Enzymatic synthesis of a ring-contracted analogue of 5-enolpyruvylshikimate-3-phosphate.
[reaction: see text] Three ring-contracted mimics of shikimate-3-phosphate, formed from the triols by shikimate kinase, were evaluated as substrates of the next enzyme in the pathway, EPSP synthase. The cyclopentylidene analogue (+)-2P was converted enzymatically to the enolpyruvyl derivative, thus demonstrating the second step of an artificial biosynthetic sequence.
An
Ming
M
Center for New Directions in Organic Synthesis, Department of Chemistry, University of California, Berkeley, California 94720-1460, USA.
Bartlett
Paul A
PA
D051229:3-Phosphoshikimate 1-Carboxyvinyltransferase; D019883:Alkyl and Aryl Transferases / Q000378:metabolism*; D002384:Catalysis; D003517:Cyclopentanes / Q000737:chemistry; D007536:Isomerism; D008956:Models, Chemical; D010728:Phosphoenolpyruvate / Q000378:metabolism; D017853:Phosphotransferases (Alcohol Group Acceptor) / Q000378:metabolism*; D012765:Shikimic Acid / Q000031:analogs & derivatives* / Q000138:chemical synthesis* / Q000378:metabolism
D003517:Cyclopentanes; C058070:5-enolpyruvoylshikimate-3-phosphate; D012765:Shikimic Acid; D010728:Phosphoenolpyruvate; D019883:Alkyl and Aryl Transferases; D051229:3-Phosphoshikimate 1-Carboxyvinyltransferase; D017853:Phosphotransferases (Alcohol Group Acceptor); C022642:shikimate kinase