Date of Award

Summer 1992

Document Type

Thesis

Degree Name

Master of Science (MS)

Department

Chemistry & Biochemistry

Program/Concentration

Chemistry

Committee Director

Laura K. Moen

Committee Member

Mark S. Elliot

Committee Member

Patricia A. Pleban

Committee Member

Roy L. Williams

Call Number for Print

Special Collections LD4331.C45H43

Abstract

The human immunodeficiency virus (HIV) reverse transcriptase (RT) (EC 2.7.7.49) is the central replication enzyme for HIV. In general, the kinetic mechanism for this and all other polymerases involves the ordered binding of two substrates: a primer-template (PT) followed by a deoxyribonucleoside triphosphate (dNTP). Previous investigations prompted this research when it was discovered that the substrate dNTP, in absence of PT, could protect a recombinant c-terminal mutant HIV-1 RT from inhibition by pyridoxal-5'-monophosphate (PLP), an active-site dNTP inhibitor. In contrast, the non-mutant recombinant HIV-1 RT required both substrates for protection from PLP inhibition. This investigation sought to determine if this c-terminal mutant RT is randomly binding the two substrates given the fact that the non-mutant RT is known to require PT binding before dNTP binding. The results of this investigation determined that the c-terminal mutant RT retains the ordered binding of substrates. Additionally, it was discovered that the c-terminal mutant RT has lost appreciable binding affinity for the PT substrate as compared to the non-mutant recombinant HIV-1 RT.

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DOI

10.25777/g7dt-8v74

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