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In plants a putative isovaleryl-CoA-dehydrogenase is located in mitochondria.
Allgemeine Botanik, Universität Ulm, Germany.
In plants the degradation pathways of branched-chain amino acids have remained somewhat unclear with respect to both their biochemistry and their intracellular location. While biochemical evidence has localized some of the catabolic enzymes in peroxisomes/glyoxysomes, others cofractionate with mitochondria. We have now identified a candidate protein and corresponding cDNA for an enzyme of the leucine catabolic pathway, the isovaleryl-CoA-dehydrogenase (IVD). This polypeptide is a member of the acyl-CoA-dehydrogenase (ACDH) family and is encoded in the nuclear genome of Arabidopsis thaliana. Expression of the putative IVD gene in pea seedlings is documented by western blot analyses with an antibody against the mammalian IVD. Subcellular fractionation identifies the putative IVD enzyme in the mitochondrion. This localization suggests that in plants mitochondria contain at least part of the branched-chain amino acid degradation pathway(s).
PMID: 10380813 [PubMed - indexed for MEDLINE]
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Cited by 3 PubMed Central articles
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The branched-chain amino acid transaminase gene family in Arabidopsis encodes plastid and mitochondrial proteins.
Diebold R, Schuster J, Däschner K, Binder S.
Plant Physiol. 2002 Jun; 129(2):540-50.
[Plant Physiol. 2002]
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The mitochondrial isovaleryl-coenzyme a dehydrogenase of arabidopsis oxidizes intermediates of leucine and valine catabolism.
Däschner K, Couée I, Binder S.
Plant Physiol. 2001 Jun; 126(2):601-12.
[Plant Physiol. 2001]
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Purification and characterization of a novel pumpkin short-chain acyl-coenzyme A oxidase with structural similarity to acyl-coenzyme A dehydrogenases.
De Bellis L, Gonzali S, Alpi A, Hayashi H, Hayashi M, Nishimura M.
Plant Physiol. 2000 May; 123(1):327-34.
[Plant Physiol. 2000]