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Glutaminyl-tRNA synthase (glutamine-hydrolysing)

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Glutaminyl-tRNA synthase (glutamine-hydrolyzing)
Identifiers
EC no.6.3.5.7
CAS no.52232-48-1
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Glu-tRNA amidotransferase or glutaminyl-tRNA synthase (glutamine-hydrolysing) enzyme (EC 6.3.5.7) is an amidotransferase that catalyzes the conversion of the non-cognate amino acid glutamyl-tRNA to the cognate glutaminyl-tRNA. It catalyzes the reaction:

ATP + glutamyl-tRNA + L-glutamine {\displaystyle \rightleftharpoons } ADP + phosphate + glutaminyl-tRNA + L-glutamate

This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds carbon-nitrogen ligases with glutamine as amido-N-donor. The systematic name of this enzyme class is glutamyl-tRNA:L-glutamine amido-ligase (ADP-forming). This enzyme participates in glutamate metabolism and alanine and aspartate metabolism.

Function and evolutionary significance

Most bacterial and all archaea genomes do not encode a glutaminyl-tRNA synthetase (GlnRS). Instead they first synthesize the attachment of an amino acid on the tRNA by first attaching a non-cognate glutamate to the tRNA. Then these organisms use the amidotransferase: glutaminyl-tRNA synthase (glutamine-hydrolysing) (EC 6.3.5.7) enzyme to convert the glutamate attached to tRNA to glutamine.

References

  1. ^ Sheppard K, Yuan J, Hohn MJ, Jester B, Devine KM, Söll D (April 2008). "From one amino acid to another: tRNA-dependent amino acid biosynthesis". Nucleic Acids Research. 36 (6): 1813–1825. doi:10.1093/nar/gkn015. PMC 2330236. PMID 18252769.
Enzymes: CO CS and CN ligases (EC 6.1-6.3)
6.1: Carbon-Oxygen
6.2: Carbon-Sulfur
6.3: Carbon-Nitrogen
Enzymes
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