135358-01-9Relevant academic research and scientific papers
Synthesis and evaluation of two new inhibitors of EPSP synthase
Pansegrau, Paul D.,Anderson, Karen S.,Widlanski, Theodore,Ream, Joel E.,Douglas Sammons,Sikorski, James A.,Knowles, Jeremy R.
, p. 2589 - 2592 (2007/10/02)
The enzyme EPSP synthase, EPSPS, (EC 2.5.1.19) catalyzes an unusual transfer reaction of the enolpyruvoyl moiety from phosphoenol pyruvate (2, PEP) regiospecifically to the 5-OH of shikimate 3-phosphate (1, S3P) to form 5-enol-pyruvoylshikimate 3-phosphate (3, EPSP). Two new inhibitors, (4, and 5) were prepared to probe the S3P binding site.
Structural Requirements for Catalysis by Chorismate Mutase
Pawlak, John L.,Padykula, Robert E.,Kronis, John D.,Aleksejczyk, Robert A.,Berchtold, Glenn A.
, p. 3374 - 3381 (2007/10/02)
The structural requirements for mutase-catalyzed Claisen rearrangement by chorismate mutase-prephenate dehydrogenase from Escherichia coli have been established.The chorismate analogue lacking the carboxyl group at C1 (5) was not a substrate for chorismate mutase.The methyl ether of chorismate was a good substrate for chorismate mutase (kcat/kuncat = 2.0*1E4).The half-lives for Claisen rearrangement and aromatization of 4-deshydroxychorismate (19) in D2O at 30 deg C, pD 7.2, were 3.5 and 8 min, respectively.In the presence of large amounts of enzyme,it was demonstrated that the Claisen rearrangement of enantiomerically pure 19 was accelerated at least 100-fold by chorismate mutase.Data available from other studies have demonstrated that ester 3 is not a substrate for chorismate mutase, and the kcat/kuncat for dihydrochorismate analogue 4 is similar to that for chorismate.These results establish that the only functional groups required on the allyl vinyl ether moiety of chorismate for mutase-catalyzed rearrangement are the two carboxylate groups.
