There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.
Abstract
Several derivatives of levodopa have been shown to be potent inhibitors of the sulfhydryl
enzyme, RNA dependent DNA polymerase, reverse transcriptase (RT). In the presence
of the polyphenol oxidase, tyrosinase, the inhibitory values were between 10(-6) M
and 10(-5) M. Structure-activity studies revealed that active oxidation or reduction
was necessary for this potent inhibitory response. Spectrophotometric analysis showed
that the presence of both the quinone and quinol was required for maximum inhibitory
activity. These data suggest that the common intermediate of oxidation of quinols
or reduction of quinones (i.e., semiquinone) is the active species. The use of tyrosinase
provides a convenient model for the detection of the actual inhibitory interaction
of a free-radical (semiquinone) with a biologically important macromolecule, reverse
transcriptase.