Feedback inhibition of dihydrodipicolinate synthase enzymes by L-lysine. Export

@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}, citeulike-linkout-0 = {http://view.ncbi.nlm.nih.gov/pubmed/9165072}, citeulike-linkout-1 = {http://www.hubmed.org/display.cgi?uids=9165072}, 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 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. IS - 3-4 JF - Biol Chem SN - 1431-6730 AD - Max-Planck Institut für Biochemie, Martinsried, Germany. EP - 210 TI - Feedback inhibition of dihydrodipicolinate synthase enzymes by L-lysine. VL - 378 SP - 207 KW - metabolism KW - regulation AU - Blickling, S AU - Knäblein, J PY - 1997///r UR - http://view.ncbi.nlm.nih.gov/pubmed/9165072 ER -