22.214.171.124 - Glutamyl-tRNA reductase
There are no alternative names for this Enzyme
(S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-glutamyl-tRNA(Glu) + NADPH
There are no Cofactors for this Enzyme
|AA||Uniprot||Uniprot Resid||PDB||PDB Resid|
intermediate formation, hydride transfer, enzyme-substrate complex formation, bimolecular nucleophilic addition, overall product formed, native state of enzyme regenerated, enzyme-substrate complex cleavage, overall reactant used, unimolecular elimination by the conjugate base, bimolecular nucleophilic substitution, aromatic unimolecular elimination by the conjugate base
- Maintenance of heme homeostasis in Staphylococcus aureus through post-translational regulation of glutamyl-tRNA reductase.
- An alanine to valine mutation of glutamyl-tRNA reductase enhances 5-aminolevulinic acid synthesis in rice.
- The GluTR-binding protein is the heme-binding factor for feedback control of glutamyl-tRNA reductase.
- Fluorescence in blue light (FLU) is involved in inactivation and localization of glutamyl-tRNA reductase during light exposure.
- Controlled Partitioning of Glutamyl-tRNA Reductase in Stroma- and Membrane-Associated Fractions Affects the Synthesis of 5-Aminolevulinic Acid.
- Staphylococcus aureus HemX Modulates Glutamyl-tRNA Reductase Abundance To Regulate Heme Biosynthesis.
- Chloroplast SRP43 acts as a chaperone for glutamyl-tRNA reductase, the rate-limiting enzyme in tetrapyrrole biosynthesis.
- N-terminal engineering of glutamyl-tRNA reductase with positive charge arginine to increase 5-aminolevulinic acid biosynthesis.
- The Arabidopsis glutamyl-tRNA reductase (GluTR) forms a ternary complex with FLU and GluTR-binding protein.
- The Non-canonical Tetratricopeptide Repeat (TPR) Domain of Fluorescent (FLU) Mediates Complex Formation with Glutamyl-tRNA Reductase.
- Crystal structure of Arabidopsis glutamyl-tRNA reductase in complex with its stimulator protein.