PMID: 8961352Nov 1, 1996Paper

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

Protein Engineering
Péter BagossiJózsef Tözsér

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.

Citations

Sep 22, 1999·European Journal of Biochemistry·P BorossJ Tözsér
Oct 25, 2000·Protein Science : a Publication of the Protein Society·K StrisovskyH G Kräusslich
Oct 26, 2005·Protein Expression and Purification·Péter BorossPéter Bagossi
Jun 15, 2011·The Journal of Physical Chemistry. B·J GarrecP Fleurat-Lessard
Jan 6, 2000·FEBS Letters·G FenyöfalviJ Tözsér
Jul 4, 1997·The Journal of Biological Chemistry·J TözsérS Oroszlan

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