Liberation of lipoate by human serum lipoamidase from bovine heart pyruvate dehydrogenase

Biochemical and Biophysical Research Communications
J Oizumi, K Hayakawa

Abstract

Lipoamidase, which hydrolyses such substrates as lipoamide, lipoylmethyl ester, lipoyllysine, and lipoyl 4-aminobenzoate (LPAB), was purified from human serum through use of synthetic substrate LPAB. The purified human serum lipoamidase showed lipoyllysine hydrolase activity (Km = 435 microM, Vmax = 64.5 nmol/min per mg of protein). The purified enzyme did not liberate the free form of lipoic acid from bovine heart pyruvate dehydrogenase (PDH). PDH was hydrolyzed quantitatively by proteinase K to lipoyllysine, which was determined by the HPLC method. Although liberation of lipoate from various lengths of lipoyl-peptides has not been tested yet, it is likely that lipoamidase requires proteinase(s) before the liberation of free lipoic acid from the enzymes.

References

May 5, 1989·Journal of Chromatography·K Hayakawa, J Oizumi
Jun 27, 1989·Biochimica Et Biophysica Acta·J Oizumi, K Hayakawa
Jan 1, 1988·Enzyme·K Hayakawa, J Oizumi
May 1, 1988·Journal of Biochemistry·K Hayakawa, J Oizumi
Dec 2, 1988·Biochimica Et Biophysica Acta·K Hayakawa, J Oizumi

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Citations

Aug 31, 1990·Clinica Chimica Acta; International Journal of Clinical Chemistry·C L Garganta, B Wolf
May 29, 2010·Microbiology and Molecular Biology Reviews : MMBR·Maroya D Spalding, Sean T Prigge
Jan 1, 1997·European Journal of Clinical Chemistry and Clinical Biochemistry : Journal of the Forum of European Clinical Chemistry Societies·E A TerentyevaI Hibi
Dec 20, 2014·Cell·Rommel A MathiasIleana M Cristea
May 1, 1990·Archives of Biochemistry and Biophysics·J Oizumi, K Hayakawa

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