PMID: 9182995May 1, 1997Paper

Characterization of human and pig kidney long-chain-acyl-CoA dehydrogenases and their role in beta-oxidation

European Journal of Biochemistry
M EderS Ghisla

Abstract

Long-chain-acyl-CoA dehydrogenase (LCADH) has been produced by recombinant techniques from the human cDNA and purified after expression in Escherichia coli. Pig kidney LCADH was purified using an optimized method which also produces apparently pure short-chain-acyl-CoA dehydrogenase (SCADH) and medium-chain-acyl-CoA dehydrogenase (MCADH) in good yields. LCADH from both sources has a maximal turnover rate (Vmax of 650-700 min(-1) at pH 7.6) with the best substrates, which is approximately fivefold higher than reported previously. The human enzyme has an approximately fivefold higher Km compared with the pig kidney enzyme with substrates of chain length from C10 to C18 and a significantly different dependence of Vmax on the chain length. Pig kidney LCADH has a similar Vmax/Km with C10 to C14 substrates as MCADH does with C6 to C10 substrates. Recombinant human LCADH, however, is significantly less efficient (approximately fourfold with C12) than purified pig kidney enzyme. We conclude that human LCADH is either quantitatively less important in beta-oxidation than in the pig, or that post-translational modifications, not present in the recombinant human enzyme, are required to optimize human LCADH activity. Our results demonstrate...Continue Reading

References

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Jul 1, 1997·European Journal of Biochemistry·E ThorelliB Dahlbäck
Jan 13, 1998·Biological Chemistry·P MacherouxS Ghisla

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Citations

Dec 23, 1998·Proceedings of the National Academy of Sciences of the United States of America·D M KurtzP A Wood
Nov 1, 2007·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·Morris A KostiukLuc G Berthiaume
Sep 11, 2010·Journal of Biomedical Science·Svend Høime HansenNiels Grunnet
Mar 29, 2000·Critical Reviews in Clinical Laboratory Sciences·M J BennettA W Strauss

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