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Literature summary for 6.1.1.12 extracted from

  • Vellekamp, G.J.; Kull, F.J.
    Allotropism in aspartyl-tRNA synthetase from porcine thyroid (1981), Eur. J. Biochem., 118, 261-269.
    View publication on PubMed
Search for more literature for 6.1.1.12

Inhibitors

Inhibitors Comment Organism Structure
K2HPO4 inhibits enzyme forms PC-1 and PC-2, PC-3 is stimulated (optimal concentration 75 mM) Sus scrofa
KCl inhibits enzyme forms PC-1 and PC-2, PC-3 is stimulated (optimal concentration 75 mM) Sus scrofa
NaCl inhibits enzyme forms PC-1 and PC-2 much more than PC-3 Sus scrofa

Metals/Ions

Metals/Ions Comment Organism Structure
K2HPO4 enzyme form PC-3 is stimulated, optimal concentration 75 mM, enzyme form PC-1 and enzyme form PC-2 are inhibited Sus scrofa
KCl enzyme form PC-3 is stimulated, optimal concentration 75 mM, enzyme form PC-1 and enzyme form PC-2 are inhibited Sus scrofa
PO43- appears to act synergistically with K+ in stimulation of enzyme form PC-3, no effect on either enzyme form PC-1 or enzyme form PC-2 Sus scrofa

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
150000
-
 gel filtration, PC-1 and PC-2 Sus scrofa
500000
-
 gel filtration, PC-3, possibly PC-3 represents a large complex of aminoacyl-tRNA synthetases Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
2 enzyme forms: PC-1, PC-2 and PC-3 Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
thyroid gland
-
 Sus scrofa
-

Substrates and Products (Substrate)

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