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Pea chloroplast carnitine acetyltransferase.

C Masterson¹, C Wood

¹Department of Biological and Nutritional Sciences, University of Newcastle, Newcastle upon Tyne, UK.

Proceedings. Biological Sciences

|February 12, 2000

Summary

Carnitine acetyltransferase (CAT) is present in pea chloroplasts. Its activity is sufficient to support fatty acid synthesis, confirming its role in this process.

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Area of Science:

Plant Biochemistry
Chloroplast Metabolism
Enzyme Function

Background:

The presence and function of carnitine acetyltransferase (CAT) within chloroplasts have been debated.
Carnitine acetyltransferase (CAT) catalyzes the reversible reaction between carnitine and acyl-CoA esters.
Understanding chloroplastic enzyme activity is crucial for elucidating plant metabolic pathways.

Purpose of the Study:

To definitively determine if chloroplasts contain carnitine acetyltransferase (CAT).
To ascertain if the detected CAT activity levels are adequate for fatty acid synthesis.
To investigate the localization and characteristics of chloroplastic CAT.

Main Methods:

Utilized a sensitive radioenzymatic assay with membrane-impermeable acetyl CoA on intact and ruptured Pisum sativum L. chloroplasts.
Partially purified the enzyme to enable spectrophotometric assays for detecting CAT activity in both forward and reverse reactions.
Determined optimal activity conditions (pH 8.5) and substrate specificity (C2-C4 acyl CoAs).

Main Results:

Carnitine acetyltransferase (CAT) activity was detected in pea chloroplasts, specifically on the stromal side of the envelope.
Enzyme activity was measurable only in ruptured chloroplasts, indicating compartmentalization.
Achieved rates of 100 nmol/min/mg protein, which is sufficient to support reported fatty acid synthesis rates from acetylcarnitine.

Conclusions:

Carnitine acetyltransferase (CAT) has been successfully demonstrated in pea chloroplasts.
The enzyme's activity level supports its proposed role in fatty acid synthesis.
Chloroplastic CAT exhibits specific substrate preferences and optimal activity at pH 8.5.

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