Aromatic inhibitors of dehydroquinate synthase: synthesis, evaluation and implications for gallic acid biosynthesis.
The role of the active site metal in determining binding to 3-dehydroquinate synthase has been examined. Protocatechuic acid, catechol, and derivatives of these aromatics were synthesized that shared the common element of an ortho dihydroxylated benzene ring. Inhibition constants were determined for each aromatic as well as the variation of this inhibition as a function of whether Co(+2) or Zn(+2) was the active site metal ion.
Chandran
S S
SS
Department of Chemistry, Michigan State University, East Lansing, MI 48823-1322, USA.
Frost
J W
JW
D016588:Anticarcinogenic Agents / Q000138:chemical synthesis / Q000494:pharmacology; D020134:Catalytic Domain; D002396:Catechols / Q000138:chemical synthesis / Q000494:pharmacology*; D003035:Cobalt; D004791:Enzyme Inhibitors / Q000138:chemical synthesis / Q000494:pharmacology; D004926:Escherichia coli / Q000201:enzymology; D005707:Gallic Acid / Q000378:metabolism; D062385:Hydroxybenzoates / Q000138:chemical synthesis / Q000494:pharmacology; D007700:Kinetics; D008667:Metalloproteins; D019761:Phosphorus-Oxygen Lyases / Q000037:antagonists & inhibitors*; D011485:Protein Binding; D015032:Zinc
D016588:Anticarcinogenic Agents; D002396:Catechols; D004791:Enzyme Inhibitors; D062385:Hydroxybenzoates; D008667:Metalloproteins; C009091:protocatechuic acid; D003035:Cobalt; D005707:Gallic Acid; C020001:3-dehydroquinate synthetase; D019761:Phosphorus-Oxygen Lyases; D015032:Zinc