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Coelenterazine sulfotransferase from Renilla muelleri.

George Tzertzinis¹, Brenda Baker¹, Jack Benner¹

¹New England Biolabs, Ipswich, Massachusetts, United States of America.

|October 17, 2022

Summary

This summary is machine-generated.

Researchers identified the gene for Renilla luciferin sulfokinase, an enzyme crucial for bioluminescence. This discovery enables new sensitive detection methods using the cloned enzyme.

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Area of Science:

Biochemistry
Molecular Biology
Marine Biology

Background:

Luciferin sulfokinase (coelenterazine sulfotransferase) activates the storage form of luciferin for bioluminescence.
The gene encoding this crucial enzyme in Renilla had not been previously identified.

Purpose of the Study:

To identify and clone the cDNA for coelenterazine sulfotransferase from Renilla.
To characterize the recombinant enzyme and demonstrate its utility in a bioluminescent assay.

Main Methods:

Combined proteomic (LC-MS/MS) and transcriptomic approaches were used.
Isoforms were identified by intersecting Renilla muelleri transcriptome with purified enzyme peptide sequences.
Two isoforms were expressed in E. coli and characterized.

Main Results:

Multiple coelenterazine sulfotransferase isoforms were identified in Renilla muelleri.
Recombinant enzymes expressed in E. coli exhibited comparable sulfotransferase activity to the native enzyme.
A sensitive bioluminescent assay for 3'-phosphoadenosine 5'-phosphate (PAP) was developed using the recombinant enzyme.

Conclusions:

The gene for Renilla coelenterazine sulfotransferase has been identified and cloned.
Recombinant isoforms are enzymatically active and suitable for biochemical studies.
The cloned enzyme facilitates a novel bioluminescent assay for PAP detection.