EPSP Synthase: The Design and Synthesis of Bisubstrate Inhibitors Incorporating Novel 3-Phosphate Mimics

Autor:	Kenneth J. Gruys, Michael J. Miller, C. Y. Han, Mark C. Walker, Dora M. Schnur, Ko-Chung Lin, Jose L. Font, Paul D. Pansegrau, Susan D. Corey, Diane Susan Braccolino, James A. Sikorski, Ajit S. Shah, D. G. Cleary, Joel E. Ream
Rok vydání:	1993
Předmět:	chemistry.chemical_classification ATP synthase biology Stereochemistry Organic Chemistry EPSP synthase Phosphate Biochemistry Catalysis Inorganic Chemistry chemistry.chemical_compound Enzyme Malonate chemistry biology.protein Methylene
Zdroj:	Phosphorus, Sulfur, and Silicon and the Related Elements. 76:115-118
ISSN:	1563-5325 1042-6507
Popis:	Novel aromatic bisubstrate inhibitors of the enzyme EPSP (5-enolpyruvoylshikimate-3-phosphate) synthase (EC 2.5.1.19) have been designed and synthesized as structural analogs of the single, catalytic intermediate 1 utilized by the enzyme. These aromatic inhibitors incorporate novel α-hydroxyphosphonates, malonate ethers and α-hydroxymalonates as replacements for the hydrolytically labile 3-phosphate group. These 3-phosphate mimics were much preferred to the corresponding methylene and vinylic phosphonates, malonates and phosphonomethyl ethers.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::4d6b80ad3beef91b4061e80035eee22b https://doi.org/10.1080/10426509308032372 Zobrazit plný text záznamu