Experimental evolution of enzyme temperature activity profile: selection in vivo and characterization of low-temperature-adapted mutants of Pyrococcus furiosus ornithine carbamoyltransferase.
We have obtained mutants of Pyrococcus furiosus ornithine carbamoyltransferase active at low temperatures by selecting for complementation of an appropriate yeast mutant after in vivo mutagenesis. The mutants were double ones, still complementing at 15 degrees C, a temperature already in the psychrophilic range. Their kinetic analysis is reported.
Roovers
M
M
Department of Microbiology, Flanders Interuniversity Institute for Biotechnology (VIB), B-1070 Brussels, Belgium.
Sanchez
R
R
Legrain
C
C
Glansdorff
N
N
D000220:Adaptation, Biological / Q000235:genetics*; D004795:Enzyme Stability; D019143:Evolution, Molecular; D005816:Genetic Complementation Test; D007700:Kinetics; D008958:Models, Molecular; D009154:Mutation; D009954:Ornithine Carbamoyltransferase / Q000235:genetics* / Q000378:metabolism; D020027:Pyrococcus furiosus / Q000201:enzymology* / Q000235:genetics; D011994:Recombinant Proteins / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000235:genetics; D013696:Temperature
D011994:Recombinant Proteins; D009954:Ornithine Carbamoyltransferase