Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:2.3.3.1 (citrate synthase)
 4,488 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Sulfoxides and sulfones were prepared by specific oxidation of 3-hydroxy-3-methylglutaryl-CoA-analogue CoA-thioether derivatives and their kinetic properties were determined with 3-hydroxy-3-methylglutaryl-CoA reductase. The oxidized CoA-thioether derivatives with a hydroxyl group at C3 were powerful competitive inhibitors, their Ki values being much smaller than the Km for 3-hydroxy-3-methylglutaryl-CoA. Sulfoxides and sulfones of substrate analogues of citrate synthase were also prepared. When tested in the appropriate reaction with citrate synthase, the sulfoxide and sulfone derivatives were competitive inhibitors, but their Ki values were greater than the Km values of the corresponding unmodified substrates.
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PMID:Inhibition of 3-hydroxy-3-methylglutaryl-CoA reductase and citrate synthase by sulfoxides and sulfones of substrate-analogue CoA-thioether derivatives. 785 98

Smith, Paul F. (University of South Dakota, Vermillion), and C. V. Henrikson. Comparative biosynthesis of mevalonic acid by Mycoplasma. J. Bacteriol. 89:146-153. 1965.-Three representative Mycoplasma, M. laidlawii strain B, M. gallisepticum strain J, and M. hominis strain 07, were examined for the presence or absence of enzymes associated with the biosynthetic pathway to mevalonic acid. M. laidlawii served as a control, because it synthesizes carotenoids from acetate. M. laidlawii was shown to contain a specific acetokinase and phosphotransacetylase for the synthesis of acetyl coenzyme A, and a beta-ketothiolase and coenzyme A transferase for the synthesis of acetoacetyl coenzyme A. M. gallisepticum contained a specific acetokinase, phosphotransacetylase, and possibly an aceto coenzyme A kinase forming acetyl coenzyme A; it also contained a beta-ketothiolase, a coenzyme A transferase, and a coenzyme A transphorase forming acetoacetyl coenzyme A directly or indirectly. The beta-ketothiolase of M. gallisepticum was not affected by iodoacetamide, in contrast to the other two strains. M. laidlawii exhibited beta-hydroxy-beta-methylglutaryl coenzyme A condensing enzyme, and M. hominis did not. This activity of M. gallisepticum was masked by thiolase activity. M. laidlawii and M. gallisepticum contained a nicotinamide adenine dinucleotide phosphate-linked beta-hydroxy-beta-methylglutaryl coenzyme A reductase, and M. hominis did not. C(14)-labeled acetate was incorporated into mevalonic acid only by M. laidlawii and M. gallisepticum. The lack of beta-hydroxy-beta-methylglutaryl coenzyme A condensing enzyme and reductase activities in M. hominis explains its growth requirement for sterol. The enzymatic block in M. gallisepticum must occur after mevalonic acid in the biosynthetic pathway to terpenoids.
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PMID:COMPARATIVE BIOSYNTHESIS OF MEVALONIC ACID BY MYCOPLASMA. 1425 55