Interaction of the high-affinity inhibitor tetrahydro-dUMP with the allosteric enzyme deoxycytidylate aminohydrolase

Arch Biochem Biophys. 1994 Apr;310(1):49-53. doi: 10.1006/abbi.1994.1138.

Abstract

Tetrahydro-dUMP, an analog of the putative transition state in aminohydrolysis of deoxycytidine monophosphate (dCMP) inhibits the allosteric enzyme deoxycytidylate aminohydrolase with high affinity. The inhibition is reversible, and its kinetics is consistent with the analog binding at the substrate site only to one and the same conformation that binds the substrate dCMP. Such kinetics is what would be expected for a transition state analog interacting in an allosteric "K system."

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Allosteric Regulation
  • Animals
  • DCMP Deaminase / antagonists & inhibitors
  • DCMP Deaminase / metabolism*
  • Deoxyuracil Nucleotides / metabolism*
  • Deoxyuracil Nucleotides / pharmacology
  • Kinetics
  • Perissodactyla
  • Spleen / enzymology

Substances

  • Deoxyuracil Nucleotides
  • 2'-deoxy-tetrahydro-5'-uridylic acid
  • DCMP Deaminase