Premium
Construction and characterization of a recombinant tripartite enzyme, galactose dehydrogenase/β‐galactosidase/galactokinase
Author(s) -
Ljungcrantz Peter,
Bülow Leif,
Mosbach Klaus
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)81446-u
Subject(s) - galactokinase , galactose , recombinant dna , enzyme , biochemistry , chemistry , dehydrogenase , escherichia coli , gene
The in‐frame gene fusion between 3 enzymes, galactose dehydrogenase, β‐galactosidase and galactokinase, is described. The purified artificial tripartite enzyme displayed all three enzymic activities. Two major forms of the hybrid protein were found, consisting of 4 and 8 subunits respectively, but other forms could also be identified. Each subunit was made up of one monomer each of galactose dehydrogenase, β‐galactosidase and galactokinase. Proximity effects exhibited by the hybrid enzyme could be demonstrated using [ 14 C ]galactose as a reporter molecule.