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4. Chorismate mutase-prephenate dehydrogenase from Escherichia coli. 1. Kinetic characterization of the dehydrogenase reaction by use of alternative substrates. Turnbull J; Cleland WW; Morrison JF Biochemistry; 1990 Nov; 29(44):10245-54. PubMed ID: 2271652 [TBL] [Abstract][Full Text] [Related]
5. Kinetic studies on the reactions catalyzed by chorismate mutase-prephenate dehydrogenase from Aerobacter aerogenes. Heyde E; Morrison JF Biochemistry; 1978 Apr; 17(8):1573-80. PubMed ID: 206281 [TBL] [Abstract][Full Text] [Related]
6. Chorismate mutase-prephenate dehydrogenase from Escherichia coli. Purification and properties of the bifunctional enzyme. Sampathkumar P; Morrison JF Biochim Biophys Acta; 1982 Apr; 702(2):204-11. PubMed ID: 7044424 [TBL] [Abstract][Full Text] [Related]
7. Chorismate mutase-prephenate dehydrogenase from Escherichia coli. 2. Evidence for two different active sites. Turnbull J; Morrison JF Biochemistry; 1990 Nov; 29(44):10255-61. PubMed ID: 2271653 [TBL] [Abstract][Full Text] [Related]
8. Chorismate mutase-prephenate dehydrogenase from Escherichia coli: positive cooperativity with substrates and inhibitors. Christopherson RI; Morrison JF Biochemistry; 1985 Feb; 24(5):1116-21. PubMed ID: 3913461 [TBL] [Abstract][Full Text] [Related]
9. Chorismate mutase-prephenate dehydrogenase from Escherichia coli: spatial relationship of the mutase and dehydrogenase sites. Christopherson RI; Heyde E; Morrison JF Biochemistry; 1983 Mar; 22(7):1650-6. PubMed ID: 6342665 [TBL] [Abstract][Full Text] [Related]
10. Partial inactivation of chorismate mutase-prephenate dehydrogenase from Escherichia coli in the presence of analogues of chorismate. Christopherson RI Int J Biochem Cell Biol; 1997 Apr; 29(4):589-94. PubMed ID: 9363636 [TBL] [Abstract][Full Text] [Related]
11. Mapping of chorismate mutase and prephenate dehydrogenase domains in the Escherichia coli T-protein. Chen S; Vincent S; Wilson DB; Ganem B Eur J Biochem; 2003 Feb; 270(4):757-63. PubMed ID: 12581215 [TBL] [Abstract][Full Text] [Related]
12. Regulation of Chorismate mutase-prephenate dehydratase and prephenate dehydrogenase from alcaligenes eutrophus. Friedrich CG; Friedrich B; Schlegel HG J Bacteriol; 1976 May; 126(2):723-32. PubMed ID: 4432 [TBL] [Abstract][Full Text] [Related]
13. Identification of active site residues of chorismate mutase-prephenate dehydrogenase from Escherichia coli. Christendat D; Turnbull J Biochemistry; 1996 Apr; 35(14):4468-79. PubMed ID: 8605196 [TBL] [Abstract][Full Text] [Related]
14. Identifying groups involved in the binding of prephenate to prephenate dehydrogenase from Escherichia coli. Christendat D; Turnbull JL Biochemistry; 1999 Apr; 38(15):4782-93. PubMed ID: 10200166 [TBL] [Abstract][Full Text] [Related]
15. Chorismate mutase-catalyzed reaction of (+/-)-chorismic acid. Hoare JH; Berchtold GA Biochem Biophys Res Commun; 1982 May; 106(2):660-2. PubMed ID: 7049179 [No Abstract] [Full Text] [Related]
16. The binding of tyrosine and NAD+ to chorismate mutase/prephenate dehydrogenase from Escherichia coli K12 and the effects of these ligands on the activity and self-association of the enzyme. Analysis in terms of a model. Hudson GS; Howlett GJ; Davidson BE J Biol Chem; 1983 Mar; 258(5):3114-20. PubMed ID: 6338013 [No Abstract] [Full Text] [Related]
17. Kinetic studies on chorismate mutase-prephenate dehydrogenase from Escherichia coli: models for the feedback inhibition of prephenate dehydrogenase by L-tyrosine. Turnbull J; Morrison JF; Cleland WW Biochemistry; 1991 Aug; 30(31):7783-8. PubMed ID: 1868056 [TBL] [Abstract][Full Text] [Related]
18. Secondary tritium isotope effects as probes of the enzymic and nonenzymic conversion of chorismate to prephenate. Addadi L; Jaffe EK; Knowles JR Biochemistry; 1983 Sep; 22(19):4494-501. PubMed ID: 6354259 [TBL] [Abstract][Full Text] [Related]
19. pH dependency of the reactions catalyzed by chorismate mutase-prephenate dehydrogenase from Escherichia coli. Turnbull J; Cleland WW; Morrison JF Biochemistry; 1991 Aug; 30(31):7777-82. PubMed ID: 1868055 [TBL] [Abstract][Full Text] [Related]
20. The prephenate dehydrogenase component of the bifunctional T-protein in enteric bacteria can utilize L-arogenate. Ahmad S; Jensen RA FEBS Lett; 1987 May; 216(1):133-9. PubMed ID: 3556217 [TBL] [Abstract][Full Text] [Related] [Next] [New Search]