A common active site model for catalysis by chorismate mutase-prephenate dehydrogenase
- 1 June 1979
- journal article
- research article
- Published by Elsevier in Journal of Theoretical Biology
- Vol. 78 (3), 393-403
- https://doi.org/10.1016/0022-5193(79)90338-2
Abstract
No abstract availableThis publication has 10 references indexed in Scilit:
- Kinetic studies on the reactions catalyzed by chorismate mutase-prephenate dehydrogenase from Aerobacter aerogenesBiochemistry, 1978
- Rearrangement of chorismate to prephenate. Use of chorismate mutase inhibitors to define the transition state structureBiochemistry, 1977
- Chorismate Mutase/Prephenate Dehydratase from Escherichia coli K12. Effects of Chemical Modification on the Enzymic Activities and Allosteric InhibitionEuropean Journal of Biochemistry, 1977
- Multifunctional ProteinsAnnual Review of Biochemistry, 1976
- Ground states of molecules. XXV. MINDO/3. Improved version of the MINDO semiempirical SCF-MO methodJournal of the American Chemical Society, 1975
- Transition-state stabilization and enzymic catalysis. Kinetic and molecular orbital studies of the rearrangement of chorismate to prephenateBiochemistry, 1973
- Studies on the relationship between the active sites of chorismate mutase-prephenate dehydrogenase from Escherichia coli or Aerobacter aerogenesBiochimica et Biophysica Acta (BBA) - Enzymology, 1972
- Characterisation of the subunits of chorismate mutase-prephenate dehydrogenase from Escherichia coli K12Biochimica et Biophysica Acta (BBA) - Protein Structure, 1971
- Studies on the subunit structure of chorismate mutase − prephenate dehydrogenase from Arobacter aerogenesBiochimica et Biophysica Acta (BBA) - Enzymology, 1970
- The Regulation of Biosynthesis of Aromatic Amino Acids and VitaminsCurrent Topics in Cellular Regulation, 1970