Betton J M, Jacob J P, Hofnung M, Broome-Smith J K
Département des Biotechnologies, Institut Pasteur-CNRS URA1444, Paris, France.
Nat Biotechnol. 1997 Nov;15(12):1276-9. doi: 10.1038/nbt1197-1276.
Hybrid proteins were generated by inserting the penicillin-hydrolyzing enzyme, TEM beta-lactamase (Bla), into the maltodextrin-binding protein (MalE). The inserted Bla was functionally accommodated by MalE when it was placed within permissive sites. The maltose binding and penicillinase activities of purified hybrids were indistinguishable from those of the wild-type MalE and Bla proteins. Moreover, these hybrids displayed an additional unexpected property: maltose stabilized the active site of inserted Bla.
