A mutant leucine aminopeptidase from Streptomyces cinnamoneus with enhanced L-aspartyl L-amino acid methyl ester synthetic activity

Biotechnology Letters
Jiro ArimaNobuhiro Mori

Abstract

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.

References

Aug 1, 1970·European Journal of Biochemistry·K Morihara, H Tsuzuki
Sep 1, 1980·Journal of Biochemistry·T Oka, K Morihara
Aug 1, 2002·Biotechnology and Applied Biochemistry·Diana KühnRenate Ulbrich-Hofmann
Jan 20, 2010·Protein Engineering, Design & Selection : PEDS·Hiroyasu OginoNoriyuki Doukyu

Related Concepts

NutraSweet
Hydrolysis
Methoxyleucine Aminopeptidase
Streptomyces
Amino Acid Substitution
Missense Mutation
Mutant Proteins
Methanol
Esters
Leucine Aminopeptidase

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