Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
chloroplast | 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 delta-aminolevulinic acid (ALA) starting with glutamyltRNAGlu, while a minor part of the active protein complex is attached to the thylakoid membrane via a GluTR-binding protein (GluTRBP) | Arabidopsis thaliana | 9507 | - |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-glutamyl-tRNAGlu + NADPH + H+ | Arabidopsis thaliana | - |
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Arabidopsis thaliana | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
seedling | - |
Arabidopsis thaliana | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-glutamyl-tRNAGlu + NADPH + H+ | - |
Arabidopsis thaliana | L-glutamate 1-semialdehyde + NADP+ + tRNAGlu | - |
? |
Synonyms | Comment | Organism |
---|---|---|
GluTR | - |
Arabidopsis thaliana |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADP+ | - |
Arabidopsis thaliana | |
NADPH | - |
Arabidopsis thaliana |
General Information | Comment | Organism |
---|---|---|
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 | Arabidopsis thaliana |
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 | Arabidopsis thaliana |