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EPSP synthase inhibitor design II. The importance of the 3-phosphate group for ligand binding at the shikimate-3-phosphate site & the identification of 3-malonate ethers as novel 3-phosphate mimics.

1993; Elsevier BV; Volume: 3; Issue: 7 Linguagem: Inglês

10.1016/s0960-894x(01)80425-x

1464-3405

Michael J. Miller, Karen S. Anderson, Diane S. Braccolino, Darryl G. Cleary, Kenneth J. Gruys, Chao Han, Ko‐Chung Lin, Paul D. Pansegrau, Joel E. Ream, R. Douglas Sammons, James A. Sikorski,

Plant biochemistry and biosynthesis

Studies using alternate substrates, inhibitor product mimics and new derivatives of 4,5-dideoxy-shikimate-3-phosphate (ddS3P) are reported which indicate that the 3-phosphate group contributes significantly to substrate and inhibitor recognition at the shikimate 3-phosphate (S3P) site and that 3-malonate ethers will function as suitable 3-phosphate replacements for substrate and inhibitor binding to the S3P site of this enzyme.