Firefly luciferin methyl ester illuminates the activity of multiple serine hydrolases

Innus Mohammad; Kate L. Liebmann; Stephen C. Miller

doi:10.1039/D3CC02540C

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Firefly luciferin methyl ester illuminates the activity of multiple serine hydrolases†

Innus Mohammad,

^a Kate L. Liebmann^a and Stephen C. Miller

*^a

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* Corresponding authors

^a Department of Biochemistry and Molecular Biotechnology, UMass Chan Medical School, 364 Plantation St., Worcester, MA 01605, USA
E-mail: Stephen.miller@umassmed.edu

Abstract

Firefly luciferin methyl ester is hydrolyzed by monoacylglycerol lipase MAGL, amidase FAAH, poorly-characterized hydrolase ABHD11, and hydrolases known for S-depalmitoylation (LYPLA1/2), not just esterase CES1. This enables activity-based bioluminescent assays for serine hydrolases and suggests that the ‘esterase activity’ responsible for hydrolyzing ester prodrugs is more diverse than previously supposed.

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Article information

DOI: https://doi.org/10.1039/D3CC02540C
Article type: Communication
Submitted: 26 May 2023
Accepted: 14 Jun 2023
First published: 14 Jun 2023

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Chem. Commun., 2023,59, 8552-8555

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Firefly luciferin methyl ester illuminates the activity of multiple serine hydrolases

I. Mohammad, K. L. Liebmann and S. C. Miller, Chem. Commun., 2023, 59, 8552 DOI: 10.1039/D3CC02540C

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Chemical Communications

Firefly luciferin methyl ester illuminates the activity of multiple serine hydrolases†

Abstract

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Firefly luciferin methyl ester illuminates the activity of multiple serine hydrolases

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