An artificial bifunctional enzyme, gamma-glutamyl kinase/gamma-glutamy
l phosphate reductase, was obtained by fusing the Escherichia coil gen
es proA and proB. The proB gene was fused to the 5'-end of the proA ge
ne with a linker encoding five amino acids. When expressed in E. coil
enhanced intracellular concentrations of proline were observed. At 0.6
M NaCl the growth rates for the strain carrying the fusion enzyme and
a control harbouring a plasmid encoding the wild-type enzymes were 32
0 and 530 min, respectively.