Feedback inhibition of dihydrodipicolinate synthase enzymes by L-lysine.

@article{citeulike:1713719, 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.}, address = {Max-Planck Institut f\"{u}r Biochemie, Martinsried, Germany.}, author = {Blickling, S. and Kn\"{a}blein, J. }, citeulike-article-id = {1713719}, issn = {1431-6730}, journal = {Biol Chem}, keywords = {metabolism, regulation}, number = {3-4}, pages = {207--210}, posted-at = {2007-10-01 06:00:58}, priority = {2}, title = {Feedback inhibition of dihydrodipicolinate synthase enzymes by L-lysine.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/9165072}, volume = {378}, year = {1997} }

TY - JOUR ID - citeulike:1713719 L3 - citeulike-article-id:1713719 TI - Feedback inhibition of dihydrodipicolinate synthase enzymes by L-lysine. JF - Biol Chem VL - 378 IS - 3-4 SP - 207 EP - 210 AD - Max-Planck Institut für Biochemie, Martinsried, Germany. SN - 1431-6730 N2 - 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. KW - metabolism KW - regulation AU - Blickling, S AU - Knäblein, J PY - 1997///r UR - http://view.ncbi.nlm.nih.gov/pubmed/9165072 ER -