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ENZYME

ENZYME entry: EC 6.3.5.6

PURL: https://purl.expasy.org/enzyme/EC/6.3.5.6
Accepted Name
asparaginyl-tRNA synthase (glutamine-hydrolyzing)
Alternative Name(s)
Asp-AdT
aspartyl-tRNA(Asn) amidotransferase
Asp-tRNA(Asn) amidotransferase
GatCAB
Reaction catalysed
L-aspartyl-tRNA(Asn) + L-glutamine + ATP + H2O = L-asparaginyl-tRNA(Asn) + L-glutamate + ADP + phosphate + 2 H(+)
Comment(s)
  • This reaction forms part of a two-reaction system for producing asparaginyl-tRNA in Deinococcus radiodurans and other organisms lacking a specific enzyme for asparagine synthesis.
  • In the first step, a non-discriminating ligase (EC 6.1.1.23) mischarges tRNA(Asn) with aspartate, leading to the formation of aspartyl-tRNA(Asn).
  • The aspartyl-tRNA(Asn) is not used in protein synthesis until the present enzyme converts it into asparaginyl-tRNA(Asn) (aspartyl- tRNA(Asp) is not a substrate for this enzyme).
  • A glutaminase subunit (cf. EC 3.5.1.2) produces an ammonia molecule that is transferred by a 30 A tunnel to a synthase subunit, where it is ligated to the carboxy group that has been activated by phosphorylation.
  • Bacterial GatCAB complexes also has the activity of EC 6.3.5.7.
Cross-references
BRENDA6.3.5.6
EC2PDB6.3.5.6
ExplorEnz6.3.5.6
KEGG Ligand Database for Enzyme Nomenclature6.3.5.6
IUBMB Enzyme Nomenclature6.3.5.6
MEDLINEFind literature relating to 6.3.5.6
MetaCyc6.3.5.6
Rhea expert-curated reactions6.3.5.6

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All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 6.3.5.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 6.3.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 6.-.-.-