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3-Methylcrotonyl-Coenzyme A Carboxylase Is a Component of the Mitochondrial Leucine Catabolic Pathway in Plants1

Marc D. Anderson2, Ping Che2, Jianping Song2, Basil J. Nikolau, and Eve Syrkin Wurtele*

Department of Botany (M.D.A., E.S.W.), and Department of Biochemistry and Biophysics (P.C., J.S., B.J.N.), Iowa State University, Ames, Iowa 50011

3-Methylcrotonyl-coenzyme A carboxylase (MCCase) is a mitochondrial biotin-containing enzyme whose metabolic function is not well understood in plants. In soybean (Glycine max) seedlings the organ-specific and developmentally induced changes in MCCase expression are regulated by mechanisms that control the accumulation of MCCase mRNA and the activity of the enzyme. During soybean cotyledon development, when seed-storage proteins are degraded, leucine (Leu) accumulation peaks transiently at 8 d after planting. The coincidence between peak MCCase expression and the decline in Leu content provides correlative evidence that MCCase is involved in the mitochondrial catabolism of Leu. Direct evidence for this conclusion was obtained from radiotracer metabolic studies using extracts from isolated mitochondria. These experiments traced the metabolic fate of [U-14C]Leu and NaH14CO3, the latter of which was incorporated into methylglutaconyl-coenzyme A (CoA) via MCCase. These studies directly demonstrate that plant mitochondria can catabolize Leu via the following scheme: Leu right-arrow alpha -ketoisocaproate right-arrow isovaleryl-CoA right-arrow 3-methylcrotonyl-CoA right-arrow 3-methylglutaconyl-CoA right-arrow 3-hydroxy-3-methylglutaryl-CoA right-arrow acetoacetate + acetyl-CoA. These findings demonstrate for the first time, to our knowledge, that the enzymes responsible for Leu catabolism are present in plant mitochondria. We conclude that a primary metabolic role of MCCase in plants is the catabolism of Leu.

1   This work was supported by National Science Foundation grant no. IBN-9507549 to E.S.W. and B.J.N. This is journal paper no. J-15558 of the Iowa Agriculture and Home Economics Experiment Station, Ames, IA; project nos. 2997 and 2913.
2   These authors contributed equally to this paper.
*   Corresponding author; e-mail mash{at}iastate.edu; fax 1-515-294-1337.

Plant Physiol. (1998) 118: 1127-1138
Copyright Clearance Center:   0032-0889/98/118//12
© 1998 American Society of Plant Physiologists




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