title: Diverse proteins homologous to inositol monophosphatase.
abstract: Bovine inositol monophosphatase (IMP) and several homologous proteins were found to share two sequence motifs with bovine inositol polyphosphate 1-phosphatase (IPP). These motifs may correspond to binding sites within IMP and IPP for inositol phosphates or for lithium, since both substances are bound by these proteins. This suggests that the proteins homologous to IMP, which have diverse biological roles but whose function is not clear, may act by enhancing the synthesis or degradation of phosphorylated compounds.
authors.affiliation: Institute for Biomedical Computing, Washington University School of Medicine, St. Louis, MO 63110.
authors.forename: A F
authors.initials: AF
authors.lastname: Neuwald
authors.forename: J D
authors.initials: JD
authors.lastname: York
authors.forename: P W
authors.initials: PW
authors.lastname: Majerus
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001233:Aspergillus nidulans / Q000235:genetics; D002417:Cattle; D016208:Databases, Factual; D004926:Escherichia coli / Q000235:genetics; D008969:Molecular Sequence Data; D009492:Neurospora crassa / Q000235:genetics; D016366:Open Reading Frames; D010744:Phosphoric Monoester Hydrolases / Q000235:genetics*; D016961:Rhizobium leguminosarum / Q000235:genetics; D012689:Sequence Homology, Nucleic Acid
chemical_list: D010744:Phosphoric Monoester Hydrolases; C021822:myo-inositol-1 (or 4)-monophosphatase