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.
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.
Wickramasinghe
N S
NS
Department of Biochemistry, University of Alabama at Birmingham 35294, USA.
Lacey
J C
JC
D000249:Adenosine Monophosphate / Q000737:chemistry; D000596:Amino Acids / Q000737:chemistry; D004951:Esterification; D007536:Isomerism; D009711:Nucleotides / Q000737:chemistry*; D012265:Ribonucleotides / Q000737:chemistry*; D014633:Valine / Q000031:analogs & derivatives* / Q000737:chemistry; D014867:Water / Q000737:chemistry*
D000596:Amino Acids; D009711:Nucleotides; D012265:Ribonucleotides; D014867:Water; D000249:Adenosine Monophosphate; D014633:Valine; C055589:N-acetylvaline