Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

6.3.5.6: asparaginyl-tRNA synthase (glutamine-hydrolysing)

This is an abbreviated version!
For detailed information about asparaginyl-tRNA synthase (glutamine-hydrolysing), go to the full flat file.

Word Map on EC 6.3.5.6

Reaction

4-phosphooxy-L-aspartyl-tRNAAsn
+
NH3
=
L-asparaginyl-tRNAAsn
+
phosphate

Synonyms

AdT, AsnRS, Asp-AdT, Asp-tRNAAsn amidotransferase, Asp/Glu-Adt, asparaginyl-transfer RNA synthetase, Asparaginyl-tRNA synthetase, aspartyl-tRNAAsn amidotransferase, GatCAB, glutamine-dependent Asp-tRNAAsn/Glu-tRNAGln amidotransferase, NRS, tRNA-dependent amidotransferase

ECTree

     6 Ligases
         6.3 Forming carbon-nitrogen bonds
             6.3.5 Carbon-nitrogen ligases with glutamine as amido-N-donor
                6.3.5.6 asparaginyl-tRNA synthase (glutamine-hydrolysing)

Engineering

Engineering on EC 6.3.5.6 - asparaginyl-tRNA synthase (glutamine-hydrolysing)

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DELTA 1-112
structures of the catalytically active N-terminally truncated enzyme (residues 112-548) is solved by X-ray crystallography
S128T
-
mutant protein retains significant glutaminase activity and transamidase activity in the presence of Gln
S152A
-
mutant is glutaminase inactive
S152T
-
mutant is glutaminase inactive
additional information