Format

Send to

Choose Destination
FEBS Lett. 2001 Apr 6;494(1-2):19-23.

Contribution of the DDDD motif of H. influenzae e (P4) to phosphomonoesterase activity and heme transport.

Author information

1
Department of Molecular Microbiology and Imunology, University of Missouri Medical School, Columbia, MO 65212, USA.

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.

PMID:
11297727
DOI:
10.1016/s0014-5793(01)02294-3
[Indexed for MEDLINE]
Free full text

Supplemental Content

Full text links

Icon for Wiley
Loading ...
Support Center