Comparative kinetic study of tryptophan synthase from Salmonella typhimurium and Photobacterium profundum
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Tryptophan Synthase is a pyridoxal 5’-phosphate dependent enzyme that catalyzes the reaction of indole-3-glycerol phosphate and L-serine to form L-tryptophan in bacteria, plants, and fungi. While the effects of different factors such as temperature, pressure and cations on catalytic properties of tryptophan synthase extracted from Salmonella typhimurium (StTrpSyn) have been extensively investigated, our interest has been turned to Photobacterium profundum, living in a deep sea environment, whose tryptophan synthase (PpTrpSyn) is predicted to have different properties. We have studied the relationships between the enzyme activity of PpTrpSyn and factors of temperature and pressure in the presence of different cations (Na+, K+) separately and compared to these of StTrpSyn. Some thermodynamic parameters have been determined. It turned out that the catalytic α β conformational change within the enzyme maybe be tuned to the environmental conditions by changes in the amino acids at the subunit interface.