Structural evidence for ammonia tunneling across the (beta alpha)(8) barrel of the imidazole glycerol phosphate synthase bienzyme complex. Export

@article{citeulike:3388343, abstract = {Since reactive ammonia is not available under physiological conditions, glutamine is used as a source for the incorporation of nitrogen in a number of metabolic pathway intermediates. The heterodimeric ImGP synthase that links histidine and purine biosynthesis belongs to the family of glutamine amidotransferases in which the glutaminase activity is coupled with a subsequent synthase activity specific for each member of the enzyme family. Its X-ray structure from the hyperthermophile Thermotoga maritima shows that the glutaminase subunit is associated with the N-terminal face of the (beta alpha)(8) barrel cyclase subunit. The complex reveals a putative tunnel for the transfer of ammonia over a distance of 25 A. Although ammonia tunneling has been reported for glutamine amidotransferases, the ImGP synthase has evolved a novel mechanism, which extends the known functional properties of the versatile (beta alpha)(8) barrel fold.}, author = {Douangamath, A. and Walker, M. and Beismann-Driemeyer, S. and Vega-Fernandez, M. C. and Sterner, R. and Wilmanns, M.}, citeulike-article-id = {3388343}, citeulike-linkout-0 = {http://view.ncbi.nlm.nih.gov/pubmed/11839304}, citeulike-linkout-1 = {http://www.hubmed.org/display.cgi?uids=11839304}, issn = {0969-2126}, journal = {Structure (London, England : 1993)}, keywords = {ammonia, channeling, channelingexample}, month = {February}, number = {2}, pages = {185--193}, posted-at = {2008-10-08 21:18:25}, priority = {2}, title = {Structural evidence for ammonia tunneling across the (beta alpha)(8) barrel of the imidazole glycerol phosphate synthase bienzyme complex.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/11839304}, volume = {10}, year = {2002} }

TY - JOUR ID - citeulike:3388343 L3 - citeulike-article-id:3388343 N2 - Since reactive ammonia is not available under physiological conditions, glutamine is used as a source for the incorporation of nitrogen in a number of metabolic pathway intermediates. The heterodimeric ImGP synthase that links histidine and purine biosynthesis belongs to the family of glutamine amidotransferases in which the glutaminase activity is coupled with a subsequent synthase activity specific for each member of the enzyme family. Its X-ray structure from the hyperthermophile Thermotoga maritima shows that the glutaminase subunit is associated with the N-terminal face of the (beta alpha)(8) barrel cyclase subunit. The complex reveals a putative tunnel for the transfer of ammonia over a distance of 25 A. Although ammonia tunneling has been reported for glutamine amidotransferases, the ImGP synthase has evolved a novel mechanism, which extends the known functional properties of the versatile (beta alpha)(8) barrel fold. IS - 2 JF - Structure (London, England : 1993) SN - 0969-2126 EP - 193 TI - Structural evidence for ammonia tunneling across the (beta alpha)(8) barrel of the imidazole glycerol phosphate synthase bienzyme complex. VL - 10 SP - 185 KW - ammonia KW - channeling KW - channelingexample AU - Douangamath, A AU - Walker, M AU - Beismann-Driemeyer, S AU - Vega-Fernandez, MC AU - Sterner, R AU - Wilmanns, M PY - 2002/02// UR - http://view.ncbi.nlm.nih.gov/pubmed/11839304 ER -