tRNA Recognition by Glutamyl-tRNA Reductase
نویسندگان
چکیده
منابع مشابه
Glutamate recognition and hydride transfer by Escherichia coli glutamyl-tRNA reductase.
The initial step of tetrapyrrole biosynthesis in Escherichia coli involves the NADPH-dependent reduction by glutamyl-tRNA reductase (GluTR) of tRNA-bound glutamate to glutamate-1-semialdehyde. We evaluated the contribution of the glutamate moiety of glutamyl-tRNA to substrate specificity in vitro using a range of substrates and enzyme variants. Unexpectedly, we found that tRNA(Glu) mischarged w...
متن کاملTwo glutamyl-tRNA reductase activities in Escherichia coli.
delta-Aminolevulinic acid (ALA) is the first committed precursor for tetrapyrrole biosynthesis. ALA formation in Escherichia coli occurs in a tRNA-dependent three-step conversion from glutamate. Glu-tRNA reductase is the key enzyme in this pathway. E. coli K12 contains two Glu-tRNA reductase activities which differ in their molecular weights. Here we describe the purification of one of these en...
متن کاملPurification of glutamyl-tRNA reductase from Synechocystis sp. PCC 6803.
delta-Aminolevulinic acid is the universal precursor for all tetrapyrroles including hemes, chlorophylls, and bilins. In plants, algae, cyanobacteria, and many other bacteria, delta-aminolevulinic acid is synthesized from glutamate in a reaction sequence that requires three enzymes, ATP, NADPH, and tRNA(Glu). The three enzymes have been characterized as glutamyl-tRNA synthetase, glutamyl-tRNA r...
متن کاملGlutamyl - tRNA Reductase from Escherichia coli and Synechocystis 6803 ”
In the cyanobacterium Synechocystis sp. PCC 6803 and in the enterobacterium Escherichia coli &aminolevulinic acid (ALA) is formed from glutamyl-tRNA by the sequential action of two enzymes, glutamyl-tRNA reductase (GluTR) and glutamate 1-semialdehyde aminotransferase. E. coli has two GluTR proteins with sizes of 45 kDa (GluTR46) and 85 kDa (GluTR85) (Jahn, D., Michelsen, U., and 5611, D. (1991...
متن کاملATP binding by glutamyl-tRNA synthetase is switched to the productive mode by tRNA binding.
Aminoacyl-tRNA synthetases catalyze the formation of an aminoacyl-AMP from an amino acid and ATP, prior to the aminoacyl transfer to tRNA. A subset of aminoacyl-tRNA synthetases, including glutamyl-tRNA synthetase (GluRS), have a regulation mechanism to avoid aminoacyl-AMP formation in the absence of tRNA. In this study, we determined the crystal structure of the 'non-productive' complex of The...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2004
ISSN: 0021-9258
DOI: 10.1074/jbc.m401529200