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

BRENDA support

Literature summary for 6.1.1.23 extracted from

  • Suzuki, K.; Sato, Y.; Maeda, Y.; Shimizu, S.; Hossain, M.T.; Ubukata, S.; Sekiguchi, T.; Takenaka, A.
    Crystallization and preliminary X-ray crystallographic study of a putative aspartyl-tRNA synthetase from the crenarchaeon Sulfolobus tokodaii strain 7 (2007), Acta Crystallogr. Sect. F, 63, 608-612.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
overexpression in Escherichia coli strain BL21(DE3) Sulfurisphaera tokodaii

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant enzyme, 5-8 mg/ml in 20 mM Tris–HCl buffer, pH 7.0, hanging-drop vapour-diffusion method, 26°C, from 0.002 ml protein solution is mixed with 0.002 ml of reservoir solution containing 100 mM sodium HEPES buffer, pH 7.5, containing 100 mM NaCl and 1.6 M (NH4)2SO4, equilibration against 0.7 ml reservoir solution, X-ray diffraction structure determination and analysis at 2.3 A resolution, molecular replacement Sulfurisphaera tokodaii

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
Sulfurisphaera tokodaii

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
49074
-
x * 49074, sequence calculation Sulfurisphaera tokodaii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-aspartate + tRNAAsn Sulfurisphaera tokodaii dual activity of the ND-AspRS since an asparaginyl-tRNA synthetase is missing in Sulfolobus tokodaii strain 7 AMP + diphosphate + aspartyl-tRNAAsn
-
?
ATP + L-aspartate + tRNAAsp Sulfurisphaera tokodaii
-
AMP + diphosphate + aspartyl-tRNAAsp
-
?

Organism

Organism UniProt Comment Textmining
no activity in Sulfolobus tokodaii
-
-
-
no activity in Sulfolobus tokodaii 7
-
-
-
Sulfurisphaera tokodaii
-
a crenarchaeon, strain 7, gene ST0205
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme from Escherichia coli strain BL21(DE3) by anion exchange and hydroxyapatite chromatography Sulfurisphaera tokodaii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-aspartate + tRNAAsn dual activity of the ND-AspRS since an asparaginyl-tRNA synthetase is missing in Sulfolobus tokodaii strain 7 Sulfurisphaera tokodaii AMP + diphosphate + aspartyl-tRNAAsn
-
?
ATP + L-aspartate + tRNAAsp
-
Sulfurisphaera tokodaii AMP + diphosphate + aspartyl-tRNAAsp
-
?
additional information the purified protein has the ability to catalyze the aspartylation of hydroxylamine through an aspartyl-AMP intermediate Sulfurisphaera tokodaii ?
-
?

Subunits

Subunits Comment Organism
? x * 49074, sequence calculation Sulfurisphaera tokodaii

Synonyms

Synonyms Comment Organism
nondiscriminating aspartyl-tRNA synthetase
-
Sulfurisphaera tokodaii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
57
-
-
Sulfurisphaera tokodaii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Sulfurisphaera tokodaii

Cofactor

Cofactor Comment Organism Structure
ATP
-
Sulfurisphaera tokodaii