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 |
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| container_title | Current opinion in biotechnology |
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| creator | Leis, Jonathan P Cameron, Craig E |
| description | 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 enzymes. Alterations in steady-state kinetic properties of the purified mutant enzymes have been detected
in vitro by following the cleavage of synthetic peptide substrates. These analyses have identified key amino acid residues in each of these enzymes that are involved in substrate specificity, and they have provided the foundation for the design of proteases with novel substrate specificities. |
| doi_str_mv | 10.1016/0958-1669(94)90049-3 |
| format | Article |
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| fulltext | fulltext |
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| ispartof | Current opinion in biotechnology, 1994, Vol.5 (4), p.403-408 |
| issn | 0958-1669 1879-0429 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | 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 |
| title | Engineering proteases with altered specificity |
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