       Document 0829
 DOCN  M9460829
 TI    The catalytic properties of the reverse transcriptase of the lentivirus
       equine infectious anemia virus.
 DT    9404
 AU    Rubinek T; Loya S; Shaharabany M; Hughes SH; Clark PK; Hizi A;
       Department of Cell Biology and Histology, Sackler School of; Medicine,
       Tel Aviv University, Israel.
 SO    Eur J Biochem. 1994 Feb 1;219(3):977-83. Unique Identifier : AIDSLINE
       MED/94155905
 AB    The reverse transcriptase (RT) of equine infectious anemia virus (EIAV)
       shares sequence similarity with the RTs of other lentiviruses,
       particularly with the RTs of human immunodeficiency viruses types 1 and
       2 (HIV-1 and HIV-2, respectively), the causative agents of acquired
       immunodeficiency syndrome (AIDS). There is a 41-42% sequence identity
       between EIAV RT and both HIV RTs (which have 61% sequence identity to
       each other). We have compared the enzymic properties of EIAV RT with
       those of HIV-1 RT. Several aspects of the activities of EIAV RT differ
       from the corresponding activities of HIV-1 RT. There are significant
       differences in the inhibition of the DNA polymerase activities by the
       deoxynucleoside triphosphate analogs, 3'-azido-2,3'-dideoxythymidine
       triphosphate, dideoxyTTP and dideoxyGTP and by the nonnucleoside
       inhibitor, tetrahydroimidazo[4,5,1-jk-1,4]benzodiazepin-2-(1H)-one and
       thione; in the dependence of DNA polymerase and RNase H activities on
       pH; in the inhibition of the DNA polymerase activities by the
       thiol-specific reagent N-ethylmaleimide; in the specific DNA polymerase
       activity; in the inhibition of the ribonuclease H activity by the zinc
       chelator orthophenanthroline. However, there are several cases in which
       EIAV RT and HIV-1 RT are more similar than was previously found for
       HIV-1 RT and HIV-2 RT. These include the Km values for the DNA
       polymerase activities, the heat stability of the DNA polymerase
       functions and the specific activity of the RNase H function.
 DE    Antiviral Agents/PHARMACOLOGY  Benzodiazepines/PHARMACOLOGY  Catalysis
       Comparative Study  DNA Polymerases/METABOLISM  Enzyme Stability
       Ethylmaleimide/PHARMACOLOGY  Heat  Hydrogen-Ion Concentration
       Imidazoles/PHARMACOLOGY  Infectious Anemia Virus, Equine/*ENZYMOLOGY
       Phenanthrolines/PHARMACOLOGY  Recombinant Proteins/METABOLISM  Reverse
       Transcriptase/ANTAGONISTS & INHIB/*METABOLISM  Ribonuclease H, Calf
       Thymus/METABOLISM  Support, U.S. Gov't, P.H.S.  JOURNAL ARTICLE

       SOURCE: National Library of Medicine.  NOTICE: This material may be
       protected by Copyright Law (Title 17, U.S.Code).

