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  Modifying human thymidylate kinase to potentiate azidothymidine activation

Brundiers, R., Lavie, A., Veit, T., Reinstein, J., Schlichting, I., Ostermann, N., et al. (1999). Modifying human thymidylate kinase to potentiate azidothymidine activation. The Journal of Biological Chemistry, 274(50), 35289-35292. doi:10.1074/jbc.274.50.35289.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-002C-2262-5 Version Permalink: https://hdl.handle.net/11858/00-001M-0000-002C-2263-3
Genre: Journal Article
Alternative Title : Modifying human thymidylate kinase to potentiate azidothymidine activation

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JBiolChem_274_1999_35289.pdf (Any fulltext), 263KB
 
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http://www.jbc.org/content/274/50/35289.full.pdf (Any fulltext)
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https://dx.doi.org/10.1074/jbc.274.50.35289 (Any fulltext)
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 Creators:
Brundiers, Ralf, Author
Lavie, Amon, Author
Veit, Thomas, Author
Reinstein, Jochen1, Author           
Schlichting, Ilme2, Author           
Ostermann, Nils, Author
Goody, Roger S.2, Author           
Konrad, Manfred, Author
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              
2Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              

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 Abstract: Based on the knowledge of the crystal structures of yeast and Escherichia coli thymidylate kinases (TmpKs) and the observation that TmpK from E. coli can phosphorylate azidothymidine monophosphate (AZT-MP) much more efficiently than either the yeast or the highly homologous human enzyme, we have engineered yeast and human TmpKs to obtain enzymes that have dramatically improved AZT-MP phosphorylation properties. These modified enzymes have properties that make them attractive candidates for gene therapeutic approaches to potentiating the action of AZT as an inhibitor of human immunodeficiency virus (HIV) replication. In particular, insertion of the lid domain of the bacterial TmpK into the human enzyme results in a pronounced change of the acceptance of AZT-MP such that it is now phosphorylated even faster than TMP.

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Language(s): eng - English
 Dates: 1999-09-301999-08-271999-12-10
 Publication Status: Issued
 Pages: 4
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 666589
DOI: 10.1074/jbc.274.50.35289
Other: 4389
 Degree: -

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Title: The Journal of Biological Chemistry
  Other : JBC
Source Genre: Journal
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Publ. Info: Baltimore, etc. : American Society for Biochemistry and Molecular Biology [etc.]
Pages: - Volume / Issue: 274 (50) Sequence Number: - Start / End Page: 35289 - 35292 Identifier: ISSN: 0021-9258
CoNE: https://pure.mpg.de/cone/journals/resource/954925410826_1