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Interaction of the high-affinity inhibitor tetrahydro-dUMP with the allosteric enzyme deoxycytidylate aminohydrolase.
Nucci, R; Febbraio, F; Piccialli, G; de Napoli, L; Vaccaro, C; Rossi, M; Whitehead, E P.
Affiliation
  • Nucci R; Institute of Protein Biochemistry and Enzymology, CNR, Naples, Italy.
Arch Biochem Biophys ; 310(1): 49-53, 1994 Apr.
Article de En | MEDLINE | ID: mdl-8161220
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."
Sujet(s)
Recherche sur Google
Collection: 01-internacional Base de données: MEDLINE Sujet principal: DCMP deaminase / Nucléotides désoxyuridyliques Limites: Animals Langue: En Journal: Arch Biochem Biophys Année: 1994 Type de document: Article Pays d'affiliation: Italie
Recherche sur Google
Collection: 01-internacional Base de données: MEDLINE Sujet principal: DCMP deaminase / Nucléotides désoxyuridyliques Limites: Animals Langue: En Journal: Arch Biochem Biophys Année: 1994 Type de document: Article Pays d'affiliation: Italie
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