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L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
L-glutamyl-tRNAGlu + NADPH + H+
L-glutaminyl-tRNAGlu + NADPH + H+
? + NADP+ + tRNAGlu
Substrates: -
Products: -
?
L-glutamyl-tRNAGlu + NADH + H+
L-glutamate 1-semialdehyde + NAD+ + tRNAGlu
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
additional information
?
-
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
L-glutamyl-tRNAGlu + NADPH + H+
-
Substrates: -
Products: -
?
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
L-glutamyl-tRNAGlu + NADPH + H+
Substrates: -
Products: -
?
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
L-glutamyl-tRNAGlu + NADPH + H+
-
Substrates: -
Products: -
?
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
L-glutamyl-tRNAGlu + NADPH + H+
-
Substrates: -
Products: -
?
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
L-glutamyl-tRNAGlu + NADPH + H+
-
Substrates: -
Products: -
?
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
L-glutamyl-tRNAGlu + NADPH + H+
-
Substrates: -
Products: -
?
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
L-glutamyl-tRNAGlu + NADPH + H+
-
Substrates: -
Products: -
?
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
L-glutamyl-tRNAGlu + NADPH + H+
-
Substrates: -
Products: -
?
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
L-glutamyl-tRNAGlu + NADPH + H+
-
Substrates: -
Products: -
?
L-glutamyl-tRNAGlu + NADH + H+
L-glutamate 1-semialdehyde + NAD+ + tRNAGlu
-
Substrates: Acidithiobacillus ferrooxidans contains three tRNAGlu where only 2 are a substrate for glutamyl-tRNA reductase
Products: -
?
L-glutamyl-tRNAGlu + NADH + H+
L-glutamate 1-semialdehyde + NAD+ + tRNAGlu
-
Substrates: -
Products: -
?
L-glutamyl-tRNAGlu + NADH + H+
L-glutamate 1-semialdehyde + NAD+ + tRNAGlu
Substrates: the enzyme also exhibits an esterase activity
Products: -
?
L-glutamyl-tRNAGlu + NADH + H+
L-glutamate 1-semialdehyde + NAD+ + tRNAGlu
Substrates: the enzyme also exhibits an esterase activity
Products: -
?
L-glutamyl-tRNAGlu + NADH + H+
L-glutamate 1-semialdehyde + NAD+ + tRNAGlu
Substrates: -
Products: -
?
L-glutamyl-tRNAGlu + NADH + H+
L-glutamate 1-semialdehyde + NAD+ + tRNAGlu
-
Substrates: much higher activity occurs with NADPH than with NADH
Products: -
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
Substrates: -
Products: -
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
Substrates: -
Products: -
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
Substrates: -
Products: -
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
Substrates: -
Products: -
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
Substrates: the enzyme catalyzes the initial step of tetrapyrrole biosynthesis in plants and prokaryotes
Products: -
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
Substrates: -
Products: -
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
Substrates: complex formation between glutamyl-tRNA synthetase and glutamyl-tRNA reductase during the tRNA-dependent synthesis of 5-aminolevulinic acid
Products: -
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
Substrates: the enzyme is involved in delta-aminolevulinic acid formation during chlorophyll biosynthesis
Products: -
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
Substrates: -
Products: -
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
Substrates: 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
Products: -
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
Substrates: 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
Products: -
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
Substrates: -
Products: -
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
Substrates: -
Products: -
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
Substrates: the enzyme catalyzes the initial step of tetrapyrrole biosynthesis
Products: -
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
Substrates: the enzyme catalyzes the initial step of tetrapyrrole biosynthesis in plants and prokaryotes
Products: -
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
Substrates: in presence of NADPH, the end product, glutamate-1-semialdehyde is formed. In the absence of NADPH, Escherichia coli GluTR exhibits substrate esterase activity
Products: -
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
Substrates: 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
Products: -
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
Substrates: -
Products: -
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
Substrates: the enzyme catalyzes the initial step of tetrapyrrole biosynthesis
Products: -
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
Substrates: the enzyme directs glutamate to chlorophyll biosynthesis
Products: -
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
Substrates: A7-U66, U29-A41, A53-U61 and U72 are expected to be required for recognition by the barley chloroplast glutamyl-tRNA(Glu) reductase
Products: -
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
Substrates: the fusion protein with glutathione S-transferase uses tRNAGlu from Hordeum vulgare chloroplast preferentially to Escherichia coli tRNAGlu
Products: -
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
Substrates: -
Products: -
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
Substrates: -
Products: -
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
Substrates: the enzyme catalyzes the initial step of tetrapyrrole biosynthesis
Products: -
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
Substrates: the enzyme is involved in the C5 pathway
Products: -
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
Substrates: in absence of NADPH, an esterase activity of GluTR hydrolyzes the highly reactive thioester of tRNAGlu to release glutamate
Products: -
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
Substrates: -
Products: -
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
Substrates: -
Products: -
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
Substrates: -
Products: -
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
Substrates: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
?
additional information
?
