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

BRENDA support

Literature summary extracted from

  • Berthet-Colominas, C.; Seignovert, L.; Hartlein, M.; Grotli, M.; Cusack, S.; Leberman, R.
    The crystal structure of asparaginyl-tRNA synthetase from Thermus thermophilus and its complexes with ATP and asparaginyl-adenylate: the mechanism of discrimination between asparagine and aspartic acid (1998), EMBO J., 17, 2947-2960.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
6.1.1.12 enzyme complexed with a non-hydrolysable analogue of asparaginyl-adenylate and with ATP, X-ray diffraction structure determination at 2.6 A resolution Thermus thermophilus
6.1.1.22 recombinant enzyme, native or complexed withATP and asparaginyl-adenylate, 3 different crystal forms, X-ray diffraction structure determination at 2.6 A resolution and analysis Thermus thermophilus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.1.1.12 ATP + L-aspartate + tRNAAsp Thermus thermophilus
-
 AMP + diphosphate + L-aspartyl-tRNAAsp
-
 ?
6.1.1.12 additional information Thermus thermophilus aspartyl- and asparaginyl-tRNA synthetases have evolved relatively recently from a comon ancestor ?
-
 ?
6.1.1.22 ATP + L-asparagine + tRNAAsn Thermus thermophilus
-
 AMP + diphosphate + L-asparaginyl-tRNAAsn
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.12 Thermus thermophilus
-
 class IIb aminoacyl-tRNA synthetase
-
6.1.1.22 Thermus thermophilus P54263 purified recombinant enzyme expressed in Escherichia coli
-

Reaction

EC Number Reaction Comment Organism Reaction ID
6.1.1.12 ATP + L-aspartate + tRNAAsp = AMP + diphosphate + L-aspartyl-tRNAAsp active site residues Thermus thermophilus
a
6.1.1.22 ATP + L-asparagine + tRNAAsn = AMP + diphosphate + L-asparaginyl-tRNAAsn mechanism of substrate specificity, structure of substrate binding sites Thermus thermophilus
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.1.1.12 ATP + L-aspartate + tRNAAsp
-
 Thermus thermophilus AMP + diphosphate + L-aspartyl-tRNAAsp
-
 ?
6.1.1.12 additional information aspartyl- and asparaginyl-tRNA synthetases have evolved relatively recently from a comon ancestor Thermus thermophilus ?
-
 ?
6.1.1.22 ATP + L-asparagine + tRNAAsn
-
 Thermus thermophilus AMP + diphosphate + L-asparaginyl-tRNAAsn
-
 ?
6.1.1.22 ATP + L-asparagine + tRNAAsn substrate specificity Thermus thermophilus AMP + diphosphate + L-asparaginyl-tRNAAsn
-
 ?

Subunits

EC Number Subunits Comment Organism
6.1.1.22 dimer class II synthetase, crystal structure determination Thermus thermophilus

Synonyms

EC Number Synonyms Comment Organism
6.1.1.12 Aspartic acid translase
-
 Thermus thermophilus
6.1.1.12 Aspartyl ribonucleate synthetase
-
 Thermus thermophilus
6.1.1.12 aspartyl ribonuleic synthetase
-
 Thermus thermophilus
6.1.1.12 Aspartyl-transfer ribonucleic acid synthetase
-
 Thermus thermophilus
6.1.1.12 Aspartyl-transfer RNA synthetase
-
 Thermus thermophilus
6.1.1.12 Aspartyl-tRNA synthetase
-
 Thermus thermophilus
6.1.1.22 AsnRS
-
 Thermus thermophilus
6.1.1.22 Asparagine translase
-
 Thermus thermophilus
6.1.1.22 Asparagine--tRNA ligase
-
 Thermus thermophilus
6.1.1.22 Asparaginyl transfer ribonucleic acid synthetase
-
 Thermus thermophilus
6.1.1.22 Asparaginyl transfer RNA synthetase
-
 Thermus thermophilus
6.1.1.22 Asparaginyl-transfer ribonucleate synthetase
-
 Thermus thermophilus
6.1.1.22 Asparaginyl-tRNA synthetase
-
 Thermus thermophilus
6.1.1.22 Asparagyl-transfer RNA synthetase
-
 Thermus thermophilus
6.1.1.22 Potentially protective 63 kDa antigen
-
 Thermus thermophilus
6.1.1.22 Synthetase, asparaginyl-transfer ribonucleate
-
 Thermus thermophilus

Cofactor

EC Number Cofactor Comment Organism Structure
6.1.1.22 ATP
-
 Thermus thermophilus