Substrate specificity of vaccinia virus thymidylate kinase
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چکیده
منابع مشابه
Substrate specificity of Epstein-Barr virus thymidine kinase.
Purified recombinant protein encoded by the BXLF-I open reading frame of the Epstein-Barr virus genome has thymidine kinase activity. The substrate behaviors of various nucleosides toward this enzyme were tested. Halogenated deoxyuridines, zidovudine, and bromovinyldeoxyuridine are efficient substrates, while acyclovir and dihydroxypropylmethylguanine are relatively poor substrates for the Epst...
متن کاملVaccinia virus encodes an active thymidylate kinase that complements a cdc8 mutant of Saccharomyces cerevisiae.
A vaccinia virus open reading frame (ORF) previously predicted to encode thymidylate kinase (TmpK) is shown to encode an active enzyme. A copy of the ORF, generated by polymerase chain reaction, was cloned into an Escherichia coli inducible expression vector. Cell extracts of E. coli expressing the vaccinia gene contained high levels of TmpK activity, whereas extracts of cells without the TmpK ...
متن کاملVaccinia virus encodes a thymidylate kinase gene: sequence and transcriptional mapping.
The nucleotide sequence and deduced amino acid sequence of a vaccinia virus gene from the SalI F fragment are shown. The predicted polypeptide shares 42% amino acid identity over a 200 amino acid region with Saccharomyces cerevisiae thymidylate kinase (TmpK) and has low homology with herpes simplex virus deoxypyrimidine kinase. Northern blotting and S1 nuclease protection showed that the TmpK g...
متن کاملMechanisms of Yersinia YopO kinase substrate specificity
Yersinia bacteria cause a range of human diseases, including yersiniosis, Far East scarlet-like fever and the plague. Yersiniae modulate and evade host immune defences through injection of Yersinia outer proteins (Yops) into phagocytic cells. One of the Yops, YopO (also known as YpkA) obstructs phagocytosis through disrupting actin filament regulation processes - inhibiting polymerization-promo...
متن کاملSubstrate specificity of protein kinase C inhibitors.
In the August issue of TiPS, Epand and Lester analysed the effect of the physicochemical properties of the membrane on protein kinase C activity. In addition to those substrates discussed that require the presence of Ca2+ and phospholipids, other substrates can be phosphorylated in the absence of these activators. It is possible that this differential substrate requirement could be exploited ph...
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ژورنال
عنوان ژورنال: FEBS Journal
سال: 2005
ISSN: 1742-464X,1742-4658
DOI: 10.1111/j.1742-4658.2005.05006.x