title: Chemistry and biology of deoxy-myo-inositol phosphates: stereospecificity of substrate interactions within an archaeal and a bacterial IMPase.
abstract: Six enantiomerically pure myo-inositol-monophosphates, including four deoxygenated analogues, have been synthesized by employing catalytic asymmetric phosphorylation methodology. These compounds were then evaluated as substrates for the direct interrogation of the stereospecificity of enzyme-substrate interactions with two inositol-monophosphatases (IMPases), one of which (from Archaeoglobus fulgidus) is characterized by an X-ray crystal structure with its substrate (d-I-1P) bound. The kinetic results lead to the finding that certain hydroxyl group contacts are actually destabilizing, while others have little effect. These new probes also allow a prediction of the active site binding mode of the substrate for the Escherichia coli IMPase for which no crystal structure exists.
authors.affiliation: Department of Chemistry, Merkert Chemistry Center, Boston College, Chestnut Hill, MA 02467-3860, USA.
authors.forename: Adam J
authors.initials: AJ
authors.lastname: Morgan
authors.forename: Yangling Karen
authors.initials: YK
authors.lastname: Wang
authors.forename: Mary F
authors.initials: MF
authors.lastname: Roberts
authors.forename: Scott J
authors.initials: SJ
authors.lastname: Miller
mesh_terms: D015720:5'-Nucleotidase / Q000737:chemistry / Q000378:metabolism*; D019843:Archaeal Proteins / Q000737:chemistry / Q000378:metabolism*; D019611:Archaeoglobus fulgidus / Q000201:enzymology*; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D007295:Inositol Phosphates / Q000737:chemistry / Q000378:metabolism*; D007700:Kinetics; D010766:Phosphorylation; D013237:Stereoisomerism; D013379:Substrate Specificity
chemical_list: D019843:Archaeal Proteins; D001426:Bacterial Proteins; D007295:Inositol Phosphates; D015720:5'-Nucleotidase