title: Mechanisms of enzyme catalysis from crystal structure analyses.
abstract: The enzyme families to which glutathione reductase and adenylate kinase belong show appreciably different structural behaviour during catalysis. While the electron transfer in glutathione reductase requires only small movements of a couple of non-hydrogen atoms, the transfer of a phosphoryl group in the nucleotide kinases involves major rearrangements with main chain displacements of up to 32 A. In both cases, the structural changes during a catalytic cycle have been derived from a number of separate X-ray crystallographic analyses.
authors.affiliation: Institut für Organische Chemie und Biochemie der Universität, Freiburg, Germany.
authors.forename: G E
authors.initials: GE
authors.lastname: Schulz
mesh_terms: D000263:Adenylate Kinase / Q000737:chemistry; D002384:Catalysis; D003461:Crystallography; D004798:Enzymes / Q000737:chemistry*; D005182:Flavin-Adenine Dinucleotide / Q000378:metabolism; D005980:Glutathione Reductase / Q000737:chemistry; D008956:Models, Chemical; D008958:Models, Molecular; D005810:Multigene Family; D009249:NADP / Q000378:metabolism; D010770:Phosphotransferases / Q000737:chemistry; D011487:Protein Conformation
chemical_list: D004798:Enzymes; D005182:Flavin-Adenine Dinucleotide; D009249:NADP; D005980:Glutathione Reductase; D010770:Phosphotransferases; D000263:Adenylate Kinase