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Literature summary for 6.1.1.20 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
Search for more literature for 6.1.1.20

Crystallization (Commentary)

Crystallization (Comment) Organism
-
 Thermus thermophilus

KM Value [mM]

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Thermus thermophilus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Thermus thermophilus

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Subunits

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

Temperature Optimum [°C]

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