Transient kinetics of ligand binding and role of the C-terminus in the dUTPase from equine infectious anemia virus

Forskningsoutput: TidskriftsbidragArtikel i vetenskaplig tidskrift

Abstract

Transient kinetics of the equine infectious anemia virus deoxyuridine 5'-triphosphate nucleotide hydrolase were characterized by monitoring the fluorescence of the protein. Rate constants for the association and dissociation of substrate and inhibitors were determined and found to be consistent with a one-step mechanism for substrate binding. A C-terminal part of the enzyme presumed to be flexible was removed by limited trypsinolysis. As a result, the activity of the dUTPase was completely quenched, but the rate constants and fluorescent signal of the truncated enzyme were affected only to a minor degree. We conclude that the flexible C-terminus is not a prerequisite for substrate binding, but indispensable for catalysis.

Detaljer

Författare
  • Johan Nord
  • Martin Kiefer
  • Hans-Werner Adolph
  • Michael M Zeppezauer
  • Per-Olof Nyman
Enheter & grupper
Forskningsområden

Ämnesklassifikation (UKÄ) – OBLIGATORISK

  • Biologiska vetenskaper

Nyckelord

Originalspråkengelska
Sidor (från-till)312-316
TidskriftFEBS Letters
Volym472
Utgivningsnummer2-3
StatusPublished - 2000
PublikationskategoriForskning
Peer review utfördJa

Relaterad forskningsoutput

Nord, J., 2000, Johan Nord, Department of Biochemistry, Center for Chemistry and Chemical Engineering, P.O. Box 124, S-221 00, Lund, Sweden. 142 s.

Forskningsoutput: AvhandlingDoktorsavhandling (sammanläggning)

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