Literature DB >> 10358938

Interaction of the recombinant herpes simplex virus type 1 thymidine kinase with thymidine and aciclovir: a kinetic study.

S Kussmann-Gerber1, C Wurth, L Scapozza, B D Pilger, V Pliska, G Folkers.   

Abstract

Herpes Simplex Virus type 1 thymidine kinase (HSV 1 TK) is a key target for antiviral therapy and it phosphorylates a broad spectrum of nucleosides and nucleotides. We report the results from kinetic and inhibition experiments with HSV 1 TK, and show that there is a preferred, but not exclusive, binding order of substrates, i.e. dT binds prior to ATP. Furthermore, the results provide new informations on the mechanism of binding suggesting that HSV1 TK undergoes conformational changes during the catalytic cycle.

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Year:  1999        PMID: 10358938     DOI: 10.1080/15257779908043078

Source DB:  PubMed          Journal:  Nucleosides Nucleotides        ISSN: 0732-8311


  1 in total

1.  The effect of substrate binding on the conformation and structural stability of Herpes simplex virus type 1 thymidine kinase.

Authors:  C Wurth; U Kessler; J Vogt; G E Schulz; G Folkers; L Scapozza
Journal:  Protein Sci       Date:  2001-01       Impact factor: 6.725

  1 in total

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