interacts through its TPR domain with glutamyl-tRNA reductase (GluTR), the rate-limiting enzyme in the formation of 5-aminolevulinic acid. The formation of the FLU-GluTR complex prevents glutamyl-tRNA, the GluTR substrate, from binding with this enzyme
physiological function
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the enzyme is required for the biosynthesis of 5-aminolevulinic acid
physiological function
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the enzyme is required for the biosynthesis of 5-aminolevulinic acid. Formation of 5-aminolevulinic acid at the beginning of the pathway is the rate limiting step of tetrapyrrole biosynthesis and target of multiple timely and spatially organized control mechanisms. Regulation of the pathway, detailed overview. Spatial organization of 5-aminolevulinic acid formation in chloroplasts. The majority of a glutamyl-tRNA reductase (GluTR) and glutamate-1 semialdehyde aminotransferase (GSAT) protein complex is located in the stroma and forms 5-aminolevulinic acid starting with glutamyltRNAGlu, while a minor part of the active protein complex is attached to the thylakoid membrane via a GluTR-binding protein (GluTRBP). At night the FLU protein, another glutamyl-tRNA reductase binding protein, binds the soluble glutamyl-tRNA reductase fraction to the thylakoid membrane and thereby inactivates 5-aminolevulinic acid formation. Only the GluTRBP bound fraction of GluTR can continue to synthesize 5-aminolevulinic acid during dark periods, preventing both a lack of heme during darkness and excessive accumulation of phototoxic intermediates of chlorophyll biosynthesis. The FLU protein i a negative regulator of 5-aminolevulinic acid biosynthesis
physiological function
the GluTR-catalyzed glutamyl-tRNAGlu reduction by NADPH is a key regulatory point of the tetrapyrrole biosynthetic pathway. Plants synthesize delta-aminolevulenic acid (ALA), the precursor for all tetrapyrrole molecules, from glutamate via a three-step pathway. The first step is ligation of glutamate to tRNAGlu catalyzed by glutamyl-tRNA synthetase. Then glutamyl-tRNA reductase (GluTR) reduces the tRNAGlu-bound glutamate to glutamate-1-semialdehyde (GSA) in an NADPH-dependent manner. GSA is subsequently isomerized to 5-aminolevulinic acid by a vitamin B6-dependent enzyme, glutamate-1-semialdehyde aminomutase (GSAM). 5-Aminolevulinic acid synthesis is the key regulatory point for the entire tetrapyrrole biosynthetic pathway, and particularly GluTR is subjected to a tight control at the post-translational level. Regulation of the enzyme within the pathway, detailed overview. Glutamate-1-semialdehyde aminomutase (GSAM) is proposed to form complex with GluTR to enable GSA channeling from GluTR to GSAM in bacteria, but not in plants
physiological function
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the enzyme is required for the biosynthesis of 5-aminolevulinic acid
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