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Literature summary extracted from

  • Fukunaga, R.; Yokoyama, S.
    Crystallization and preliminary X-ray crystallographic study of alanyl-tRNA synthetase from the archaeon Archaeoglobus fulgidus (2007), Acta Crystallogr. Sect. F, 63, 224-228.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.1.1.7 expression of the full-length AlaRS, of the N-terminal fragment lacking the C-terminal oligomerization domain, residues 1-739, and of the C-terminal oligomerization domain of AlaRS, residues 737-906, in Escherichia coli strain BL21 Archaeoglobus fulgidus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
6.1.1.7 purified recombinant full-length enzyme, N-terminal domain, and C-terminal domain, hanging-drop vapour-diffusion method, mixing of 0.001 ml of protein and reservoir solution, and equilibration against 0.5 ml of reservoir solution at 20°C, for crystallization of the AlaRS-FL–tRNAAla complex, tRNAAla is heated at 80°C for 5 min and is gradually cooled to room temperature for refolding, in presence of 1 mM AMP-PNP, different methods for the different protein samples are used, overview, X-ray diffraction structure determination and analysis at 3.2-3.5 A resolution Archaeoglobus fulgidus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.1.1.7 Mg2+
-
Archaeoglobus fulgidus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.1.1.7 ATP + L-alanine + tRNAAla Archaeoglobus fulgidus
-
AMP + diphosphate + L-alanyl-tRNAAla
-
?

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.7 Archaeoglobus fulgidus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.1.1.7 recombinant full-length AlaRS and AlaRS domains from Escherichia coli strain BL21 by anion exchange chromatography followed by hydrophobic interaction and adsorption chromatography, respectively Archaeoglobus fulgidus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.1.1.7 ATP + L-alanine + tRNAAla
-
Archaeoglobus fulgidus AMP + diphosphate + L-alanyl-tRNAAla
-
?
6.1.1.7 ATP + L-alanine + tRNAAla the aminoacylation reaction takes place in two steps catalyzed by the same active site: the synthesis of an aminoacyladenylate as an activated intermediate from the amino acid and ATP and the transfer of the aminoacyl moiety to the 3'-terminus of the cognate tRNA to yield the aminoacyl-tRNA, the synthetic active site of AlaRS misrecognizes noncognate glycine and serine as well as recognizing the cognate alanine and produces GlytRNAAla and Ser-tRNAAla, the editing domain hydrolyzes the incorrect products GlytRNAAla and Ser-tRNAAla and thus contributes to accurate aminoacylation, three tRNA isoacceptors, tRNAAla1, tRNA and tRNAAla3 Archaeoglobus fulgidus AMP + diphosphate + L-alanyl-tRNAAla
-
?

Subunits

EC Number Subunits Comment Organism
6.1.1.7 More AlaRS consists of four parts: an N-terminal aminoacylation active-site domain, a tRNA-recognition module, an editing domain and a C-terminal oligomerization domain Archaeoglobus fulgidus

Synonyms

EC Number Synonyms Comment Organism
6.1.1.7 Alanyl-tRNA synthetase
-
Archaeoglobus fulgidus
6.1.1.7 AlaRS
-
Archaeoglobus fulgidus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.1.1.7 65
-
assay at Archaeoglobus fulgidus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.1.1.7 7.5
-
assay at Archaeoglobus fulgidus

Cofactor

EC Number Cofactor Comment Organism Structure
6.1.1.7 ATP
-
Archaeoglobus fulgidus