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Fluorogenic probes for detecting deacylase and demethylase activity towards post-translationally-modified lysine residues.

ABSTRACT: Reversible enzymatic post-translational modification of the ε-amino groups of lysine residues (e.g. N-acylation reactions) plays an important role in regulating the cellular activities of numerous proteins. This study describes how enzyme catalyzed N-deprotection of lysine residues of non-fluorescent peptide-coumarin probes can be used to generate N-deprotected peptides that undergo spontaneous O- to N-ester transfer reactions (uncatalyzed) to generate a highly fluorescent N-carbamoyl peptide. This enables detection of enzyme catalyzed N-deacetylation, N-demalonylation, N-desuccinylation and N-demethylation reactions activities towards the N-modified lysine residues of these probes using simple 'turn on' fluorescent assays.

SUBMITTER: Hori Y

PROVIDER: S-EPMC8179349 | biostudies-literature | 2021 Jan

REPOSITORIES: biostudies-literature

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Fluorogenic probes for detecting deacylase and demethylase activity towards post-translationally-modified lysine residues.

Hori Yuichiro Y Nishiura Miyako M Tao Tomomi T Baba Reisuke R Bull Steven D SD Kikuchi Kazuya K

Chemical science 20210107 7

Reversible enzymatic post-translational modification of the ε-amino groups of lysine residues (e.g. N-acylation reactions) plays an important role in regulating the cellular activities of numerous proteins. This study describes how enzyme catalyzed N-deprotection of lysine residues of non-fluorescent peptide-coumarin probes can be used to generate N-deprotected peptides that undergo spontaneous O- to N-ester transfer reactions (uncatalyzed) to generate a highly fluorescent < ...[more]

PMID: 34164016

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