title: Feedback inhibition of dihydrodipicolinate synthase enzymes by L-lysine.
abstract: Dihydrodipicolinate synthase (DHDPS) is the first enzyme unique to the lysine biosynthetic pathway and is feedback regulated by L-lysine in plants and some bacteria. The allosteric binding site has been localized by X-ray crystallography and is in agreement with reported mutations of plant DHDPS enzymes, which confer insensitivity to feedback inhibition. Three possible elements of the mechanism of lysine inhibition are discussed.
authors.affiliation: Max-Planck Institut für Biochemie, Martinsried, Germany.
authors.forename: S
authors.initials: S
authors.lastname: Blickling
authors.forename: J
authors.initials: J
authors.lastname: Knäblein
mesh_terms: D000595:Amino Acid Sequence; D001419:Bacteria / Q000201:enzymology; D005246:Feedback / Q000502:physiology; D006836:Hydro-Lyases / Q000037:antagonists & inhibitors* / Q000378:metabolism; D007527:Isoenzymes / Q000037:antagonists & inhibitors* / Q000378:metabolism; D008239:Lysine / Q000378:metabolism / Q000494:pharmacology / Q000502:physiology*; D008969:Molecular Sequence Data; D010944:Plants / Q000201:enzymology
chemical_list: D007527:Isoenzymes; D006836:Hydro-Lyases; C020040:4-hydroxy-tetrahydrodipicolinate synthase; D008239:Lysine