Esterification of all four monoribonucleotides with acetyl-D-L-valine proceeds with a preference for the D-isomer but the D/L ratio in the products declines as a function of the hydrophobicity of the nucleotide

Bioorg Chem. 1992:20:265-8. doi: 10.1016/0045-2068(92)90019-y.

Abstract

We recently reported that esterification of 5'-AMP with N-acetyl amino acids proceeds with a preference for D-amino acids, and the D/L ratio in products declines as the hydrophobicity of the amino acid declines. Using one amino acid, Ac-Val, we now show that esterification of all four nucleotides proceeds with a preference for the D-isomer and the preference declines as the hydrophobicity of the nucleotide declines. So, in both types of experiments, the preferences seem determined by hydrophobic interactions.

MeSH terms

  • Adenosine Monophosphate / chemistry
  • Amino Acids / chemistry
  • Esterification
  • Isomerism
  • Nucleotides / chemistry*
  • Ribonucleotides / chemistry*
  • Valine / analogs & derivatives*
  • Valine / chemistry
  • Water / chemistry*

Substances

  • Amino Acids
  • Nucleotides
  • Ribonucleotides
  • Water
  • Adenosine Monophosphate
  • Valine
  • N-acetylvaline