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爱泼斯坦-巴尔病毒胸苷激酶的底物特异性

Substrate specificity of Epstein-Barr virus thymidine kinase.

作者信息

Tung P P, Summers W C

机构信息

Department of Therapeutic Radiology, Yale University School of Medicine, New Haven, Connecticut 06520-8040.

出版信息

Antimicrob Agents Chemother. 1994 Sep;38(9):2175-9. doi: 10.1128/AAC.38.9.2175.

DOI:10.1128/AAC.38.9.2175
PMID:7811040
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC284705/
Abstract

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 Epstein-Barr virus thymidine kinase.

摘要

由爱泼斯坦-巴尔病毒基因组的BXLF-I开放阅读框编码的纯化重组蛋白具有胸苷激酶活性。测试了各种核苷对该酶的底物行为。卤代脱氧尿苷、齐多夫定和溴乙烯基脱氧尿苷是有效的底物，而阿昔洛韦和二羟丙基甲基鸟嘌呤是爱泼斯坦-巴尔病毒胸苷激酶相对较差的底物。

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