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β-Alanyl peptide synthesis by Streptomyces S9 aminopeptidase

Paper ID Volume ID Publish Year Pages File Format Full-Text
24400 43512 2010 7 PDF Available
β-Alanyl peptide synthesis by Streptomyces S9 aminopeptidase

Synthesis of β-alanine (β-Ala) containing dipeptide using S9 aminopeptidase from Streptomyces thermocyaneoviolaceus NBRC14271 (S9AP-St) was demonstrated with β-Ala-benzyl ester (-OBzl) and various l-aminoacyl derivatives. For synthesis of β-Ala-containing dipeptide, β-Ala-OBzl was used preferentially as the acyl donor for S9AP-St, producing synthesized dipeptides having β-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-β-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 β-Ala-OBzl to carnosine-OMe that was greater than 30%.

S9AP-St, S9 aminopeptidase from Streptomyces thermocyaneoviolaceus; β-Ala-BCAA, β-alanyl-branched chain amino acidS9 aminopeptidase; Aminolysis; β-Alanyl peptide; Streptomyces; Substrate specificity; Peptide synthesis
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β-Alanyl peptide synthesis by Streptomyces S9 aminopeptidase
Database: Elsevier - ScienceDirect
Journal: Journal of Biotechnology - Volume 147, Issue 1, 3 May 2010, Pages 52–58
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Physical Sciences and Engineering Chemical Engineering Bioengineering