Conversion of the Cleavage Specificity of Subtilisin YaB on Oxidized Insulin Chains to an Elastase-like Specificity by Replacement of Gly124 with Ala
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- MEI Hui-Ching
- <i>Institute of Biochemistry, National Yang-Ming University</i> <i>Department of Medical Technology, China Medical College</i>
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- LI Ywan-Feng
- <i>Institute of Biochemistry, National Yang-Ming University</i>
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- HSU Chi-Cheng
- <i>Institute of Biochemistry, National Yang-Ming University</i>
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- TSAI Ying-Chieh
- <i>Institute of Biochemistry, National Yang-Ming University</i>
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- TAKAGI Hiroshi
- <i>Department of Bioscience, Fukui Prefectural University</i>
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Abstract
Replacement of Gly124 on the S1 pocket of subtilisin YaB with Ala changed the cleavage pattern on oxidized insulin B-chain from the subtilisin type to the elastase type. The initial cleavage site in the B-chain shifted from L15-Y16 for wild-type YaB to A14-L15 for the G124A mutant. Upon complete hydrolysis with the G124A mutant, four of the six major cleavage sites on the B-chain were identical to porcine pancreatic elastase cleavage sites.<br>
Journal
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- Bioscience, Biotechnology, and Biochemistry
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Bioscience, Biotechnology, and Biochemistry 67 (7), 1601-1604, 2003
Japan Society for Bioscience, Biotechnology, and Agrochemistry
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Details 詳細情報について
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- CRID
- 1390001206473763200
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- NII Article ID
- 110002694273
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- NII Book ID
- AA10824164
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- COI
- 1:CAS:528:DC%2BD3sXmtFeks78%3D
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- ISSN
- 13476947
- 09168451
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- NDL BIB ID
- 6622282
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- PubMed
- 12913311
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- Text Lang
- en
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- Data Source
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- JaLC
- NDL
- Crossref
- PubMed
- CiNii Articles
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- Abstract License Flag
- Disallowed