EC Number   |
Natural Substrates |
|---|
   2.3.2.20 | L-leucyl-tRNALeu + L-phenylalanyl-tRNAPhe |
highest activity |
| 2.3.2.20 | L-leucyl-tRNALeu + L-phenylalanyl-tRNAPhe |
second best activity |
| 2.3.2.20 | L-leucyl-tRNALeu + L-phenylalanyl-tRNAPhe |
the enzyme uses more efficiently Phe-tRNAPhe than any of the Leu-tRNALeu. The efficiency of cyclo(L-phenylalanyl-L-phenylalanyl) synthesis is not affected by the presence of Leu-tRNALeuGAG or Leu-tRNALeuTAA indicating that these molecules do not compete with Phe-tRNAPhe for binding to the enzyme. In contrast, Leu-tRNALeuCAA, Leu-tRNALeuTAG or or Leu-tRNALeuCAG isoacceptors inhibit cyclo(L-phenylalanyl-L-phenylalanyl) synthesis revealing a competition with Phe-tRNAPhe |
| 2.3.2.20 | L-phenylalanyl-tRNAPhe + L-leucyl-tRNALeu |
- |
| 2.3.2.20 | L-phenylalanyl-tRNAPhe + L-methionyl-tRNAMet |
lowest activity |
| 2.3.2.20 | L-phenylalanyl-tRNAPhe + L-phenylalanyl-tRNAPhe |
highest activity |
| 2.3.2.20 | L-phenylalanyl-tRNAPhe + L-phenylalanyl-tRNAPhe |
second best activity |
| 2.3.2.20 | L-phenylalanyl-tRNAPhe + L-tyrosinyl-tRNATyr |
- |
| 2.3.2.20 | L-tryptophanyl-tRNATrp + L-tryptophanyl-tRNATrp |
- |
| 2.3.2.20 | more |
the enzyme does not accept other aromatic aminoacyl-tRNA substrates than L-tryptophanyl-tRNA |
