Member database | PROSITE patterns |
PROSITE patterns type | conserved site |
Short name | EPSP_SYNTHASE_2 |
Description
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase) (EC 2.5.1.19)
catalyzes the sixth step in the biosynthesis from chorismate of the aromatic
amino acids (the shikimate pathway) in bacteria (gene aroA), plants and fungi
(where it is part of a multifunctional enzyme which catalyzes five consecutive
steps in this pathway)
[1]. EPSP synthase has been extensively studied as it
is the target of the potent herbicide glyphosate which inhibits the enzyme.
The sequence of EPSP from various biological sources shows that the structure
of the enzyme has been well conserved throughout evolution. We selected two
conserved regions as signature patterns. The first pattern corresponds to a
region that is part of the active site and which is also important for the
resistance to glyphosate
[2]. The second pattern is located in the C-terminal
part of the protein and contains a conserved lysine which seems to be
important for the activity of the enzyme.
References
1.Structure and topological symmetry of the glyphosate target 5-enolpyruvylshikimate-3-phosphate synthase: a distinctive protein fold. Stallings WC, Abdel-Meguid SS, Lim LW, Shieh HS, Dayringer HE, Leimgruber NK, Stegeman RA, Anderson KS, Sikorski JA, Padgette SR, Kishore GM. Proc. Natl. Acad. Sci. U.S.A. 88, 5046-50, (1991). View articlePMID: 11607190
2.Site-directed mutagenesis of a conserved region of the 5-enolpyruvylshikimate-3-phosphate synthase active site. Padgette SR, Re DB, Gasser CS, Eichholtz DA, Frazier RB, Hironaka CM, Levine EB, Shah DM, Fraley RT, Kishore GM. J. Biol. Chem. 266, 22364-9, (1991). View articlePMID: 1939260