title: Catalytic roles of lysines (K9, K27, K31) in the N-terminal domain in human adenylate kinase by random site-directed mutagenesis.
abstract: To elucidate lysine residues in the N-terminal domain of human cytosolic adenylate kinase (hAK1, EC 2.7.4.3), random site-directed mutagenesis of K9, K27, and K31 residues was performed, and six mutants were analyzed by steady-state kinetics. K9 residue may play an important role in catalysis by interacting with AMP2-. K27 and K31 residues appear to play a functional role in catalysis by interacting with MgATP2-. In human AK, the epsilon-amino group in the side chain of these lysine residues would be essential for phosphoryl transfer between MgATP2- and AMP2- during transition state.
authors.affiliation: Department of Hygiene, Miyazaki Medical College, Japan.
authors.forename: T
authors.initials: T
authors.lastname: Ayabe
authors.forename: S K
authors.initials: SK
authors.lastname: Park
authors.forename: H
authors.initials: H
authors.lastname: Takenaka
authors.forename: M
authors.initials: M
authors.lastname: Sumida
authors.forename: S
authors.initials: S
authors.lastname: Uesugi
authors.forename: O
authors.initials: O
authors.lastname: Takenaka
authors.forename: M
authors.initials: M
authors.lastname: Hamada
mesh_terms: D000249:Adenosine Monophosphate / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D000263:Adenylate Kinase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D001665:Binding Sites; D002384:Catalysis; D006801:Humans; D007700:Kinetics; D008239:Lysine / Q000378:metabolism*; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D011487:Protein Conformation
chemical_list: D000249:Adenosine Monophosphate; D000255:Adenosine Triphosphate; D000263:Adenylate Kinase; D008239:Lysine