Need for Aromatic Residue at Position 115 for Proteolytic Activity Found by Site-directed Mutagenesis of Tryptophan 115 in Thermolysin
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概要
- 論文の詳細を見る
In thermolysin, tryptophan 115 seems to be at the S2 subsite. Trp-115 was replaced with tyrosine, phenylalanine, leucine, and valine during site-directed mutagenesis in order to evaluate the role of Trp-115 in the proteolytic activity of thermolysin. The mutant enzymes with Tyr-115 or Phe-115 had as much proteolytic activity as the wild-type enzyme, but the other two mutant enzymes had no activity. We found earlier that the substitution of Trp-115 with alanine, glutamic acid, lysine, and glutamine cause the enzyme to lose all activity, so an aromatic amino acid at position 115 seems to be essential for thermolysin.
- 社団法人日本農芸化学会の論文
- 1998-04-23
著者
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Kubo Motoki
Department Of Bioscience And Technology Faculty Of Science And Engineering Ritsumeikan University
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Kubo Motoki
Department Of Chemistry And Biochemistry Numazu College Of Technology:(present Address) Faculty Of S
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INOUYE Kuniyo
Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University
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Kubo Motoki
Department Of Bioscience & Technology Faculty Of Science & Engineering Ritsumeikan Universit
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Inouye Kuniyo
Division Of Applied Life Sciences Graduate School Of Agricultur Kyoto University
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MAZDA Nozomi
Department of Chemistry and Biochemistry, Numazu College of Technology
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Inouye Kuniyo
Division If Applied Life Sciences Graduate School Of Agriculture Kyoto University
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Mazda Nozomi
Department Of Chemistry And Biochemistry Numazu College Of Technology
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