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Issue 23, 2016
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Discovery of a pyruvylated peptide-metabolizing enzyme using a fluorescent substrate-based protein discovery technique

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Abstract

We employed a fluorescent substrate-based target discovery approach to screen the enzymome for metabolic activity towards pyruvyl-amidated peptides, and identified an acylamino acid-releasing enzyme (APEH). Cells overexpressing APEH exhibited higher metabolic activity towards the probe, N-pyruvyl-leucyl-7-amido-4-methylcoumarin (Pyr-Leu-AMC), while the selective APEH inhibitor AA74-1 blocked the reaction. Metabolism of various pyruvylated peptides in liver lysate was almost completely blocked by AA74-1. Pyruvyl peptides are synthesized in response to oxidative stress, but their biological role is poorly understood; identification of a key contributor to their metabolism should stimulate research on pathways leading from oxidative stress to protein modification and biological output.

Graphical abstract: Discovery of a pyruvylated peptide-metabolizing enzyme using a fluorescent substrate-based protein discovery technique

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Supplementary files

Article information


Submitted
27 Jan 2016
Accepted
19 Feb 2016
First published
22 Feb 2016

Chem. Commun., 2016,52, 4377-4380
Article type
Communication

Discovery of a pyruvylated peptide-metabolizing enzyme using a fluorescent substrate-based protein discovery technique

K. Yoshioka, T. Komatsu, K. Hanaoka, T. Ueno, T. Terai, T. Nagano and Y. Urano, Chem. Commun., 2016, 52, 4377
DOI: 10.1039/C6CC00829A

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