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Literature summary for 6.1.1.24 extracted from

  • Mailu, B.M.; Li, L.; Arthur, J.; Nelson, T.M.; Ramasamy, G.; Fritz-Wolf, K.; Becker, K.; Gardner, M.J.
    Plasmodium apicoplast Gln-tRNAGln biosynthesis utilizes a unique GatAB amidotransferase essential for erythrocytic stage parasites (2015), J. Biol. Chem., 290, 29629-29641 .
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
drug development the apicoplast indirect aminoacylation pathway is a potential drug target Plasmodium falciparum

Cloned(Commentary)

Cloned (Comment) Organism
gene Pf3D7_1357200, recombinant expression of codon-optimized GluRS in Escherichia coli KRX cells Plasmodium falciparum

Localization

Localization Comment Organism GeneOntology No. Textmining
apicoplast
-
Plasmodium falciparum 20011
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Plasmodium falciparum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-glutamate + tRNAGln Plasmodium falciparum
-
AMP + diphosphate + L-glutamyl-tRNAGln
-
?
ATP + L-glutamate + tRNAGlu Plasmodium falciparum
-
AMP + diphosphate + L-glutamyl-tRNAGlu
-
?
additional information Plasmodium falciparum the glutamyl residue of Glu-tRNAGln is then transamidated by a glutamyl-tRNAGln amidotransferase (Glu-AdT) in the presence of ATP using Gln as an amide donor, producing GlntRNAGln, coupled reaction assay ?
-
?

Organism

Organism UniProt Comment Textmining
Plasmodium falciparum Q8IDD3
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-glutamate + tRNAGln
-
Plasmodium falciparum AMP + diphosphate + L-glutamyl-tRNAGln
-
?
ATP + L-glutamate + tRNAGlu
-
Plasmodium falciparum AMP + diphosphate + L-glutamyl-tRNAGlu
-
?
additional information the glutamyl residue of Glu-tRNAGln is then transamidated by a glutamyl-tRNAGln amidotransferase (Glu-AdT) in the presence of ATP using Gln as an amide donor, producing GlntRNAGln, coupled reaction assay Plasmodium falciparum ?
-
?
additional information the non-discriminating GluRS (ND-GluRS) can glutamylate both tRNAGlu and tRNAGln Plasmodium falciparum ?
-
?

Synonyms

Synonyms Comment Organism
ND-GluRS
-
Plasmodium falciparum
non-discriminating GluRS
-
Plasmodium falciparum
non-discriminating glutamyl-tRNA synthetase
-
Plasmodium falciparum
Pf3D7_1357200
-
Plasmodium falciparum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Plasmodium falciparum

Cofactor

Cofactor Comment Organism Structure
ATP
-
Plasmodium falciparum

General Information

General Information Comment Organism
metabolism the malaria parasite Plasmodium falciparum apicoplast indirect aminoacylation pathway utilizes a non-discriminating glutamyl-tRNA synthetase to synthesize Glu-tRNAGln and a glutaminyl-tRNA amidotransferase to convert Glu-tRNAGln to Gln-tRNAGln Plasmodium falciparum
physiological function Plasmodium apicoplast protein synthesis is essential for parasite survival, aminoacyl-tRNA formation is essential for protein synthesis. The malaria parasite Plasmodium falciparum apicoplast indirect aminoacylation pathway utilizes a non-discriminating glutamyl-tRNA synthetase to synthesize Glu-tRNAGln and a glutaminyl-tRNA amidotransferase to convert Glu-tRNAGln to Gln-tRNAGln. Formation of apicoplast Gln-tRNAGln proceeds via indirect aminoacylation. The nucleus-encoded non-discriminating GluRS is imported into the apicoplast is responsible for the formation of misacylated Glu-tRNAGln and is essential in the erythrocytic stages Plasmodium falciparum