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A mutant leucine aminopeptidase from Streptomyces cinnamoneus with enhanced L: -aspartyl L: -amino acid methyl ester synthetic activity.
MedLine Citation:
PMID:  22354473     Owner:  NLM     Status:  Publisher    
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.
Jiro Arima; Mirai Kono; Manami Kita; Nobuhiro Mori
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-2-22
Journal Detail:
Title:  Biotechnology letters     Volume:  -     ISSN:  1573-6776     ISO Abbreviation:  -     Publication Date:  2012 Feb 
Date Detail:
Created Date:  2012-2-22     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  8008051     Medline TA:  Biotechnol Lett     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Department of Agricultural, Biological, and Environmental Sciences, Faculty of Agriculture, Tottori University, Tottori, 680-8553, Japan,
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