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Review
. 2014 Mar;47(3):149-57.
doi: 10.5483/bmbrep.2014.47.3.264.

Small-molecule probes elucidate global enzyme activity in a proteomic context

Jun-Seok Lee  1 , Young-Hwa Yoo  2 , Chang No Yoon  2
Affiliations
Review

Small-molecule probes elucidate global enzyme activity in a proteomic context

Jun-Seok Lee et al. BMB Rep. 2014 Mar.

Abstract

The recent dramatic improvements in high-resolution mass spectrometry (MS) have revolutionized the speed and scope of proteomic studies. Conventional MS-based proteomics methodologies allow global protein profiling based on expression levels. Although these techniques are promising, there are numerous biological activities yet to be unveiled, such as the dynamic regulation of enzyme activity. Chemical proteomics is an emerging field that extends these types proteomic profiling. In particular, activity-based protein profiling (ABPP) utilizes small-molecule probes to monitor enzyme activity directly in living intact subjects. In this mini-review, we summarize the unique roles of small-molecule probes in proteomics studies and highlight some recent examples in which this principle has been applied.

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Figures

Fig. 1.
Fig. 1.. Three strategies to design activity-based probes and general workflow of activity-based protein profiling.
Fig. 2.
Fig. 2.. Enzymatic reaction mediated bio-imaging applications. left: Selective direct labeling of target protein; right: Non-selective enzymatic labeling of adjacent proteins.
See this image and copyright information in PMC

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