antibiotic-1233a and Liver-Neoplasms

antibiotic-1233a has been researched along with Liver-Neoplasms* in 1 studies

Other Studies

1 other study(ies) available for antibiotic-1233a and Liver-Neoplasms

Article	Year
Inhibition of 3-hydroxy-3-methylglutaryl coenzyme A synthase by antibiotic 1233A and other beta-lactones. Biochemical and biophysical research communications, 1990, Jun-15, Volume: 169, Issue:2 3-Hydroxy-3-methylglutaryl CoA synthase was shown to be inhibited in a time-dependent, irreversible manner by compounds containing the substituted beta-lactone functionality found in the natural product 1233A. The rate of inactivation (kinact) was found to approach the rate of catalysis (kcat). The inactivation was irreversible over several hours. A related compound lacking the hydroxymethyl substituent on the beta-lactone ring is a reversible inhibitor and is competitive with respect to acetylCoA. The results are consistent with beta-lactone ring opening by the active site Cys to form an enzyme bound thioester. Topics: Acetates; Animals; Anti-Bacterial Agents; Carcinoma, Hepatocellular; Cell Line; Cholestyramine Resin; Fatty Acids, Unsaturated; Humans; Hydroxymethylglutaryl-CoA Synthase; Kinetics; Lactones; Liver; Liver Neoplasms; Lovastatin; Molecular Structure; Oxo-Acid-Lyases; Rats; Structure-Activity Relationship; Tumor Cells, Cultured	1990

Article

Year

Inhibition of 3-hydroxy-3-methylglutaryl coenzyme A synthase by antibiotic 1233A and other beta-lactones.

Biochemical and biophysical research communications, 1990, Jun-15, Volume: 169, Issue:2

3-Hydroxy-3-methylglutaryl CoA synthase was shown to be inhibited in a time-dependent, irreversible manner by compounds containing the substituted beta-lactone functionality found in the natural product 1233A. The rate of inactivation (kinact) was found to approach the rate of catalysis (kcat). The inactivation was irreversible over several hours. A related compound lacking the hydroxymethyl substituent on the beta-lactone ring is a reversible inhibitor and is competitive with respect to acetylCoA. The results are consistent with beta-lactone ring opening by the active site Cys to form an enzyme bound thioester.

Topics: Acetates; Animals; Anti-Bacterial Agents; Carcinoma, Hepatocellular; Cell Line; Cholestyramine Resin; Fatty Acids, Unsaturated; Humans; Hydroxymethylglutaryl-CoA Synthase; Kinetics; Lactones; Liver; Liver Neoplasms; Lovastatin; Molecular Structure; Oxo-Acid-Lyases; Rats; Structure-Activity Relationship; Tumor Cells, Cultured

1990