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BRENDA support

Literature summary for 6.1.1.12 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)

Crystallization (Comment) Organism
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]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information very low kinetic effiency at 17°C Thermus thermophilus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-aspartate + tRNAAsp Thermus thermophilus
-
AMP + diphosphate + L-aspartyl-tRNAAsp
-
?

Organism

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

Reaction

Reaction Comment Organism Reaction ID
ATP + L-aspartate + tRNAAsp = AMP + diphosphate + L-aspartyl-tRNAAsp pathway for tRNA binding and recognition is proposed Thermus thermophilus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-aspartate + tRNAAsp
-
Thermus thermophilus AMP + diphosphate + L-aspartyl-tRNAAsp
-
?

Synonyms

Synonyms Comment Organism
Aspartic acid translase
-
Thermus thermophilus
Aspartyl ribonucleate synthetase
-
Thermus thermophilus
aspartyl ribonuleic synthetase
-
Thermus thermophilus
Aspartyl-transfer ribonucleic acid synthetase
-
Thermus thermophilus
Aspartyl-transfer RNA synthetase
-
Thermus thermophilus
Aspartyl-tRNA synthetase
-
Thermus thermophilus

pH Optimum

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