Interaction of the high-affinity inhibitor tetrahydro-dUMP with the allosteric enzyme deoxycytidylate aminohydrolase.
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."
Nucci
R
R
Institute of Protein Biochemistry and Enzymology, CNR, Naples, Italy.
Febbraio
F
F
Piccialli
G
G
de Napoli
L
L
Vaccaro
C
C
Rossi
M
M
Whitehead
E P
EP
D000494:Allosteric Regulation; D000818:Animals; D003844:DCMP Deaminase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D003856:Deoxyuracil Nucleotides / Q000378:metabolism* / Q000494:pharmacology; D007700:Kinetics; D010527:Perissodactyla; D013154:Spleen / Q000201:enzymology
D003856:Deoxyuracil Nucleotides; C086818:2'-deoxy-tetrahydro-5'-uridylic acid; D003844:DCMP Deaminase