| A mutant leucine aminopeptidase from Streptomyces cinnamoneus with enhanced L: -aspartyl L: -amino acid methyl ester synthetic activity. | |
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MedLine Citation:
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PMID: 22354473 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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L: -Aspartyl L: -amino acid methyl ester was synthesized using a mutant of a thermostable leucine aminopeptidase from Streptomyces cinnamoneus, D198 K SSAP, obtained in previously. A peptide of high-intensity sweetener, L: -aspartyl-L: -phenylalanine methyl ester, was selected as a model for demonstrating the synthesis of L: -aspartyl L: -amino acid methyl ester. The hydrolytic activities of D198 K SSAP toward L: -aspartyl-L: -phenylalanine and its methyl ester were, respectively, 74-fold and fourfold higher than those of wild type. Similarly, the initial rate of the enzyme for L: -aspartyl-L: -phenylalanine methyl ester synthesis was over fivefold higher than that of wild-type SSAP in 90% methanol (v/v) in a one-pot reaction. Furthermore, other L: -aspartyl L: -amino acid methyl esters were synthesized efficiently using D198 K SSAP. Results show that the substitution of Asp198 of SSAP with Lys is effective for synthesizing L: -aspartyl L: -amino acid methyl ester. |
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Authors:
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Jiro Arima; Mirai Kono; Manami Kita; Nobuhiro Mori |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2012-2-22 |
Journal Detail:
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Title: Biotechnology letters Volume: - ISSN: 1573-6776 ISO Abbreviation: - Publication Date: 2012 Feb |
Date Detail:
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Created Date: 2012-2-22 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 8008051 Medline TA: Biotechnol Lett Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Affiliation:
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Department of Agricultural, Biological, and Environmental Sciences, Faculty of Agriculture, Tottori University, Tottori, 680-8553, Japan, arima@muses.tottori-u.ac.jp. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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