Activity of linked HIV-1 proteinase dimers containing mutations in the active site region

P. Bagossi, Yin Shyun E Cheng, Stephen Oroszlan, J. Tőzsér

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

Mutations were introduced into the active site triplet (Asp-Thr-Gly) of one or both subunits of a linked dimer of human immunodeficiency virus type 1 proteinase. Mutation of Thr to Ser in one or both subunits did not alter the activity of the enzyme substantially, whereas its mutation to Asn in one subunit caused a dramatic decrease in catalytic efficiency. Mutation of Gly to Val in one subunit also yielded an enzyme with very low activity. The enzymes containing Thr → Asn and Gly → Val mutations in both subunits resulted in inactive enzymes, based on their inability to self-process and on assay with an oligopeptide substrate. The dramatic decrease in enzyme efficiency of the mutants was interpreted using molecular models of the enzymes.

Original languageEnglish
Pages (from-to)997-1003
Number of pages7
JournalProtein Engineering
Volume9
Issue number11
Publication statusPublished - Nov 1996

Fingerprint

HIV Protease
Dimers
HIV-1
Catalytic Domain
Peptide Hydrolases
Enzymes
Mutation
Oligopeptides
Molecular Models
Viruses
Assays
Catalyst activity
Substrates

Keywords

  • Active site
  • Enzyme kinetics
  • Linked HIV proteinase dimer
  • Oligopeptide substrates

ASJC Scopus subject areas

  • Molecular Biology
  • Biochemistry

Cite this

Activity of linked HIV-1 proteinase dimers containing mutations in the active site region. / Bagossi, P.; Cheng, Yin Shyun E; Oroszlan, Stephen; Tőzsér, J.

In: Protein Engineering, Vol. 9, No. 11, 11.1996, p. 997-1003.

Research output: Contribution to journalArticle

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