Template-binding site of AMV reverse transcriptase and inactivation of the enzyme by N-ethylmaleimide

Parnaik, Veena K. ; Das, Mukkattu Ramachandra (1981) Template-binding site of AMV reverse transcriptase and inactivation of the enzyme by N-ethylmaleimide Biochimica et Biophysica Acta, 655 (2). pp. 181-188. ISSN 0005-2787

Full text not available from this repository.

Official URL: http://linkinghub.elsevier.com/retrieve/pii/000527...

Related URL: http://dx.doi.org/10.1016/0005-2787(81)90007-1

Abstract

N-Ethylmaleimide, a sulfhydryl-specific reagent, strongly inhibits AMV reverse transcriptase by specifically interfering with the template-binding site of the enzyme. However, the kinetics of inhibition differ widely with the composition and structure of the templates employed. The copying of templates with multiple 3'-hydroxyl termini appeared to be more susceptible to N-ethylmaleimide treatment, suggesting that the reagent may interfere with initiation of DNA synthesis. The ability of a template bound to enzyme prior to N-ethylmaleimide treatment to protect against inactivation of copying of other templates also, implies a common binding site for the different templates. Template exchange experiments demonstrated competition between activated calf thymus DNA and rAn · dT12-18 for binding to the enzyme. Thus, templates varying widely in composition and conformation appear to bind at a common site on reverse transcriptase. The experimental data also show suggestive evidence for small but finite differences in the requirements for optimal binding for templates of different structures.

Item Type:Article
Source:Copyright of this article belongs to Elsevier Science.
Keywords:Reverse Transcriptase; Template-binding Site; Sulfhydryl Group Inhibition
ID Code:8524
Deposited On:27 Oct 2010 06:22
Last Modified:26 Dec 2011 13:29

Repository Staff Only: item control page