-
Substrates: 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
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
-
additional information
?
-
-
Substrates: 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
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
L-glutamyl-tRNAGlu + NADPH + H+
-
Substrates: -
Products: -
?
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
L-glutamyl-tRNAGlu + NADPH + H+
Substrates: -
Products: -
?
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
L-glutamyl-tRNAGlu + NADPH + H+
-
Substrates: -
Products: -
?
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
L-glutamyl-tRNAGlu + NADPH + H+
-
Substrates: -
Products: -
?
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
L-glutamyl-tRNAGlu + NADPH + H+
-
Substrates: -
Products: -
?
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
L-glutamyl-tRNAGlu + NADPH + H+
-
Substrates: -
Products: -
?
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
L-glutamyl-tRNAGlu + NADPH + H+
-
Substrates: -
Products: -
?
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
L-glutamyl-tRNAGlu + NADPH + H+
-
Substrates: -
Products: -
?
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
L-glutamyl-tRNAGlu + NADPH + H+
-
Substrates: -
Products: -
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
Substrates: -
Products: -
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
Substrates: -
Products: -
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
Substrates: -
Products: -
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
Substrates: the enzyme catalyzes the initial step of tetrapyrrole biosynthesis in plants and prokaryotes
Products: -
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
Substrates: complex formation between glutamyl-tRNA synthetase and glutamyl-tRNA reductase during the tRNA-dependent synthesis of 5-aminolevulinic acid
Products: -
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
Substrates: the enzyme is involved in delta-aminolevulinic acid formation during chlorophyll biosynthesis
Products: -
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
Substrates: 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
Products: -
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
Substrates: 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
Products: -
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
Substrates: the enzyme catalyzes the initial step of tetrapyrrole biosynthesis
Products: -
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
Substrates: the enzyme catalyzes the initial step of tetrapyrrole biosynthesis in plants and prokaryotes
Products: -
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
Substrates: -
Products: -
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
Substrates: the enzyme catalyzes the initial step of tetrapyrrole biosynthesis
Products: -
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
Substrates: the enzyme directs glutamate to chlorophyll biosynthesis
Products: -
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
Substrates: -
Products: -
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
Substrates: the enzyme catalyzes the initial step of tetrapyrrole biosynthesis
Products: -
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
Substrates: the enzyme is involved in the C5 pathway
Products: -
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
Substrates: -
Products: -
?
L-glutamyl-tRNAGlu + NADPH + H+
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
Substrates: -
Products: -
?
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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)
metabolism
-
GluTR is proposed to be the key regulatory enzyme of tetrapyrrole biosynthetic pathway that is tightly controlled at transcriptional and posttranslational levels
metabolism
-
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
-
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
-
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
-
the enzyme is the first unique enzyme in the tetrapyrrole biosynhetic pathway in plants
metabolism
-
enzyme abundance as a critical regulator of Staphylococcus aureus heme synthesis. HemX controls enzyme abundance in heme-proficient cells to regulate heme synthesis
metabolism
-
the enzyme catalyzes the rate-limiting step of 5-aminolevulinic acid synthesis
metabolism
-
the enzyme is essential for chlorophyll biosynthesis in rice
metabolism
-
enzyme abundance as a critical regulator of Staphylococcus aureus heme synthesis. HemX controls enzyme abundance in heme-proficient cells to regulate heme synthesis
-
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
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
-
the enzyme is required for the biosynthesis of 5-aminolevulinic acid
physiological function
-
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
-
the enzyme is required for the biosynthesis of 5-aminolevulinic acid
-
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Willows, R.D.; Kannangara, C.G.; Pontoppidan, B.
Nucleotides of tRNA(Glu) involved in recognition by barley chloroplast glutamyl-tRNA synthetase and glutamyl-tRNA reductase
Biochim. Biophys. Acta
1263
228-234
1995
Hordeum vulgare
brenda
Loida, P.J.; Thompson, R.L.; Walker, D.M.; CaJacob, C.A.
Novel inhibitors of glutamyl-tRNA(Glu) reductase identified through cell-based screening of the heme/chlorophyll biosynthetic pathway
Arch. Biochem. Biophys.
372
230-237
1999
Arabidopsis thaliana
brenda
Moser, J.; Schubert, W.D.; Heinz, D.W.; Jahn, D.
Structure and function of glutamyl-tRNA reductase involved in 5-aminolaevulinic acid formation
Biochem. Soc. Trans.
30
579-584
2002
Methanopyrus kandleri
brenda
Pontoppida, B.; Kannangara, C.G.
Purification and partial characterization of barley glutamyl-tRNAGlu reductase,the enzyme that directs glutamate to chlorophyll biosynthesis
Eur. J. Biochem.
225
529-537
1994
Hordeum vulgare
brenda
Jahn, D.
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