title: The hepatitis B virus X protein is a potent AMP kinase.
abstract: The hepatitis B virus X-protein (HBx) has been expressed in Escherichia coli both as an unfused protein and with an N-terminal hexaHis-containing fusion sequence. Both forms of HBx, after purification, displayed a potent AMP kinase activity, in which HBx phosphorylates AMP to ADP, using ATP as the exclusive phosphate donor. We also found that HBx has previously unreported GTPase and GTP-ADP nucleoside diphosphate kinase activities.
authors.affiliation: Biomolecular Research Institute Ltd, Parkville, Victoria, Australia. Theod/mel.dbe.csiro.au
authors.forename: T A
authors.initials: TA
authors.lastname: Dopheide
authors.forename: A A
authors.initials: AA
authors.lastname: Azad
mesh_terms: D000263:Adenylate Kinase / Q000032:analysis*; D000595:Amino Acid Sequence; D020558:GTP Phosphohydrolases / Q000032:analysis; D008969:Molecular Sequence Data; D015534:Trans-Activators / Q000032:analysis* / Q000502:physiology; D054334:Viral Regulatory and Accessory Proteins
chemical_list: D015534:Trans-Activators; D054334:Viral Regulatory and Accessory Proteins; C057628:hepatitis B virus X protein; D000263:Adenylate Kinase; D020558:GTP Phosphohydrolases