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Literature summary extracted from

  • Briand, C.; Poterszman, A.; Eiler, S.; Webster, G.; Thierry, J.; Moras, D.
    An intermediate step in the recognition of tRNA(Asp) by aspartyl-tRNA synthetase (2000), J. Mol. Biol., 299, 1051-1060.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
6.1.1.12 purified enzyme complexed with tRNAAsp from Thermus thermophilus or Escherichia coli, potential intermediate of the recognition process, protein solution: 15 mg/ml of enzyme, 7.35 mg/ml of tRNA, plus equal volume of reservoir solution: 10 mM MgCl2, 50 mM HEPES, pH 7.5, 0.7 M sodium citrate, 17°C, 2 weeks, X-ray diffraction structure determination at 3.5 A resolution, structure analysis Thermus thermophilus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.1.1.12 additional information
-
 additional information very low kinetic effiency at 17°C 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
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.12 Thermus thermophilus
-
 prokaryotic dimeric class IIb aspartyl-tRNA synthetase
-

Reaction

EC Number Reaction Comment Organism Reaction ID
6.1.1.12 ATP + L-aspartate + tRNAAsp = AMP + diphosphate + L-aspartyl-tRNAAsp pathway for tRNA binding and recognition is proposed 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
-
 ?

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

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.1.1.12 additional information
-
 very low kinetic effiency at 17°C Thermus thermophilus