Publication Type : Journal Article
Thematic Areas : Biotech
Publisher : Elsevier
Source : Biochimica et Biophysica Acta (BBA)-Protein Structure and Molecular Enzymology, Elsevier, Volume 1164, Number 1, p.108–112 (1993)
Url : http://www.sciencedirect.com/science/article/pii/016748389390118B
Keywords : Diallyl disulfide, Enzyme inactivation, HMG-CoA reductase, Intramolecular disulfide, Irreversible inactivation
Campus : Amritapuri
School : School of Biotechnology
Center : Biotechnology, Phytochemistry Labs
Department : biotechnology
Year : 1993
Abstract : Treatment with diallyl disulfide, a constituent of garlic oil, irreversibly inactivated microsomal and a soluble 50 kDa form of HMG-CoA reductase. No radioactivity was found to be protein-bound on treating the soluble enzyme with [35S]diallyl disulfide, indicating the absence of the mixed disulfide of the type allyl-S-S-protein. SDS-PAGE and Western blot analyses of the diallyl-disulfide-treated protein showed no traces of the dimer of the type protein-S-S-protein, but clearly indicated BME-reversible increased mobility, as expected of an intramolecular protein disulfide. The sulfhydryl groups, as measured by alkylation with iodo[2-14C]acetic acid, were found to decrease in the diallyl-disulfide-treated enzyme protein. Tryptic peptide analysis also gave support for the possible presence of disulfide-containing peptides in such a protein. It appears that diallyl disulfide inactivated HMG-CoA reductase by forming an internal protein disulfide that became inaccessible for reduction by DTT, and thereby retaining the inactive state of the enzyme.
Cite this Research Publication : R. V. Omkumar, Kadam, S. M., Banerji, A., and Ramasarma, T., “On the involvement of intramolecular protein disulfide in the irreversible inactivation of 3-hydroxy-3-methylglutaryl-CoA reductase by diallyl disulfide”, Biochimica et Biophysica Acta (BBA)-Protein Structure and Molecular Enzymology, vol. 1164, pp. 108–112, 1993.