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• W2154764564 startingPage "2327" @default.
• W2154764564 abstract "A new S9 family aminopeptidase derived from the actinobacterial thermophile Acidothermus cellulolyticus was cloned and engineered into a transaminopeptidase by site-directed mutagenesis of catalytic Ser491 into Cys. The engineered biocatalyst, designated aminolysin-A, can catalyze the formation of peptide bonds to give linear homo-oligopeptides, hetero-dipeptides, and cyclic dipeptides using cost-effective substrates in a one-pot reaction. Aminolysin-A can recognize several C-terminal-modified amino acids, including the L- and D-forms, as acyl donors as well as free amines, including amino acids and puromycin aminonucleoside, as acyl acceptors. The absence of amino acid esters prevents the formation of peptides; therefore, the reaction mechanism involves aminolysis and not a reverse reaction of hydrolysis. The aminolysin system will be a beneficial tool for the preparation of structurally diverse peptide mimetics by a simple approach." @default.
• W2154764564 created "2016-06-24" @default.
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• W2154764564 date "2011-01-01" @default.
• W2154764564 modified "2023-09-27" @default.
• W2154764564 title "Peptide bond formation by aminolysin-A catalysis: A simple approach to enzymatic synthesis of diverse short oligopeptides and biologically active puromycins" @default.
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• W2154764564 doi "https://doi.org/10.1039/c0ob00403k" @default.
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• W2154764564 hasPublicationYear "2011" @default.
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