Abstract
Microbial transglutaminase (mTG) shows broad substrate specificity that is amenable to in vitro bio-conjugation applications. Herein, test proteins were genetically fused with peptide tags, followed by mTG-mediated propargylation of their reactive Gln residues. The propargylated proteins were subjected to copper-assisted azide-alkyne cycloaddition to demonstrate either fluorescent labelling or immobilization.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Alkynes / chemistry
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Azides / chemistry
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Catalysis
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Copper / chemistry
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Cycloaddition Reaction
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Enzymes, Immobilized / chemistry*
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Enzymes, Immobilized / metabolism
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Glutamine / chemistry*
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Glutamine / metabolism
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Oligopeptides / chemistry
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Pargyline / analogs & derivatives*
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Pargyline / chemistry
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Pargyline / metabolism
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Propylamines / chemistry*
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Propylamines / metabolism
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Proteins / chemistry*
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Proteins / metabolism
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Streptomycetaceae / enzymology
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Substrate Specificity
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Transglutaminases / metabolism*
Substances
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Alkynes
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Azides
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Enzymes, Immobilized
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Oligopeptides
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Propylamines
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Proteins
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Glutamine
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propargylamine
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tyrosyl-alanyl-glycine
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Copper
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Pargyline
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Transglutaminases