A comparative study of the thermal inactivation of the isolated and associated domains within the beta 2 subunit of Escherichia coli tryptophan synthetase. Evidence for strong interdomain interactions.
作者： C.R. Zetina , M.E. Goldberg
DOI: 10.1016/S0021-9258(19)85676-4
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摘要: Abstract The irreversible inactivation by heat of the F1 and F2 regions beta 2 subunit Escherichia coli tryptophan synthetase (L-serine hydrolyase (adding indole) EC 4.2.1.20) has been studied. By comparing kinetics fragments, either isolated proteolysis or associated within protein, it is shown that fragment protected considerably against its interactions with complementary fragment. An important stabilization protein conformation coenzyme, pyridoxal 5'-phosphate, also observed. using a hybrid enzyme preparation, single 5'-phosphate molecule two protomers likely to be caused strengthening interdomain upon binding coenzyme. These results point strong energetic coupling between domains chain.
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