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

Laurence Arnold | Zendy; Simone Kunzelmann | Zendy; Martin R. Webb | Zendy; Ian A. Taylor | Zendy

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

Author(s) -

Laurence Arnold,

Simone Kunzelmann,

Martin R. Webb,

Ian A. Taylor

Publication year - 2014

Publication title -

antimicrobial agents and chemotherapy

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.07

H-Index - 259

eISSN - 1070-6283

pISSN - 0066-4804

DOI - 10.1128/aac.03903-14

Subject(s) - samhd1 , enzyme , nucleotide , biochemistry , biology , chemistry , reverse transcriptase , rna , gene

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.

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