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Literature summary extracted from

  • Ankilova, V.N.; Reshetnikova, L.S.; Chernaya, M.M.; Lavrik, O.I.
    Phenylalanyl-tRNA synthetase from Thermus thermophilus HB8. Purification and properties of the crystallizing enzyme (1988), FEBS Lett., 227, 9-13.
No PubMed abstract available

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
6.1.1.20
-
 Thermus thermophilus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.1.1.20 additional information
-
 additional information negative cooperativity exists in the binding of all substrates Thermus thermophilus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
6.1.1.20 40000
-
 2 * 40000 (alpha) + 2 * 92000 (beta), SDS-PAGE Thermus thermophilus
6.1.1.20 92000
-
 2 * 40000 (alpha) + 2 * 92000 (beta), SDS-PAGE Thermus thermophilus
6.1.1.20 245000
-
 gel filtration Thermus thermophilus

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.20 Thermus thermophilus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.1.1.20
-
 Thermus thermophilus

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
6.1.1.20 0.198
-
-
 Thermus thermophilus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.1.1.20 ATP + L-phenylalanine + tRNAPhe
-
 Thermus thermophilus AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
 ?

Subunits

EC Number Subunits Comment Organism
6.1.1.20 tetramer 2 * 40000 (alpha) + 2 * 92000 (beta), SDS-PAGE Thermus thermophilus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.1.1.20 70
-
 E. coli tRNAPhe, aminoacylation Thermus thermophilus
6.1.1.20 80
-
 Thermus thermophilus tRNAPhe, aminoacylation Thermus thermophilus