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Measurement of ALA synthase activity.

P R Sinclair¹, N Gorman, N W Cornell

¹VA Medical Center, White River Junction, Vermont, USA.

Current Protocols in Toxicology

|October 19, 2010

Summary

δ-aminolevulinate synthase, the key enzyme in heme synthesis, is regulated by heme and inducible by drugs. Assays were developed to measure its activity using radiometric or colorimetric methods.

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Area of Science:

Biochemistry
Enzymology
Cellular Metabolism

Background:

δ-aminolevulinate (ALA) synthase is the rate-limiting enzyme in heme biosynthesis.
Heme synthesis is tightly regulated, with ALA synthase being inducible by various agents and feedback-inhibited by heme.
Understanding ALA synthase activity is crucial for studying heme metabolism and related disorders.

Purpose of the Study:

To describe and validate methods for assaying δ-aminolevulinate (ALA) synthase activity.
To provide tools for researchers studying heme synthesis and its regulation.
To facilitate the investigation of factors affecting ALA synthase function.

Main Methods:

A radiometric assay utilizing [¹⁴C]succinate as a substrate to quantify ALA synthase activity.
A colorimetric assay based on the chemical conversion of ALA to a pyrrole derivative for enzyme activity measurement.
Standard biochemical and enzymatic assay techniques.

Main Results:

Established protocols for both radiometric and colorimetric measurement of ALA synthase activity.
Demonstrated the feasibility of using [¹⁴C]succinate for radiometric detection.
Validated a colorimetric approach for ALA detection, offering an alternative assay method.
Provided a comprehensive description of two distinct methods for assessing ALA synthase enzyme kinetics.

Conclusions:

Two reliable assay methods, radiometric and colorimetric, have been developed for δ-aminolevulinate synthase.
These assays provide valuable tools for researchers investigating heme biosynthesis and its regulation.
The described methods enable detailed studies on the induction and feedback inhibition of ALA synthase.

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