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- W2005417072 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." @default.
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- W2005417072 date "2010-06-23" @default.
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- W2005417072 title "Biochemical Characterization of<scp>L</scp>-Carnitine Dehydrogenases from<i>Rhizobium</i>sp. and<i>Xanthomonas translucens</i>" @default.
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- W2005417072 doi "https://doi.org/10.1271/bbb.100072" @default.
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