ChemBioChem · 2010 · 32 citations · 14 references
Life SciencesBiochemistryMolecular BiologyBiocatalysisEnzymologyProtein BiochemistryPeptide ChemistryProtein GlycoengineeringProtein SynthesisCyclic PeptidesEnzymatic BiosynthesisGlycopeptide SynthesisPost-translationally Modified Peptide BiosynthesisPost-translationally Modified Peptides
The ability of microbial transglutaminase to ligate two polypeptides through glutamine and lysine residues was exploited to generate cyclic peptides. Peptides with an N-terminal short glutamine-donor sequence (Ala-Leu-Gln), a variable polypeptide linker and a C-terminal lysine residue could efficiently be cyclised by the enzyme. Detailed facts of importance to specialist readers are published as ”Supporting Information”. Such documents are peer-reviewed, but not copy-edited or typeset. They are made available as submitted by the authors. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.
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