Article
The crystal structure of d-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeon Methanothermus fervidus in the presence of NADP(+) at 2.1 A resolution.
Journal of molecular biology - 24 Mar 2000
Charron C, Talfournier F, Isupov M N, Littlechild J A, Branlant G, Vitoux B, Aubry A
Abstract excerpt
The crystal structure of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from the archaeon Methanothermus fervidus has been solved in the holo form at 2.1 A resolution by molecular replacement. Unlike bacterial and eukaryotic homologous enzymes which are strictly NAD(+)-dependent, GAPDH from this organism exhibits a dual-cofactor specificity, with a marked preference for NADP(+) over NAD(+). The present...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.
