DOI | Resolve DOI: https://doi.org/10.1016/S0006-291X(88)81175-6 |
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Author | Search for: Anand, N.; Search for: Stephen, E.; Search for: Narang, S. |
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Format | Text, Article |
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Abstract | The active site amino acids (Glull and Asp20) in T4-lysozyme have been mutated to their isosteric residues Gln or Asn and/or acidic residues such as Glu → Asp or Asp → Glu by the oligonucleotide-replacement method. Out of eight mutants so generated the mutant T4-lysozyme obtained from pTLY.Asp11 retains maximum amount of activity (∼16%), pTLY.Asn20 the least (0.9%) whereas pTLY.Gln11 lost completely. A systematic study of the active and inactive mutants thus generated supports the important role of Glu11 and Asp20 in T4-lysozyme activity as predicted in earlier studies. |
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Publication date | 1988-06-18 |
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Publisher | Elsevier |
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In | |
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Language | English |
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Peer reviewed | Yes |
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NRC number | ANAND1988 |
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NPARC number | 9379472 |
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Export citation | Export as RIS |
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Report a correction | Report a correction (opens in a new tab) |
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Record identifier | 08a319fc-b1ed-4a4e-8a62-0a31e313520b |
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Record created | 2009-07-10 |
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Record modified | 2020-03-17 |
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