b-Alanyl peptide synthesis by Streptomyces S9 aminopeptidase

Synthesis of b-alanine (b-Ala) containing dipeptide using S9 aminopeptidase from Streptomyces thermocyaneoviolaceus NBRC14271 (S9AP-St) was demonstrated with b-Ala-benzyl ester (-OBzl) and various l-aminoacyl derivatives. For synthesis of b-Ala-containing dipeptide, b-Ala-OBzl was used preferentiall...

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Bibliographic Details
Published inJournal of biotechnology Vol. 147; no. 1; pp. 52 - 58
Main Authors Arima, Jiro, Morimoto, Masazumi, Usuki, Hirokazu, Mori, Nobuhiro, Hatanaka, Tadashi
Format Journal Article
LanguageEnglish
Published 03.05.2010
Subjects
Biotechnology
Catalysis
Catalysts
Conversion ratio
Derivatives
Esters
Peptides
Streptomyces
Synthesis
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Summary:Synthesis of b-alanine (b-Ala) containing dipeptide using S9 aminopeptidase from Streptomyces thermocyaneoviolaceus NBRC14271 (S9AP-St) was demonstrated with b-Ala-benzyl ester (-OBzl) and various l-aminoacyl derivatives. For synthesis of b-Ala-containing dipeptide, b-Ala-OBzl was used preferentially as the acyl donor for S9AP-St, producing synthesized dipeptides having b-Ala-Xaa structure. In contrast, engineering of S9AP-St into "transaminopeptidase" by substitution of catalytic Ser with Cys - designated as aminolysin-S - produced only dipeptides having Xaa-b-Ala structure. Investigation of the specificity of S9AP-St toward acyl acceptors showed that S9AP has a broad substrate specificity toward various aminoacyl derivatives. Furthermore, S9AP-St produced carnosine methyl ester (-OMe) with a conversion ratio of b-Ala-OBzl to carnosine-OMe that was greater than 30%.
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ISSN:0168-1656
DOI:10.1016/j.jbiotec.2010.03.007