title: How do kinases transfer phosphoryl groups?
abstract: Understanding how phosphoryl transfer is accomplished by kinases, a ubiquitous group of enzymes, is central to many biochemical processes. Qualitative analysis of the crystal structures of enzyme-substrate complexes of kinases reveals structural features of these enzymes important to phosphoryl transfer. Recently determined crystal structures which mimic the transition state complex have added new insight into the debate as to whether kinases use associative or dissociative mechanisms of catalysis.
authors.affiliation: Department of Biochemistry, University of Saskatchewan, Saskatoon, Saskatchewan, Canada.
authors.forename: A
authors.initials: A
authors.lastname: Matte
authors.forename: L W
authors.initials: LW
authors.lastname: Tari
authors.forename: L T
authors.initials: LT
authors.lastname: Delbaere
mesh_terms: D002384:Catalysis; D002412:Cations / Q000737:chemistry; D008958:Models, Molecular; D009711:Nucleotides / Q000737:chemistry; D010710:Phosphates / Q000378:metabolism*; D010770:Phosphotransferases / Q000737:chemistry*; D011485:Protein Binding; D011487:Protein Conformation
chemical_list: D002412:Cations; D009711:Nucleotides; D010710:Phosphates; D010770:Phosphotransferases