Engineering proteases with altered specificity

Recent analysis of the crystal structures, both of the retroviral aspartyl proteases from Rous sarcoma virus and human immunodeficiency virus type 1 and of the serine proteases subtilisin and α-lytic protease, has enabled the rational design of mutations in the substrate-binding pocket of these enzy...

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Veröffentlicht in:	Current opinion in biotechnology 1994, Vol.5 (4), p.403-408
Hauptverfasser:	Leis, Jonathan P, Cameron, Craig E
Format:	Artikel
Sprache:	eng
Schlagworte:	Aspartic Acid Endopeptidases - genetics Aspartic Acid Endopeptidases - metabolism Bacteria - enzymology human immunodeficiency virus 1 Models, Molecular Mutagenesis Protein Engineering Retroviridae - enzymology Rous sarcoma virus Serine Endopeptidases - genetics Serine Endopeptidases - metabolism Structure-Activity Relationship Substrate Specificity
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