title: Contribution of the DDDD motif of H. influenzae e (P4) to phosphomonoesterase activity and heme transport.
abstract: Haemophilus influenzae lipoprotein e (P4) is a member of the DDDD phosphohydrolase superfamily and mediates heme transport. Each of the aspartate residues of the signature motif is required for phosphomonoesterase activity, as none of the e (P4) single D mutants (D64A, D66A, D181N, and D185A) possessed detectable phosphomonoesterase activity. These results suggest that the signature motif is essential to the phosphomonoesterase activity of lipoprotein e (P4). When assessed for phosphomonoesterase-dependent heme transport activity in Escherichia coli hemA strains, plasmids containing D181N and D185A retained heme transport as indicated by aerobic growth while D64A and D66A did not. We conclude that phosphomonoesterase activity is not required for heme transport.
authors: Department of Molecular Microbiology and Imunology, University of Missouri Medical School, Columbia, MO 65212, USA.
authors: T J
authors: TJ
authors: Reilly
authors: B A
authors: BA
authors: Green
authors: G W
authors: GW
authors: Zlotnick
authors: A L
authors: AL
authors: Smith
mesh_terms: D001224:Aspartic Acid / Q000235:genetics / Q000378:metabolism; D001425:Bacterial Outer Membrane Proteins / Q000235:genetics / Q000378:metabolism*; D001665:Binding Sites; D001692:Biological Transport; D004926:Escherichia coli / Q000254:growth & development; D004950:Esterases; D006193:Haemophilus influenzae / Q000201:enzymology*; D006418:Heme / Q000378:metabolism*; D008074:Lipoproteins / Q000235:genetics / Q000378:metabolism*; D016297:Mutagenesis, Site-Directed; D010744:Phosphoric Monoester Hydrolases / Q000235:genetics / Q000378:metabolism*
chemical_list: D001425:Bacterial Outer Membrane Proteins; D008074:Lipoproteins; C098614:e(P4) lipoprotein, Haemophilus influenzae; D001224:Aspartic Acid; D006418:Heme; D004950:Esterases; D010744:Phosphoric Monoester Hydrolases