Channeling of substrates and intermediates in enzyme-catalyzed reactions. Export

@article{citeulike:3870616, abstract = {The three-dimensional structures of tryptophan synthase, carbamoyl phosphate synthetase, glutamine phosphoribosylpyrophosphate amidotransferase, and asparagine synthetase have revealed the relative locations of multiple active sites within these proteins. In all of these polyfunctional enzymes, a product formed from the catalytic reaction at one active site is a substrate for an enzymatic reaction at a distal active site. Reaction intermediates are translocated from one active site to the next through the participation of an intermolecular tunnel. The tunnel in tryptophan synthase is approximately 25 A in length, whereas the tunnel in carbamoyl phosphate synthetase is nearly 100 A long. Kinetic studies have demonstrated that the individual reactions are coordinated through allosteric coupling of one active site with another. The participation of these molecular tunnels is thought to protect reactive intermediates from coming in contact with the external medium.}, author = {Huang, X. and Holden, H. M. and Raushel, F. M.}, citeulike-article-id = {3870616}, citeulike-linkout-0 = {http://dx.doi.org/10.1146/annurev.biochem.70.1.149}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/11395405}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=11395405}, doi = {10.1146/annurev.biochem.70.1.149}, issn = {0066-4154}, journal = {Annual review of biochemistry}, keywords = {channeling, metabolic, review}, pages = {149--180}, posted-at = {2009-01-09 04:44:03}, priority = {2}, title = {Channeling of substrates and intermediates in enzyme-catalyzed reactions.}, url = {http://dx.doi.org/10.1146/annurev.biochem.70.1.149}, volume = {70}, year = {2001} }

TY - JOUR ID - citeulike:3870616 L3 - citeulike-article-id:3870616 N2 - The three-dimensional structures of tryptophan synthase, carbamoyl phosphate synthetase, glutamine phosphoribosylpyrophosphate amidotransferase, and asparagine synthetase have revealed the relative locations of multiple active sites within these proteins. In all of these polyfunctional enzymes, a product formed from the catalytic reaction at one active site is a substrate for an enzymatic reaction at a distal active site. Reaction intermediates are translocated from one active site to the next through the participation of an intermolecular tunnel. The tunnel in tryptophan synthase is approximately 25 A in length, whereas the tunnel in carbamoyl phosphate synthetase is nearly 100 A long. Kinetic studies have demonstrated that the individual reactions are coordinated through allosteric coupling of one active site with another. The participation of these molecular tunnels is thought to protect reactive intermediates from coming in contact with the external medium. JF - Annual review of biochemistry SN - 0066-4154 EP - 180 TI - Channeling of substrates and intermediates in enzyme-catalyzed reactions. VL - 70 SP - 149 KW - channeling KW - metabolic KW - review AU - Huang, X AU - Holden, HM AU - Raushel, FM PY - 2001/// UR - http://dx.doi.org/10.1146/annurev.biochem.70.1.149 ER -