Bioscience, Biotechnology, and Biochemistry
Online ISSN : 1347-6947
Print ISSN : 0916-8451
Biochemistry & Molecular Biology Regular Papers
Biochemical Characterization of L-Carnitine Dehydrogenases from Rhizobium sp. and Xanthomonas translucens
Jiro ARIMAAkifumi UESUMIHitoshi MITSUZUMINobuhiro MORI
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2010 Volume 74 Issue 6 Pages 1237-1242

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Abstract

Recently, we obtained two L-carnitine dehydrogenases (CDHs) from soil isolates, Rhizobium sp. (Rs-CDH) and Xanthomonas translucens (Xt-CDH). The respective molecular masses of Rs-CDH and Xt-CDH were approximately 50 kDa and 37 kDa. In this study, the genes encoding both enzymes were cloned. Their primary structures exhibited high identities with those of 3-hydroxyacyl-CoA dehydrogenases. In addition, Rs-CDH had a 180-residue long extra sequence in its C-terminal region. Except for the initial 20 residues, the extra sequence exhibited similarity to thioesterase. The activity of Rs-CDH was affected only slightly by deletion of thioesterase domain, but it was eliminated by the deletion of the whole C-terminal extra sequence. A further deletion experiment indicated that the region of Ala330–Pro335 of Rs-CDH has important functions in catalytic activity. Moreover, based on the deletion experiment on Xt-CDH, the five-residue tail is considered to have a function similar to Ala330–Pro335 of Rs-CDH.

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© 2010 by Japan Society for Bioscience, Biotechnology, and Agrochemistry
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