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PMID: 2015912 Published · ppublish English Comparative Study Journal Article Research Support, U.S. Gov't, P.H.S.

Comparison of the HIV-1 and HIV-2 proteinases using oligopeptide substrates representing cleavage sites in Gag and Gag-Pol polyproteins.

FEBS letters ·Vol. 281 ·No. 1-2 ·1991-04-09 ·Pages 77-80

Tözsér J, Bláha I, Copeland TD, Wondrak EM, Oroszlan S

Abstract

The substrate specificity of the human immunodeficiency virus type 1 (HIV-1) and type 2 (HIV-2) proteinases was compared using oligopeptides corresponding to cleavage sites in the Gag and Gag-Pol polyproteins of both viruses. All peptides mimicking cleavage sites at the junction of major functional protein domains were correctly cleaved by both enzymes. However, some other peptides thought to represent secondary cleavage sites remained intact. The kinetic parameters (Km and kcat) obtained for the different substrates showed several hundred-fold variation but were similar for the same substrate.

MeSH Terms
Amino Acid Sequence Fusion Proteins, gag-pol/metabolism Gene Products, gag/metabolism HIV Protease/metabolism HIV-1/enzymology HIV-2/enzymology Molecular Sequence Data Oligopeptides/metabolism Recombinant Proteins/metabolism Substrate Specificity
Chemicals
Fusion Proteins, gag-pol Gene Products, gag Oligopeptides Recombinant Proteins HIV Protease
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Tözsér J
Laboratory of Molecular Virology and Carcinogenesis, ABL-Basic Research Program, NCI-Frederick Cancer Research and Development Center, MD 21702.
Bláha I
Copeland T D
Wondrak E M
Oroszlan S
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
1991-04-09
Pages
77-80
Language
English
Region
England
NLM ID
0155157
Subset
IM
Grants
NCI NIH HHS · N01-CO-74101 · United States
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