A Continuous Enzyme-Coupled Assay for Triphosphohydrolase Activity of HIV-1 Restriction Factor SAMHD1

被引：34

作者：

Arnold, Laurence H. ^{[1
]}

Kunzelmann, Simone ^{[2
]}

Webb, Martin R. ^{[2
]}

Taylor, Ian A. ^{[1
]}

机构：

[1] Natl Inst Med Res, MRC, Div Mol Struct, London NW7 1AA, England

[2] Natl Inst Med Res, MRC, Div Phys Biochem, London NW7 1AA, England

来源：

ANTIMICROBIAL AGENTS AND CHEMOTHERAPY | 2015年 / 59卷 / 01期

基金：

英国医学研究理事会;

关键词：

REVERSE-TRANSCRIPTASE INHIBITORS; DEOXYNUCLEOSIDE TRIPHOSPHATE TRIPHOSPHOHYDROLASE; SACCHAROMYCES-CEREVISIAE; INORGANIC-PHOSPHATE; SOLUBLE EXOPOLYPHOSPHATASE; MITOCHONDRIAL-DNA; INFECTION; CELLS; PURIFICATION; REPLICATION;

D O I：

10.1128/AAC.03903-14

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

The development of deoxynucleoside triphosphate (dNTP)-based drugs requires a quantitative understanding of any inhibition, activation, or hydrolysis by off-target cellular enzymes. SAMHD1 is a regulatory dNTP-triphosphohydrolase that inhibits HIV-1 replication in human myeloid cells. We describe here an enzyme-coupled assay for quantifying the activation, inhibition, and hydrolysis of dNTPs, nucleotide analogues, and nucleotide analogue inhibitors by triphosphohydrolase enzymes. The assay facilitates mechanistic studies of triphosphohydrolase enzymes and the quantification of off-target effects of nucleotide-based antiviral and chemotherapeutic agents.

引用

页码：186 / 192

页数：7

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